EC 1.1.1.1     
Accepted name: alcohol dehydrogenase
Reaction: (1) a primary alcohol + NAD+ = an aldehyde + NADH + H+
(2) a secondary alcohol + NAD+ = a ketone + NADH + H+
Other name(s): aldehyde reductase; ADH; alcohol dehydrogenase (NAD); aliphatic alcohol dehydrogenase; ethanol dehydrogenase; NAD-dependent alcohol dehydrogenase; NAD-specific aromatic alcohol dehydrogenase; NADH-alcohol dehydrogenase; NADH-aldehyde dehydrogenase; primary alcohol dehydrogenase; yeast alcohol dehydrogenase
Systematic name: alcohol:NAD+ oxidoreductase
Comments: A zinc protein. Acts on primary or secondary alcohols or hemi-acetals with very broad specificity; however the enzyme oxidizes methanol much more poorly than ethanol. The animal, but not the yeast, enzyme acts also on cyclic secondary alcohols.
References:
1.  Brändén, G.-I., Jörnvall, H., Eklund, H. and Furugren, B. Alcohol dehydrogenase. In: Boyer, P.D. (Ed.), The Enzymes, 3rd edn, vol. 11, Academic Press, New York, 1975, pp. 103–190.
2.  Jörnvall, H. Differences between alcohol dehydrogenases. Structural properties and evolutionary aspects. Eur. J. Biochem. 72 (1977) 443–452. [PMID: 320001]
3.  Negelein, E. and Wulff, H.-J. Diphosphopyridinproteid ackohol, acetaldehyd. Biochem. Z. 293 (1937) 351–389.
4.  Sund, H. and Theorell, H. Alcohol dehydrogenase. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Ed.), The Enzymes, 2nd edn, vol. 7, Academic Press, New York, 1963, pp. 25–83.
5.  Theorell, H. Kinetics and equilibria in the liver alcohol dehydrogenase system. Adv. Enzymol. Relat. Subj. Biochem. 20 (1958) 31–49. [PMID: 13605979]
[EC 1.1.1.1 created 1961, modified 2011]
 
 
EC 1.1.1.2     
Accepted name: alcohol dehydrogenase (NADP+)
Reaction: an alcohol + NADP+ = an aldehyde + NADPH + H+
Other name(s): aldehyde reductase (NADPH2); NADP-alcohol dehydrogenase; NADP+-aldehyde reductase; NADP+-dependent aldehyde reductase; NADPH-aldehyde reductase; NADPH-dependent aldehyde reductase; nonspecific succinic semialdehyde reductase; ALR 1; low-Km aldehyde reductase; high-Km aldehyde reductase; alcohol dehydrogenase (NADP)
Systematic name: alcohol:NADP+ oxidoreductase
Comments: A zinc protein. Some members of this group oxidize only primary alcohols; others act also on secondary alcohols. May be identical with EC 1.1.1.19 (L-glucuronate reductase), EC 1.1.1.33 [mevaldate reductase (NADPH)] and EC 1.1.1.55 [lactaldehyde reductase (NADPH)]. Re-specific with respect to NADPH.
References:
1.  Bosron, W.F. and Prairie, R.L. Triphosphopyridine nucleotide-linked aldehyde reductase. I. Purification and properties of the enzyme from pig kidney cortex. J. Biol. Chem. 247 (1972) 4480–4485. [PMID: 4402936]
2.  DeMoss, R. Triphosphopyridine nucleotide-specific ethanol dehydrogenase from Leuconostoc mesenteroides. Bacteriol. Proc. (1953) 81.
3.  Reeves, R.E., Montalvo, F.E. and Lushbaugh, T.S. Nicotinamide-adenine dinucleotide phosphate-dependent alcohol dehydrogenase. Enzyme from Entamoeba histolytica and some enzyme inhibitors. Int. J. Biochem. 2 (1971) 55–64.
4.  Tabakoff, B. and Erwin, V.G. Purification and characterization of a reduced nicotinamide adenine dinucleotide phosphate-linked aldehyde reductase from brain. J. Biol. Chem. 245 (1970) 3263–3268. [PMID: 4393513]
[EC 1.1.1.2 created 1961]
 
 
EC 1.1.1.3     
Accepted name: homoserine dehydrogenase
Reaction: L-homoserine + NAD(P)+ = L-aspartate 4-semialdehyde + NAD(P)H + H+
Other name(s): HSDH; HSD
Systematic name: L-homoserine:NAD(P)+ oxidoreductase
Comments: The yeast enzyme acts most rapidly with NAD+; the Neurospora enzyme with NADP+. The enzyme from Escherichia coli is a multi-functional protein, which also catalyses the reaction of EC 2.7.2.4 (aspartate kinase).
References:
1.  Black, S. and Wright, N.G. Homoserine dehydrogenase. J. Biol. Chem. 213 (1955) 51–60. [PMID: 14353905]
2.  Starnes, W.L., Munk, P., Maul, S.B., Cunningham, G.N., Cox, D.J. and Shive, W. Threonine-sensitive aspartokinase-homoserine dehydrogenase complex, amino acid composition, molecular weight, and subunit composition of the complex. Biochemistry 11 (1972) 677–687. [PMID: 4551091]
3.  Véron, M., Falcoz-Kelly, F. and Cohen, G.N. The threonine-sensitive homoserine dehydrogenase and aspartokinase activities of Escherichia coli K12. The two catalytic activities are carried by two independent regions of the polypeptide chain. Eur. J. Biochem. 28 (1972) 520–527. [PMID: 4562990]
[EC 1.1.1.3 created 1961, modified 1976]
 
 
EC 1.1.1.4     
Accepted name: (R,R)-butanediol dehydrogenase
Reaction: (R,R)-butane-2,3-diol + NAD+ = (R)-acetoin + NADH + H+
Other name(s): butyleneglycol dehydrogenase; D-butanediol dehydrogenase; D-(–)-butanediol dehydrogenase; butylene glycol dehydrogenase; diacetyl (acetoin) reductase; D-aminopropanol dehydrogenase; 1-amino-2-propanol dehydrogenase; 2,3-butanediol dehydrogenase; D-1-amino-2-propanol dehydrogenase; (R)-diacetyl reductase; (R)-2,3-butanediol dehydrogenase; D-1-amino-2-propanol:NAD+ oxidoreductase; 1-amino-2-propanol oxidoreductase; aminopropanol oxidoreductase
Systematic name: (R,R)-butane-2,3-diol:NAD+ oxidoreductase
Comments: Also converts diacetyl into acetoin with NADH as reductant.
References:
1.  Strecker, H.J. and Harary, I. Bacterial butylene glycol dehydrogenase and diacetyl reductase. J. Biol. Chem. 211 (1954) 263–270. [PMID: 13211662]
2.  Taylor, M.B. and Juni, E. Stereoisomeric specificities of 2,3-butanediol dehydrogenase. Biochim. Biophys. Acta 39 (1960) 448–457. [PMID: 13837186]
[EC 1.1.1.4 created 1961 (EC 1.1.1.74 created 1972, incorporated 1976)]
 
 
EC 1.1.1.5      
Transferred entry: acetoin dehydrogenase. Now EC 1.1.1.303, diacetyl reductase [(R)-acetoin forming] and EC 1.1.1.304, diacetyl reductase [(S)-acetoin forming]
[EC 1.1.1.5 created 1961, modified 1976, deleted 2010]
 
 
EC 1.1.1.6     
Accepted name: glycerol dehydrogenase
Reaction: glycerol + NAD+ = glycerone + NADH + H+
Other name(s): glycerin dehydrogenase; NAD-linked glycerol dehydrogenase
Systematic name: glycerol:NAD+ 2-oxidoreductase
Comments: Also acts on propane-1,2-diol.
References:
1.  Asnis, R.E. and Brodie, A.F. A glycerol dehydrogenase from Escherichia coli. J. Biol. Chem. 203 (1953) 153–159. [PMID: 13069498]
2.  Burton, R.M. and Kaplan, N.O. A DPN specific glycerol dehydrogenase from Aerobacter aerogenes. J. Am. Chem. Soc. 75 (1953) 1005–1007.
3.  Lin, E.C.C. and Magasanik, B. The activation of glycerol dehydrogenase from Aerobacter aerogenes by monovalent cations. J. Biol. Chem. 235 (1960) 1820–1823. [PMID: 14417009]
[EC 1.1.1.6 created 1961]
 
 
EC 1.1.1.7     
Accepted name: propanediol-phosphate dehydrogenase
Reaction: propane-1,2-diol 1-phosphate + NAD+ = hydroxyacetone phosphate + NADH + H+
Other name(s): PDP dehydrogenase; 1,2-propanediol-1-phosphate:NAD+ oxidoreductase; propanediol phosphate dehydrogenase
Systematic name: propane-1,2-diol-1-phosphate:NAD+ oxidoreductase
References:
1.  Sellinger, O.Z. and Miller, O.N. The metabolism of acetol phosphate. II. 1,2-Propanediol-1-phosphate dehydrogenase. J. Biol. Chem. 234 (1959) 1641–1646. [PMID: 13672935]
[EC 1.1.1.7 created 1961]
 
 
EC 1.1.1.8     
Accepted name: glycerol-3-phosphate dehydrogenase (NAD+)
Reaction: sn-glycerol 3-phosphate + NAD+ = glycerone phosphate + NADH + H+
Glossary: glycerone phosphate = dihydroxyacetone phosphate = 3-hydroxy-2-oxopropyl phosphate
Other name(s): α-glycerol phosphate dehydrogenase (NAD+); α-glycerophosphate dehydrogenase (NAD+); glycerol 1-phosphate dehydrogenase; glycerol phosphate dehydrogenase (NAD+); glycerophosphate dehydrogenase (NAD+); hydroglycerophosphate dehydrogenase; L-α-glycerol phosphate dehydrogenase; L-α-glycerophosphate dehydrogenase; L-glycerol phosphate dehydrogenase; L-glycerophosphate dehydrogenase (ambiguous); NAD+-α-glycerophosphate dehydrogenase; NAD+-dependent glycerol phosphate dehydrogenase; NAD+-dependent glycerol-3-phosphate dehydrogenase; NAD+-L-glycerol-3-phosphate dehydrogenase; NAD+-linked glycerol 3-phosphate dehydrogenase; NADH-dihydroxyacetone phosphate reductase; glycerol-3-phosphate dehydrogenase (NAD+); L-glycerol-3-phosphate dehydrogenase (ambiguous)
Systematic name: sn-glycerol-3-phosphate:NAD+ 2-oxidoreductase
Comments: Also acts on propane-1,2-diol phosphate and glycerone sulfate (but with a much lower affinity).
References:
1.  Baranowski, T. α-Glycerophosphate dehydrogenase. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Ed.), The Enzymes, 2nd edn, vol. 7, Academic Press, New York, 1963, pp. 85–96.
2.  Brosemer, R.W. and Kuhn, R.W. Comparative structural properties of honeybee and rabbit α-glycerophosphate dehydrogenases. Biochemistry 8 (1969) 2095–2105. [PMID: 4307630]
3.  O'Brien, S.J. and MacIntyre, R.J. The α-glycerophosphate cycle in Drosophila melanogaster. I. Biochemical and developmental aspects. Biochem. Genet. 7 (1972) 141–161. [PMID: 4340553]
4.  Warkentin, K.L. and Fondy, T.P. Isolation and characterization of cytoplasmic L-glycerol-3-phosphate dehydrogenase from rabbit-renal-adipose tissue and its comparison with the skeletal-muscle enzyme. Eur. J. Biochem. 36 (1973) 97–109. [PMID: 4200180]
5.  Albertyn, J., van Tonder, A. and Prior, B.A. Purification and characterization of glycerol-3-phosphate dehydrogenase of Saccharomyces cerevisiae. FEBS Lett. 308 (1992) 130–132. [PMID: 1499720]
6.  Koekemoer, T.C., Litthauer, D. and Oelofsen, W. Isolation and characterization of adipose tissue glycerol-3-phosphate dehydrogenase. Int. J. Biochem. Cell Biol. 27 (1995) 625–632. [PMID: 7671141]
[EC 1.1.1.8 created 1961, modified 2005]
 
 
EC 1.1.1.9     
Accepted name: D-xylulose reductase
Reaction: xylitol + NAD+ = D-xylulose + NADH + H+
Other name(s): NAD+-dependent xylitol dehydrogenase; xylitol dehydrogenase (ambiguous); erythritol dehydrogenase; 2,3-cis-polyol(DPN) dehydrogenase (C3-5); pentitol-DPN dehydrogenase (ambiguous); xylitol-2-dehydrogenase
Systematic name: xylitol:NAD+ 2-oxidoreductase (D-xylulose-forming)
Comments: Also acts as an L-erythrulose reductase.
References:
1.  Chiang, C. and Knight, S.G. A new pathway of pentose metabolism. Biochem. Biophys. Res. Commun. 3 (1960) 554–559. [PMID: 13692998]
2.  Hickman, J. and Ashwell, G. A sensitive and stereospecific enzymatic assay for xylulose. J. Biol. Chem. 234 (1959) 758–761. [PMID: 13654257]
3.  Jakoby, W.B. and Fredericks, J. Erythritol dehydrogenase from Aerobacter aerogenes. Biochim. Biophys. Acta 48 (1961) 26–32. [PMID: 13789254]
[EC 1.1.1.9 created 1961]
 
 
EC 1.1.1.10     
Accepted name: L-xylulose reductase
Reaction: xylitol + NADP+ = L-xylulose + NADPH + H+
Other name(s): xylitol dehydrogenase (ambiguous)
Systematic name: xylitol:NADP+ 4-oxidoreductase (L-xylulose-forming)
References:
1.  Doten, R.C. and Mortlock, R.P. Characterization of xylitol-utilizing mutants of Erwinia uredovora. J. Bacteriol. 161 (1985) 529–533. [PMID: 2981816]
2.  Hickman, J. and Ashwell, G. A sensitive and stereospecific enzymatic assay for xylulose. J. Biol. Chem. 234 (1959) 758–761. [PMID: 13654257]
3.  Hollmann, S. and Touster, O. The L-xylulose-xylitol enzyme and other polyol dehydrogenases of guinea pig liver mitochondria. J. Biol. Chem. 225 (1957) 87–102. [PMID: 13416220]
4.  Touster, O., Reynolds, V.H. and Hutcheson, R.M. The reduction of L-xylulose to xylitol by guinea pig liver mitochondria. J. Biol. Chem. 221 (1956) 697–709. [PMID: 13357463]
[EC 1.1.1.10 created 1961]
 
 
EC 1.1.1.11     
Accepted name: D-arabinitol 4-dehydrogenase
Reaction: D-arabinitol + NAD+ = D-xylulose + NADH + H+
Other name(s): D-arabitol dehydrogenase; arabitol dehydrogenase
Systematic name: D-arabinitol:NAD+ 4-oxidoreductase
References:
1.  Lin, E.C.C. An inducible D-arabitol dehydrogenase from Aerobacter aerogenes. J. Biol. Chem. 236 (1961) 31–36. [PMID: 13762204]
2.  Wood, W.A., McDonough, M.J. and Jacobs, L.B. Ribitol and D-arabitol utilization by Aerobacter aerogenes. J. Biol. Chem. 236 (1961) 2190–2195. [PMID: 13786517]
[EC 1.1.1.11 created 1961]
 
 
EC 1.1.1.12     
Accepted name: L-arabinitol 4-dehydrogenase
Reaction: L-arabinitol + NAD+ = L-xylulose + NADH + H+
Other name(s): pentitol-DPN dehydrogenase (ambiguous); L-arabitol dehydrogenase
Systematic name: L-arabinitol:NAD+ 4-oxidoreductase (L-xylulose-forming)
References:
1.  Chiang, C. and Knight, S.G. A new pathway of pentose metabolism. Biochem. Biophys. Res. Commun. 3 (1960) 554–559. [PMID: 13692998]
2.  Chiang, C. and Knight, S.G. L-Arabinose metabolism by cell-free extracts of Penicillium chrysogenum. Biochim. Biophys. Acta 46 (1961) 271–278. [PMID: 13692999]
[EC 1.1.1.12 created 1961]
 
 
EC 1.1.1.13     
Accepted name: L-arabinitol 2-dehydrogenase
Reaction: L-arabinitol + NAD+ = L-ribulose + NADH + H+
Other name(s): L-arabinitol dehydrogenase (ribulose-forming); L-arabinitol (ribulose-forming) dehydrogenase
Systematic name: L-arabinitol:NAD+ 2-oxidoreductase (L-ribulose-forming)
References:
1.  Chiang, C. and Knight, S.G. L-Arabinose metabolism by cell-free extracts of Penicillium chrysogenum. Biochim. Biophys. Acta 46 (1961) 271–278. [PMID: 13692999]
[EC 1.1.1.13 created 1961]
 
 
EC 1.1.1.14     
Accepted name: L-iditol 2-dehydrogenase
Reaction: L-iditol + NAD+ = L-sorbose + NADH + H+
Other name(s): polyol dehydrogenase; sorbitol dehydrogenase; L-iditol:NAD+ 5-oxidoreductase; L-iditol (sorbitol) dehydrogenase; glucitol dehydrogenase; L-iditol:NAD+ oxidoreductase; NAD+-dependent sorbitol dehydrogenase; NAD+-sorbitol dehydrogenase
Systematic name: L-iditol:NAD+ 2-oxidoreductase
Comments: This enzyme is widely distributed and has been described in archaea, bacteria, yeast, plants and animals. It acts on a number of sugar alcohols, including (but not limited to) L-iditol, D-glucitol, D-xylitol, and D-galactitol. Enzymes from different organisms or tissues display different substrate specificity. The enzyme is specific to NAD+ and can not use NADP+.
References:
1.  Bailey, J.P., Renz, C. and McGuinness, E.T. Sorbitol dehydrogenase from horse liver: purification, characterization and comparative properties. Comp. Biochem. Physiol. 69B (1981) 909–914.
2.  Burnell, J.N. and Holmes, R.S. Purification and properties of sorbitol dehydrogenase from mouse liver. Int. J. Biochem. 15 (1983) 507–511. [PMID: 6852349]
3.  Leissing, N. and McGuinness, E.T. Rapid affinity purification and properties of rat liver sorbitol dehydrogenase. Biochim. Biophys. Acta 524 (1978) 254–261. [PMID: 667078]
4.  Negm, F.B. and Loescher, W.H. Detection and characterization of sorbitol dehydrogenase from apple callus tissue. Plant Physiol. 64 (1979) 69–73. [PMID: 16660917]
5.  O'Brien, M.M., Schofield, P.J. and Edwards, M.R. Polyol-pathway enzymes of human brain. Partial purification and properties of sorbitol dehydrogenase. Biochem. J. 211 (1983) 81–90. [PMID: 6870831]
6.  Ng, K., Ye, R., Wu, X.C. and Wong, S.L. Sorbitol dehydrogenase from Bacillus subtilis. Purification, characterization, and gene cloning. J. Biol. Chem. 267 (1992) 24989–24994. [PMID: 1460002]
[EC 1.1.1.14 created 1961, modified 2011]
 
 
EC 1.1.1.15     
Accepted name: D-iditol 2-dehydrogenase
Reaction: D-iditol + NAD+ = D-sorbose + NADH + H+
Other name(s): D-sorbitol dehydrogenase
Systematic name: D-iditol:NAD+ 2-oxidoreductase
Comments: Also converts xylitol into L-xylulose and L-glucitol into L-fructose.
References:
1.  Shaw, D.R.D. Polyol dehydrogenases. 3. Galactitol dehydrogenase and D-iditol dehydrogenase. Biochem. J. 64 (1956) 394–405. [PMID: 13373783]
[EC 1.1.1.15 created 1961]
 
 
EC 1.1.1.16     
Accepted name: galactitol 2-dehydrogenase
Reaction: galactitol + NAD+ = D-tagatose + NADH + H+
Other name(s): dulcitol dehydrogenase; AtuSorbD (gene name); galactitol:NAD+ 2-oxidoreductase
Systematic name: galactitol:NAD+ 2-oxidoreductase (D-tagatose-forming)
Comments: Also converts other alditols containing an L-threo-configuration adjacent to a primary alcohol group into the corresponding sugars. The enzyme from Agrobacterium fabrum C58 is part of D-altritol and galactitol degradation pathways.
References:
1.  Shaw, D.R.D. Polyol dehydrogenases. 3. Galactitol dehydrogenase and D-iditol dehydrogenase. Biochem. J. 64 (1956) 394–405. [PMID: 13373783]
2.  Wichelecki, D.J., Vetting, M.W., Chou, L., Al-Obaidi, N., Bouvier, J.T., Almo, S.C. and Gerlt, J.A. ATP-binding cassette (ABC) transport system solute-binding protein-guided identification of novel D-altritol and galactitol catabolic pathways in Agrobacterium tumefaciens C58. J. Biol. Chem. 290 (2015) 28963–28976. [PMID: 26472925]
[EC 1.1.1.16 created 1961]
 
 
EC 1.1.1.17     
Accepted name: mannitol-1-phosphate 5-dehydrogenase
Reaction: D-mannitol 1-phosphate + NAD+ = D-fructose 6-phosphate + NADH + H+
Other name(s): hexose reductase; mannitol 1-phosphate dehydrogenase; D-mannitol-1-phosphate dehydrogenase; fructose 6-phosphate reductase
Systematic name: D-mannitol-1-phosphate:NAD+ 5-oxidoreductase
References:
1.  Marmur, J. and Hotchkiss, R.D. Mannitol metabolism, a transferable property of pneumococcus. J. Biol. Chem. 214 (1955) 383–396. [PMID: 14367396]
2.  Wolfe, J.B. and Kaplan, N.O. Hexose phosphate and hexose reductase. A. D-Mannitol-1-phosphate dehydrogenase from E. coli. Methods Enzymol. 1 (1955) 346–348.
3.  Wolfe, J.B. and Kaplan, N.O. D-Mannitol 1-phosphate dehydrogenase from Escherichia coli. J. Biol. Chem. 218 (1956) 849–869. [PMID: 13295236]
[EC 1.1.1.17 created 1961]
 
 
EC 1.1.1.18     
Accepted name: inositol 2-dehydrogenase
Reaction: myo-inositol + NAD+ = 2,4,6/3,5-pentahydroxycyclohexanone + NADH + H+
Other name(s): myo-inositol 2-dehydrogenase; myo-inositol:NAD+ oxidoreductase; inositol dehydrogenase; myo-inositol dehydrogenase
Systematic name: myo-inositol:NAD+ 2-oxidoreductase
References:
1.  Berman, T. and Magasanik, B. The pathway of myo-inositol degradation in Aerobacter aerogenes. Dehydrogenation and dehydration. J. Biol. Chem. 241 (1966) 800–806. [PMID: 5905122]
2.  Larner, J., Jackson, W.T., Graves, D.J. and Stamner, J.R. Inositol dehydrogenase from Aerobacter aerogenes. Arch. Biochem. Biophys. 60 (1956) 352–363. [PMID: 13292912]
3.  Vidal-Lieria, M. and van Uden, N. Inositol dehydrogenase from the yeast Cryptococcus melibiosum. Biochim. Biophys. Acta 293 (1973) 295–303. [PMID: 4351258]
[EC 1.1.1.18 created 1961]
 
 
EC 1.1.1.19     
Accepted name: glucuronate reductase
Reaction: L-gulonate + NADP+ = D-glucuronate + NADPH + H+
Other name(s): L-hexonate:NADP dehydrogenase; TPN-L-gulonate dehydrogenase; NADP-L-gulonate dehydrogenase; D-glucuronate dehydrogenase; D-glucuronate reductase; L-glucuronate reductase (incorrect)
Systematic name: L-gulonate:NADP+ 6-oxidoreductase
Comments: Also reduces D-galacturonate. May be identical with EC 1.1.1.2 [alcohol dehydrogenase (NADP+)].
References:
1.  Sivak, A. and Hoffmann-Ostenhof, O. Enzymes of meso-inositol catabolism in the yeast Schwanniomyces occidentalis. Biochim. Biophys. Acta 53 (1961) 426–428. [PMID: 13913518]
2.  von Wartburg, J.P. and Wermoth, B. Aldehyde reductase. In: Jakoby, W.B. (Ed.), Enzymatic Basis of Detoxication, vol. 1, Academic Press, New York, 1980, pp. 249–260.
3.  York, J.L., Grollman, A.P. and Bublitz, C. TPN-L-gulonate dehydrogenase. Biochim. Biophys. Acta 47 (1961) 298–306. [PMID: 13787380]
[EC 1.1.1.19 created 1961]
 
 
EC 1.1.1.20     
Accepted name: glucuronolactone reductase
Reaction: L-gulono-1,4-lactone + NADP+ = D-glucurono-3,6-lactone + NADPH + H+
Other name(s): GRase; gulonolactone dehydrogenase
Systematic name: L-gulono-1,4-lactone:NADP+ 1-oxidoreductase
References:
1.  Suzuki, K., Mano, Y. and Shimazono, N. Conversion of L-gulonolactone to L-ascorbic acid; properties of the microsomal enzyme in rat liver. J. Biochem. (Tokyo) 48 (1960) 313–315.
[EC 1.1.1.20 created 1961]
 
 
EC 1.1.1.21     
Accepted name: aldose reductase
Reaction: alditol + NAD(P)+ = aldose + NAD(P)H + H+
Other name(s): polyol dehydrogenase (NADP+); ALR2; alditol:NADP+ oxidoreductase; alditol:NADP+ 1-oxidoreductase; NADPH-aldopentose reductase; NADPH-aldose reductase; aldehyde reductase (misleading)
Systematic name: alditol:NAD(P)+ 1-oxidoreductase
Comments: Has wide specificity.
References:
1.  Attwood, M.A. and Doughty, C.C. Purification and properties of calf liver aldose reductase. Biochim. Biophys. Acta 370 (1974) 358–368. [PMID: 4216364]
2.  Boghosian, R.A. and McGuinness, E.T. Affinity purification and properties of porcine brain aldose reductase. Biochim. Biophys. Acta 567 (1979) 278–286. [PMID: 36151]
3.  Hers, H.G. L’Aldose-réductase. Biochim. Biophys. Acta 37 (1960) 120–126. [PMID: 14401390]
4.  Scher, B.M. and Horecker, B.L. Pentose metabolism in Candida. 3. The triphosphopyridine nucleotide-specific polyol dehydrogenase of Candida utilis. Arch. Biochem. Biophys. 116 (1966) 117–128. [PMID: 4381350]
[EC 1.1.1.21 created 1961 (EC 1.1.1.139 created 1972, incorporated 1978), modified 2019]
 
 
EC 1.1.1.22     
Accepted name: UDP-glucose 6-dehydrogenase
Reaction: UDP-α-D-glucose + 2 NAD+ + H2O = UDP-α-D-glucuronate + 2 NADH + 2 H+
Other name(s): UDP-glucose dehydrogenase; uridine diphosphoglucose dehydrogenase; UDPG dehydrogenase; UDPG:NAD oxidoreductase; UDP-α-D-glucose:NAD oxidoreductase; UDP-glucose:NAD+ oxidoreductase; uridine diphosphate glucose dehydrogenase; UDP-D-glucose dehydrogenase; uridine diphosphate D-glucose dehydrogenase
Systematic name: UDP-α-D-glucose:NAD+ 6-oxidoreductase
Comments: Also acts on UDP-α-D-2-deoxyglucose.
References:
1.  Druzhinina, T.N., Kusov, Y.Y., Shibaev, V.N., Kochetkov, N.K., Biely, P., Kucar, S. and Bauer, S. Uridine diphosphate 2-deoxyglucose. Chemical synthesis, enzymic oxidation and epimerization. Biochim. Biophys. Acta 381 (1975) 301–307. [PMID: 1091296]
2.  Maxwell, E.S., Kalckar, H.M. and Strominger, J.L. Some properties of uridine diphosphoglucose dehydrogenase. Arch. Biochem. Biophys. 65 (1956) 2–10. [PMID: 13373402]
3.  Strominger, J.L. and Mapson, L.W. Uridine diphosphoglucose dehydrogenase of pea seedlings. Biochem. J. 66 (1957) 567–572. [PMID: 13459898]
4.  Strominger, J.L., Maxwell, E.S., Axelrod, J. and Kalckar, H.M. Enzymatic formation of uridine diphosphogluconic acid. J. Biol. Chem. 224 (1957) 79–90. [PMID: 13398389]
[EC 1.1.1.22 created 1961]
 
 
EC 1.1.1.23     
Accepted name: histidinol dehydrogenase
Reaction: L-histidinol + 2 NAD+ + H2O = L-histidine + 2 NADH + 3 H+
Other name(s): L-histidinol dehydrogenase
Systematic name: L-histidinol:NAD+ oxidoreductase
Comments: Also oxidizes L-histidinal. The Neurospora enzyme also catalyses the reactions of EC 3.5.4.19 (phosphoribosyl-AMP cyclohydrolase) and EC 3.6.1.31 (phosphoribosyl-ATP diphosphatase).
References:
1.  Adams, E. Enzymatic synthesis of histidine from histidinol. J. Biol. Chem. 209 (1954) 829–846. [PMID: 13192138]
2.  Adams, E. L-Histidinal, a biosynthetic precursor of histidine. J. Biol. Chem. 217 (1955) 325–344. [PMID: 13271397]
3.  Loper, J.C. Histidinol dehydrogenase from Salmonella typhimurium. Crystallization and composition studies. J. Biol. Chem. 243 (1968) 3264–3272. [PMID: 4872177]
4.  Yourno, J. and Ino, I. Purification and crystallization of histidinol dehydrogenase from Salmonella typhimurium LT-2. J. Biol. Chem. 243 (1968) 3273–3276. [PMID: 4872176]
[EC 1.1.1.23 created 1961]
 
 
EC 1.1.1.24     
Accepted name: quinate/shikimate dehydrogenase (NAD+)
Reaction: L-quinate + NAD+ = 3-dehydroquinate + NADH + H+
Glossary: quinate = (1R,3R,4R,5R)-1,3,4,5-tetrahydroxycyclohexanecarboxylic acid and is a cyclitol carboxylate
The numbering system used for the 3-dehydroquinate is that of the recommendations on cyclitols, sections I-8 and I-9: and is shown in the reaction diagram. The use of the term '5-dehydroquinate' for this compound is based on an earlier system of numbering.
Other name(s): quinate dehydrogenase (ambiguous); quinic dehydrogenase (ambiguous); quinate:NAD oxidoreductase; quinate 5-dehydrogenase (ambiguous); quinate:NAD+ 5-oxidoreductase
Systematic name: L-quinate:NAD+ 3-oxidoreductase
Comments: The enzyme, found mostly in bacteria (mostly, but not exclusively in Gram-positive bacteria), fungi, and plants, participates in the degradation of quinate and shikimate with a strong preference for NAD+ as a cofactor. While the enzyme can act on both quinate and shikimate, activity is higher with the former. cf. EC 1.1.5.8, quinate/shikimate dehydrogenase (quinone), EC 1.1.1.282, quinate/shikimate dehydrogenase [NAD(P)+], and EC 1.1.1.25, shikimate dehydrogenase (NADP+).
References:
1.  Mitsuhashi, S. and Davis, B.D. Aromatic biosynthesis. XIII. Conversion of quinic acid to 5-dehydroquinic acid by quinic dehydrogenase. Biochim. Biophys. Acta 15 (1954) 268–280. [PMID: 13208693]
2.  Gamborg, O.L. Aromatic metabolism in plants. III. Quinate dehydrogenase from mung bean cell suspension cultures. Biochim. Biophys. Acta 128 (1966) 483–491.
3.  Hawkins, A.R., Giles, N.H. and Kinghorn, J.R. Genetical and biochemical aspects of quinate breakdown in the filamentous fungus Aspergillus nidulans. Biochem. Genet. 20 (1982) 271–286. [PMID: 7049157]
4.  Singh, S., Stavrinides, J., Christendat, D. and Guttman, D.S. A phylogenomic analysis of the shikimate dehydrogenases reveals broadscale functional diversification and identifies one functionally distinct subclass. Mol. Biol. Evol. 25 (2008) 2221–2232. [PMID: 18669580]
5.  Teramoto, H., Inui, M. and Yukawa, H. Regulation of expression of genes involved in quinate and shikimate utilization in Corynebacterium glutamicum. Appl. Environ. Microbiol. 75 (2009) 3461–3468. [PMID: 19376919]
6.  Kubota, T., Tanaka, Y., Hiraga, K., Inui, M. and Yukawa, H. Characterization of shikimate dehydrogenase homologues of Corynebacterium glutamicum. Appl. Microbiol. Biotechnol. 97 (2013) 8139–8149. [PMID: 23306642]
7.  Peek, J. and Christendat, D. The shikimate dehydrogenase family: functional diversity within a conserved structural and mechanistic framework. Arch. Biochem. Biophys. 566 (2015) 85–99. [PMID: 25524738]
[EC 1.1.1.24 created 1961, modified 1976, modified 2004, modified 2021]
 
 
EC 1.1.1.25     
Accepted name: shikimate dehydrogenase (NADP+)
Reaction: shikimate + NADP+ = 3-dehydroshikimate + NADPH + H+
Other name(s): shikimate dehydrogenase; dehydroshikimic reductase; shikimate oxidoreductase; shikimate:NADP+ oxidoreductase; 5-dehydroshikimate reductase; shikimate 5-dehydrogenase; 5-dehydroshikimic reductase; DHS reductase; shikimate:NADP+ 5-oxidoreductase; AroE
Systematic name: shikimate:NADP+ 3-oxidoreductase
Comments: NAD+ cannot replace NADP+ [3]. In higher organisms, this enzyme forms part of a multienzyme complex with EC 4.2.1.10, 3-dehydroquinate dehydratase [4]. cf. EC 1.1.1.24, quinate/shikimate dehydrogenase (NAD+), EC 1.1.5.8, quinate/shikimate dehydrogenase (quinone), and EC 1.1.1.282, quinate/shikimate dehydrogenase [NAD(P)+].
References:
1.  Mitsuhashi, S. and Davis, B.D. Aromatic biosynthesis. XIII. Conversion of quinic acid to 5-dehydroquinic acid by quinic dehydrogenase. Biochim. Biophys. Acta 15 (1954) 268–280. [PMID: 13208693]
2.  Yaniv, H. and Gilvarg, C. Aromatic biosynthesis. XIV. 5-Dehydroshikimic reductase. J. Biol. Chem. 213 (1955) 787–795. [PMID: 14367339]
3.  Balinsky, D. and Davies, D.D. Aromatic biosynthesis in higher plants. 1. Preparation and properties of dehydroshikimic reductase. Biochem. J. 80 (1961) 292–296. [PMID: 13686342]
4.  Chaudhuri, S. and Coggins, J.R. The purification of shikimate dehydrogenase from Escherichia coli. Biochem. J. 226 (1985) 217–223. [PMID: 3883995]
5.  Anton, I.A. and Coggins, J.R. Sequencing and overexpression of the Escherichia coli aroE gene encoding shikimate dehydrogenase. Biochem. J. 249 (1988) 319–326. [PMID: 3277621]
6.  Ye, S., Von Delft, F., Brooun, A., Knuth, M.W., Swanson, R.V. and McRee, D.E. The crystal structure of shikimate dehydrogenase (AroE) reveals a unique NADPH binding mode. J. Bacteriol. 185 (2003) 4144–4151. [PMID: 12837789]
[EC 1.1.1.25 created 1961, modified 1976, modified 2004, modified 2021]
 
 
EC 1.1.1.26     
Accepted name: glyoxylate reductase
Reaction: glycolate + NAD+ = glyoxylate + NADH + H+
Other name(s): NADH-glyoxylate reductase; glyoxylic acid reductase; NADH-dependent glyoxylate reductase
Systematic name: glycolate:NAD+ oxidoreductase
Comments: Reduces glyoxylate to glycolate or hydroxypyruvate to D-glycerate.
References:
1.  Zelitch, I. Oxidation and reduction of glycolic and glyoxylic acids in plants. II. Glyoxylic acid reductase. J. Biol. Chem. 201 (1953) 719–726. [PMID: 13061410]
2.  Zelitch, I. The isolation and action of crystalline glyoxylic acid reductase from tobacco leaves. J. Biol. Chem. 216 (1955) 553–575. [PMID: 13271335]
[EC 1.1.1.26 created 1961]
 
 
EC 1.1.1.27     
Accepted name: L-lactate dehydrogenase
Reaction: (S)-lactate + NAD+ = pyruvate + NADH + H+
Other name(s): lactic acid dehydrogenase; L(+)-nLDH; L-(+)-lactate dehydrogenase; L-lactic dehydrogenase; L-lactic acid dehydrogenase; lactate dehydrogenase; lactate dehydrogenase NAD-dependent; lactic dehydrogenase; NAD-lactate dehydrogenase
Systematic name: (S)-lactate:NAD+ oxidoreductase
Comments: Also oxidizes other (S)-2-hydroxymonocarboxylic acids. NADP+ also acts, more slowly, with the animal, but not the bacterial, enzyme.
References:
1.  Dennis, D. and Kaplan, N.O. D and L-lactic acid dehydrogenase in Lactobacillus plantarum. J. Biol. Chem. 235 (1960) 810–818. [PMID: 13815938]
2.  Everse, J. and Kaplan, N.O. Lactate dehydrogenases: structure and function. Adv. Enzymol. Relat. Subj. Biochem. 37 (1973) 61–133. [PMID: 4146647]
3.  Holbrook, J.J., Liljas, A., Steindel, S.J. and Rossmann, M.G. Lactate dehydrogenase. In: Boyer, P.D. (Ed.), The Enzymes, 3rd edn, vol. 11, Academic Press, New York, 1975, pp. 191–292.
4.  Schär, H.-P. and Zuber, H. Structure and function of L-lactate dehydrogenases from thermophilic and mesophilic bacteria. I) Isolation and characterization of lactate dehydrogenases from thermophilic and mesophilic bacilli. Hoppe-Seyler's Z. Physiol. Chem. 360 (1979) 795–807. [PMID: 114469]
[EC 1.1.1.27 created 1961]
 
 
EC 1.1.1.28     
Accepted name: D-lactate dehydrogenase
Reaction: (R)-lactate + NAD+ = pyruvate + NADH + H+
Other name(s): lactic acid dehydrogenase; lactic acid dehydrogenase; D-specific lactic dehydrogenase; D-(-)-lactate dehydrogenase (NAD); D-lactic acid dehydrogenase; D-lactic dehydrogenase
Systematic name: (R)-lactate:NAD+ oxidoreductase
References:
1.  Dennis, D. and Kaplan, N.O. D and L-lactic acid dehydrogenase in Lactobacillus plantarum. J. Biol. Chem. 235 (1960) 810–818. [PMID: 13815938]
[EC 1.1.1.28 created 1961]
 
 
EC 1.1.1.29     
Accepted name: glycerate dehydrogenase
Reaction: D-glycerate + NAD+ = hydroxypyruvate + NADH + H+
Other name(s): D-glycerate dehydrogenase; hydroxypyruvate reductase; (R)-glycerate:NAD+ oxidoreductase
Systematic name: D-glycerate:NAD+ oxidoreductase
References:
1.  Holzer, H. and Holldorf, A. Isolation of a D-glycerate dehydrogenase, its properties, and its use for the optical determination of hydroxypyruvate in the presence of pyruvate. Biochem. Z. 329 (1957) 292–312. [PMID: 13522707]
2.  Stafford, H.A., Magaldi, A. and Vennesland, B. The enzymatic reduction of hydroxypyruvic acid to D-glyceric acid in higher plants. J. Biol. Chem. 207 (1954) 621–629. [PMID: 13163046]
[EC 1.1.1.29 created 1961]
 
 
EC 1.1.1.30     
Accepted name: 3-hydroxybutyrate dehydrogenase
Reaction: (R)-3-hydroxybutanoate + NAD+ = acetoacetate + NADH + H+
Other name(s): NAD-β-hydroxybutyrate dehydrogenase; hydroxybutyrate oxidoreductase; β-hydroxybutyrate dehydrogenase; D-β-hydroxybutyrate dehydrogenase; D-3-hydroxybutyrate dehydrogenase; D-(-)-3-hydroxybutyrate dehydrogenase; β-hydroxybutyric acid dehydrogenase; 3-D-hydroxybutyrate dehydrogenase; β-hydroxybutyric dehydrogenase
Systematic name: (R)-3-hydroxybutanoate:NAD+ oxidoreductase
Comments: Also oxidizes other 3-hydroxymonocarboxylic acids.
References:
1.  Bergmeyer, H.-U., Gawehn, K., Klotzsch, H., Krebs, H.A. and Williamson, D.H. Purification and properties of crystalline 3-hydroxybutyrate dehydrogenase from Rhodopseudomonas spheroides. Biochem. J. 102 (1967) 423–431. [PMID: 4291491]
2.  Delafield, F.P., Cooksey, K.E. and Doudoroff, M. β-Hydroxybutyric dehydrogenase and dimer hydrolase of Pseudomonas lemoignei. J. Biol. Chem. 240 (1965) 4023–4028. [PMID: 4954074]
3.  Lehninger, A.L., Sudduth, H.C. and Wise, J.B. D-β-Hydroxybutyric dehydrogenase of mitochondria. J. Biol. Chem. 235 (1960) 2450–2455. [PMID: 14415394]
[EC 1.1.1.30 created 1961]
 
 
EC 1.1.1.31     
Accepted name: 3-hydroxyisobutyrate dehydrogenase
Reaction: 3-hydroxy-2-methylpropanoate + NAD+ = 2-methyl-3-oxopropanoate + NADH + H+
Other name(s): β-hydroxyisobutyrate dehydrogenase
Systematic name: 3-hydroxy-2-methylpropanoate:NAD+ oxidoreductase
References:
1.  Robinson, W.G. and Coon, M.J. Purification and properties of β-hydroxyisobutyric dehydrogenase. J. Biol. Chem. 225 (1957) 511–521. [PMID: 13416257]
[EC 1.1.1.31 created 1961]
 
 
EC 1.1.1.32     
Accepted name: mevaldate reductase
Reaction: (R)-mevalonate + NAD+ = mevaldate + NADH + H+
Other name(s): mevalonic dehydrogenase
Systematic name: (R)-mevalonate:NAD+ oxidoreductase
References:
1.  Schlesinger, M.J. and Coon, M.J. Reduction of mevaldic acid to mevalonic acid by a partial purified enzyme from liver. J. Biol. Chem. 236 (1961) 2421–2424. [PMID: 13747804]
[EC 1.1.1.32 created 1961]
 
 
EC 1.1.1.33     
Accepted name: mevaldate reductase (NADPH)
Reaction: (R)-mevalonate + NADP+ = mevaldate + NADPH + H+
Other name(s): mevaldate (reduced nicotinamide adenine dinucleotide phosphate) reductase; mevaldate reductase (NADPH2)
Systematic name: (R)-mevalonate:NADP+ oxidoreductase
Comments: May be identical with EC 1.1.1.2 [alcohol dehydrogenase (NADP+)].
References:
1.  Coon, M.J., Kupiecki, F.P., Dekker, E.E., Schlesinger, M.J. and del Campillo, A. The enzymic synthesis of branched-chain acids. In: Wolstenholme, G.E.W. and O'Connor, M. (Ed.), CIBA Symposium on the Biosynthesis of Terpenes and Sterols, CIBA Symposium on the Biosynthesis of Terpenes and Sterols, London, 1959, pp. 62–74.
2.  von Wartburg, J.P. and Wermoth, B. Aldehyde reductase. In: Jakoby, W.B. (Ed.), Enzymatic Basis of Detoxication, vol. 1, Academic Press, New York, 1980, pp. 249–260.
[EC 1.1.1.33 created 1961]
 
 
EC 1.1.1.34     
Accepted name: hydroxymethylglutaryl-CoA reductase (NADPH)
Reaction: (R)-mevalonate + CoA + 2 NADP+ = (S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
Other name(s): hydroxymethylglutaryl coenzyme A reductase (reduced nicotinamide adenine dinucleotide phosphate); 3-hydroxy-3-methylglutaryl-CoA reductase (ambiguous); β-hydroxy-β-methylglutaryl coenzyme A reductase (ambiguous); hydroxymethylglutaryl CoA reductase (NADPH); S-3-hydroxy-3-methylglutaryl-CoA reductase (ambiguous); NADPH-hydroxymethylglutaryl-CoA reductase; HMGCoA reductase-mevalonate:NADP-oxidoreductase (acetylating-CoA); 3-hydroxy-3-methylglutaryl CoA reductase (NADPH); hydroxymethylglutaryl-CoA reductase (NADPH2)
Systematic name: (R)-mevalonate:NADP+ oxidoreductase (CoA-acylating)
Comments: The enzyme is inactivated by EC 2.7.11.31 {[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase} and reactivated by EC 3.1.3.47 {[hydroxymethylglutaryl-CoA reductase (NADPH)]-phosphatase}.
References:
1.  Bucher, N.L.R., Overath, P. and Lynen, F. β-Hydroxy-β-methylglutaryl coenzyme A reductase, cleavage and condensing enzymes in relation to cholesterol formation in rat liver. Biochim. Biophys. Acta 40 (1960) 491–501. [PMID: 13805544]
2.  Durr, I.F. and Rudney, H. The reduction of β-hydroxy-β-methylglutaryl coenzyme A to mevalonic acid. J. Biol. Chem. 235 (1960) 2572–2578. [PMID: 13818862]
3.  Kawachi, T. and Rudney, H. Solubilization and purification of β-hydroxy-β-methylglutaryl coenzyme A reductase from rat liver. Biochemistry 9 (1970) 1700. [PMID: 4985697]
[EC 1.1.1.34 created 1961]
 
 
EC 1.1.1.35     
Accepted name: 3-hydroxyacyl-CoA dehydrogenase
Reaction: (S)-3-hydroxyacyl-CoA + NAD+ = 3-oxoacyl-CoA + NADH + H+
Other name(s): β-hydroxyacyl dehydrogenase; β-keto-reductase; 3-keto reductase; 3-hydroxyacyl coenzyme A dehydrogenase; β-hydroxyacyl-coenzyme A synthetase; β-hydroxyacylcoenzyme A dehydrogenase; β-hydroxybutyrylcoenzyme A dehydrogenase; 3-hydroxyacetyl-coenzyme A dehydrogenase; L-3-hydroxyacyl coenzyme A dehydrogenase; L-3-hydroxyacyl CoA dehydrogenase; β-hydroxyacyl CoA dehydrogenase; 3β-hydroxyacyl coenzyme A dehydrogenase; 3-hydroxybutyryl-CoA dehydrogenase; β-ketoacyl-CoA reductase; β-hydroxy acid dehydrogenase; 3-L-hydroxyacyl-CoA dehydrogenase; 3-hydroxyisobutyryl-CoA dehydrogenase; 1-specific DPN-linked β-hydroxybutyric dehydrogenase
Systematic name: (S)-3-hydroxyacyl-CoA:NAD+ oxidoreductase
Comments: Also oxidizes S-3-hydroxyacyl-N-acylthioethanolamine and S-3-hydroxyacyl-hydrolipoate. Some enzymes act, more slowly, with NADP+. Broad specificity to acyl chain-length (cf. EC 1.1.1.211 [long-chain-3-hydroxyacyl-CoA dehydrogenase]).
References:
1.  Hillmer, P. and Gottschalk, G. Solubilization and partial characterisation of particulate dehydrogenases from Clostridium kluyveri. Biochim. Biophys. Acta 334 (1974) 12–23.
2.  Lehninger, A.L. and Greville, G.D. The enzymatic oxidation of d- and l-β-hydroxybutyrate. Biochim. Biophys. Acta 12 (1953) 188–202. [PMID: 13115428]
3.  Stern, J.R. Crystalline β-hydroxybutyrate dehydrogenase from pig heart. Biochim. Biophys. Acta 26 (1957) 448–449. [PMID: 13499396]
4.  Wakil, S.J., Green, D.E., Mii, S. and Mahler, H.R. Studies on the fatty acid oxidizing system of animal tissues. VI. β-Hydroxyacyl coenzyme A dehydrogenase. J. Biol. Chem. 207 (1954) 631–638. [PMID: 13163047]
[EC 1.1.1.35 created 1961]
 
 
EC 1.1.1.36     
Accepted name: acetoacetyl-CoA reductase
Reaction: (R)-3-hydroxyacyl-CoA + NADP+ = 3-oxoacyl-CoA + NADPH + H+
Other name(s): acetoacetyl coenzyme A reductase; hydroxyacyl coenzyme-A dehydrogenase; NADP-linked acetoacetyl CoA reductase; NADPH:acetoacetyl-CoA reductase; D(–)-β-hydroxybutyryl CoA-NADP oxidoreductase; short chain β-ketoacetyl(acetoacetyl)-CoA reductase; β-ketoacyl-CoA reductase; D-3-hydroxyacyl-CoA reductase; (R)-3-hydroxyacyl-CoA dehydrogenase
Systematic name: (R)-3-hydroxyacyl-CoA:NADP+ oxidoreductase
References:
1.  Wakil, S.J. and Bressler, R. Studies on the mechanism of fatty acid synthesis. X. Reduced triphosphopyridine nucleotide-acetoacetyl coenzyme A reductase. J. Biol. Chem. 237 (1962) 687–693. [PMID: 14004466]
[EC 1.1.1.36 created 1961]
 
 
EC 1.1.1.37     
Accepted name: malate dehydrogenase
Reaction: (S)-malate + NAD+ = oxaloacetate + NADH + H+
Other name(s): malic dehydrogenase; L-malate dehydrogenase; NAD-L-malate dehydrogenase; malic acid dehydrogenase; NAD-dependent malic dehydrogenase; NAD-malate dehydrogenase; NAD-malic dehydrogenase; malate (NAD) dehydrogenase; NAD-dependent malate dehydrogenase; NAD-specific malate dehydrogenase; NAD-linked malate dehydrogenase; MDH (ambiguous); L-malate-NAD+ oxidoreductase
Systematic name: (S)-malate:NAD+ oxidoreductase
Comments: There are several forms of malate dehydrogenases that differ by their use of substrate and cofactors. This NAD+-dependent enzyme forms oxaloacetate and unlike EC 1.1.1.38, malate dehydrogenase (oxaloacetate-decarboxylating), is unable to convert it to pyruvate. Also oxidizes some other 2-hydroxydicarboxylic acids. cf. EC 1.1.1.82, malate dehydrogenase (NADP+); EC 1.1.1.299, malate dehydrogenase [NAD(P)+]; and EC 1.1.5.4, malate dehydrogenase (quinone).
References:
1.  Banaszak, L.J. and Bradshaw, R.A. Malate dehydrogenase. In: Boyer, P.D. (Ed.), The Enzymes, 3rd edn, vol. 11, Academic Press, New York, 1975, pp. 369–396.
2.  Guha, A., Englard, S. and Listowsky, I. Beef heart malic dehydrogenases. VII. Reactivity of sulfhydryl groups and conformation of the supernatant enzyme. J. Biol. Chem. 243 (1968) 609–615. [PMID: 5637713]
3.  McReynolds, M.S. and Kitto, G.B. Purification and properties of Drosophila malate dehydrogenases. Biochim. Biophys. Acta 198 (1970) 165–175. [PMID: 4313528]
4.  Wolfe, R.G. and Nielands, J.B. Some molecular and kinetic properties of heart malic dehydrogenase. J. Biol. Chem. 221 (1956) 61–69. [PMID: 13345798]
[EC 1.1.1.37 created 1961]
 
 
EC 1.1.1.38     
Accepted name: malate dehydrogenase (oxaloacetate-decarboxylating)
Reaction: (1) (S)-malate + NAD+ = pyruvate + CO2 + NADH
(2) oxaloacetate = pyruvate + CO2
Other name(s): ’malic’ enzyme (ambiguous); pyruvic-malic carboxylase (ambiguous); NAD+-specific malic enzyme; NAD+-malic enzyme; NAD+-linked malic enzyme
Systematic name: (S)-malate:NAD+ oxidoreductase (oxaloacetate-decarboxylating)
Comments: Unlike EC 1.1.1.39, malate dehydrogenase (decarboxylating), this enzyme can also decarboxylate oxaloacetate. cf. EC 1.1.1.40, malate dehydrogenase (oxaloacetate-decarboxylating) (NADP+).
References:
1.  Kaufman, S., Korkes, S. and del Campillo, A. Biosynthesis of dicarboxylic acids by carbon dioxide fixation. V. Further studies of the "malic" enzyme of Lactobacillus arabinosus. J. Biol. Chem. 192 (1951) 301–312. [PMID: 14917678]
2.  Yamaguchi, M. Studies on regulatory functions of malic enzymes. IV. Effects of sulfhydryl group modification on the catalytic function of NAD-linked malic enzyme from Escherichia coli. J. Biochem. 86 (1979) 325–333. [PMID: 225306]
[EC 1.1.1.38 created 1961]
 
 
EC 1.1.1.39     
Accepted name: malate dehydrogenase (decarboxylating)
Reaction: (S)-malate + NAD+ = pyruvate + CO2 + NADH
Other name(s): ’malic’ enzyme (ambiguous); pyruvic-malic carboxylase (ambiguous); NAD-specific malic enzyme (ambiguous); NAD-malic enzyme (ambiguous); malate dehydrogenase (decarboxylating) (ambiguous)
Systematic name: (S)-malate:NAD+ oxidoreductase (decarboxylating)
Comments: There are several forms of malate dehydrogenases that differ in their use of substrates and cofactors. This particular form is found only in the plant kingdom. Unlike EC 1.1.1.38, which catalyses a similar reaction, this enzyme can not bind oxaloacetate, and thus does not decarboxylate exogeneously-added oxaloacetate. cf. EC 1.1.1.37, malate dehydrogenase; EC 1.1.1.38, malate dehydrogenase (oxaloacetate-decarboxylating); and EC 1.1.1.83, D-malate dehydrogenase (decarboxylating).
References:
1.  Macrae, A.R. Isolation and properties of a ’malic’ enzyme from cauliflower bud mitochondria. Biochem. J. 122 (1971) 495–501. [PMID: 4399380]
2.  Grover, S.D., Canellas, P.F. and Wedding, R.T. Purification of NAD malic enzyme from potato and investigation of some physical and kinetic properties. Arch. Biochem. Biophys. 209 (1981) 396–407. [PMID: 7294802]
3.  Wedding, R.T. and Black, M.K. Physical and kinetic properties and regulation of the NAD malic enzyme purified from leaves of Crassula argentea. Plant Physiol. 72 (1983) 1021–1028. [PMID: 16663114]
4.  Wedding, R.T. Malic enzymes of higher plants: characteristics, regulation, and physiological function. Plant Physiol. 90 (1989) 367–371. [PMID: 16666776]
[EC 1.1.1.39 created 1961]
 
 
EC 1.1.1.40     
Accepted name: malate dehydrogenase (oxaloacetate-decarboxylating) (NADP+)
Reaction: (1) (S)-malate + NADP+ = pyruvate + CO2 + NADPH
(2) oxaloacetate = pyruvate + CO2
Other name(s): ’malic’ enzyme (ambiguous); pyruvic-malic carboxylase (ambiguous); malate dehydrogenase (decarboxylating, NADP+); NADP+-linked decarboxylating malic enzyme; NADP+-malic enzyme; NADP+-specific malic enzyme; NADP+-specific malate dehydrogenase; malate dehydrogenase (NADP+, decarboxylating); L-malate:NADP+ oxidoreductase
Systematic name: (S)-malate:NADP+ oxidoreductase (oxaloacetate-decarboxylating)
Comments: The enzyme catalyses the oxidative decarboxylation of (S)-malate in the presence of NADP+ and divalent metal ions, and the decarboxylation of oxaloacetate. cf. EC 1.1.1.38, malate dehydrogenase (oxaloacetate-decarboxylating), and EC 1.1.1.39, malate dehydrogenase (decarboxylating).
References:
1.  Harary, I., Korey, S.R. and Ochoa, S. Biosynthesis of dicarboxylic acids by carbon dioxide fixation. VII. Equilibrium of "malic" enzyme reaction. J. Biol. Chem. 203 (1953) 595–604. [PMID: 13084629]
2.  Ochoa, S., Mehler, A.H. and Kornberg, A. Biosynthesis of dicarboxylic acids by carbon dioxide fixation. I. Isolation and properties of an enzyme from pigeon liver catalyzing the reversible oxidative decarboxylation of l-malic acid. J. Biol. Chem. 174 (1948) 979–1000. [PMID: 18871257]
3.  Rutter, W.J. and Lardy, H.A. Purification and properties of pigeon liver malic enzyme. J. Biol. Chem. 233 (1958) 374–382. [PMID: 13563505]
4.  Stickland, R.G. Some properties of the malic enzyme of pigeon liver. 1. Conversion of malate into pyruvate. Biochem. J. 73 (1959) 646–654. [PMID: 13834656]
5.  Stickland, R.G. Some properties of the malic enzyme of pigeon liver. 2. Synthesis of malate from pyruvate. Biochem. J. 73 (1959) 654–659. [PMID: 13834657]
6.  Walker, D.A. Physiological studies on acid metabolism. 7. Malic enzyme from KalanchoĆ« crenata: effects of carbon dioxide concentration. Biochem. J. 74 (1960) 216–223. [PMID: 13842495]
[EC 1.1.1.40 created 1961, modified 1976]
 
 
EC 1.1.1.41     
Accepted name: isocitrate dehydrogenase (NAD+)
Reaction: isocitrate + NAD+ = 2-oxoglutarate + CO2 + NADH
Glossary: isocitrate = (1R,2S)-1-hydroxypropane-1,2,3-tricarboxylate (previously known as threo-Ds-isocitrate)
Other name(s): isocitric dehydrogenase; β-ketoglutaric-isocitric carboxylase; isocitric acid dehydrogenase; NAD dependent isocitrate dehydrogenase; NAD isocitrate dehydrogenase; NAD-linked isocitrate dehydrogenase; NAD-specific isocitrate dehydrogenase; NAD isocitric dehydrogenase; isocitrate dehydrogenase (NAD); IDH (ambiguous); nicotinamide adenine dinucleotide isocitrate dehydrogenase
Systematic name: isocitrate:NAD+ oxidoreductase (decarboxylating)
Comments: Requires Mn2+ or Mg2+ for activity. Unlike EC 1.1.1.42, isocitrate dehydrogenase (NADP+), oxalosuccinate cannot be used as a substrate. In eukaryotes, isocitrate dehydrogenase exists in two forms: an NAD+-linked enzyme found only in mitochondria and displaying allosteric properties, and a non-allosteric, NADP+-linked enzyme that is found in both mitochondria and cytoplasm [7]. The enzyme from some species can also use NADP+ but much more slowly [9].
References:
1.  Hathaway, J.A. and Atkinson, D.E. The effect of adenylic acid on yeast nicotinamide adenine dinucleotide isocitrate dehydrogenase, a possible metabolic control mechanism. J. Biol. Chem. 238 (1963) 2875–2881. [PMID: 14063317]
2.  Kornberg, A. and Pricer, W.E. Di- and triphosphopyridine nucleotide isocitric dehydrogenase in yeast. J. Biol. Chem. 189 (1951) 123–136. [PMID: 14832224]
3.  Plaut, G.W.E. Isocitrate dehydrogenases. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Ed.), The Enzymes, 2nd edn, vol. 7, Academic Press, New York, 1963, pp. 105–126.
4.  Plaut, G.W.E. and Sung, S.-C. Diphosphopyridine nucleotide isocitric dehydrogenase from animal tissues. J. Biol. Chem. 207 (1954) 305–314. [PMID: 13152105]
5.  Ramakrishnan, C.V. and Martin, S.M. Isocitric dehydrogenase in Aspergillus niger. Arch. Biochem. Biophys. 55 (1955) 403–407.
6.  Vickery, H.B. A suggested new nomenclature for the isomers of isocitric acid. J. Biol. Chem. 237 (1962) 1739–1741. [PMID: 13925783]
7.  Camacho, M.L., Brown, R.A., Bonete, M.J., Danson, M.J. and Hough, D.W. Isocitrate dehydrogenases from Haloferax volcanii and Sulfolobus solfataricus: enzyme purification, characterisation and N-terminal sequence. FEMS Microbiol. Lett. 134 (1995) 85–90. [PMID: 8593959]
8.  Kim, Y.O., Koh, H.J., Kim, S.H., Jo, S.H., Huh, J.W., Jeong, K.S., Lee, I.J., Song, B.J. and Huh, T.L. Identification and functional characterization of a novel, tissue-specific NAD+-dependent isocitrate dehydrogenase β subunit isoform. J. Biol. Chem. 274 (1999) 36866–36875. [PMID: 10601238]
9.  Inoue, H., Tamura, T., Ehara, N., Nishito, A., Nakayama, Y., Maekawa, M., Imada, K., Tanaka, H. and Inagaki, K. Biochemical and molecular characterization of the NAD+-dependent isocitrate dehydrogenase from the chemolithotroph Acidithiobacillus thiooxidans. FEMS Microbiol. Lett. 214 (2002) 127–132. [PMID: 12204383]
[EC 1.1.1.41 created 1961, modified 2005]
 
 
EC 1.1.1.42     
Accepted name: isocitrate dehydrogenase (NADP+)
Reaction: isocitrate + NADP+ = 2-oxoglutarate + CO2 + NADPH + H+ (overall reaction)
(1a) isocitrate + NADP+ = oxalosuccinate + NADPH + H+
(1b) oxalosuccinate = 2-oxoglutarate + CO2
Glossary: isocitrate = (1R,2S)-1-hydroxypropane-1,2,3-tricarboxylate (previously known as threo-Ds-isocitrate)
oxalosuccinate = 1-oxopropane-1,2,3-tricarboxylate
Other name(s): oxalosuccinate decarboxylase; oxalsuccinic decarboxylase; isocitrate (NADP) dehydrogenase; isocitrate (nicotinamide adenine dinucleotide phosphate) dehydrogenase; NADP-specific isocitrate dehydrogenase; NADP-linked isocitrate dehydrogenase; NADP-dependent isocitrate dehydrogenase; NADP isocitric dehydrogenase; isocitrate dehydrogenase (NADP-dependent); NADP-dependent isocitric dehydrogenase; triphosphopyridine nucleotide-linked isocitrate dehydrogenase-oxalosuccinate carboxylase; NADP+-linked isocitrate dehydrogenase; IDH (ambiguous); dual-cofactor-specific isocitrate dehydrogenase; NADP+-ICDH; NADP+-IDH; IDP; IDP1; IDP2; IDP3
Systematic name: isocitrate:NADP+ oxidoreductase (decarboxylating)
Comments: Requires Mn2+ or Mg2+ for activity. Unlike EC 1.1.1.41, isocitrate dehydrogenase (NAD+), oxalosuccinate can be used as a substrate. In eukaryotes, isocitrate dehydrogenase exists in two forms: an NAD+-linked enzyme found only in mitochondria and displaying allosteric properties, and a non-allosteric, NADP+-linked enzyme that is found in both mitochondria and cytoplasm [6]. The enzyme from some species can also use NAD+ but much more slowly [6,7].
References:
1.  Agosin, M.U. and Weinbach, E.C. Partial purification and characterization of the isocitric dehydrogenase from Trypanosoma cruzi. Biochim. Biophys. Acta 21 (1956) 117–126. [PMID: 13363868]
2.  Moyle, J. and Dixon, M. Purification of the isocitrate enzyme (triphosphopyridine nucleotide-linked isocitrate dehydrogenase-oxalosuccinate carboxylase). Biochem. J. 63 (1956) 548–552. [PMID: 13355848]
3.  Plaut, G.W.E. Isocitrate dehydrogenases. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Ed.), The Enzymes, 2nd edn, vol. 7, Academic Press, New York, 1963, pp. 105–126.
4.  Siebert, G., Dubuc, J., Warner, R.C. and Plaut, G.W.E. The preparation of isocitrate dehydrogenase from mammalian heart. J. Biol. Chem. 226 (1957) 965–975. [PMID: 13438885]
5.  Vickery, H.B. A suggested new nomenclature for the isomers of isocitric acid. J. Biol. Chem. 237 (1962) 1739–1741. [PMID: 13925783]
6.  Camacho, M.L., Brown, R.A., Bonete, M.J., Danson, M.J. and Hough, D.W. Isocitrate dehydrogenases from Haloferax volcanii and Sulfolobus solfataricus: enzyme purification, characterisation and N-terminal sequence. FEMS Microbiol. Lett. 134 (1995) 85–90. [PMID: 8593959]
7.  Steen, I.H., Lien, T. and Birkeland, N.-K. Biochemical and phylogenetic characterization of isocitrate dehydrogenase from a hyperthermophilic archaeon, Archaeoglobus fulgidus. Arch. Microbiol. 168 (1997) 412–420. [PMID: 9325430]
8.  Koh, H.J., Lee, S.M., Son, B.G., Lee, S.H., Ryoo, Z.Y., Chang, K.T., Park, J.W., Park, D.C., Song, B.J., Veech, R.L., Song, H. and Huh, T.L. Cytosolic NADP+-dependent isocitrate dehydrogenase plays a key role in lipid metabolism. J. Biol. Chem. 279 (2004) 39968–39974. [PMID: 15254034]
9.  Ceccarelli, C., Grodsky, N.B., Ariyaratne, N., Colman, R.F. and Bahnson, B.J. Crystal structure of porcine mitochondrial NADP+-dependent isocitrate dehydrogenase complexed with Mn2+ and isocitrate. Insights into the enzyme mechanism. J. Biol. Chem. 277 (2002) 43454–43462. [PMID: 12207025]
[EC 1.1.1.42 created 1961, modified 2005]
 
 
EC 1.1.1.43     
Accepted name: phosphogluconate 2-dehydrogenase
Reaction: 6-phospho-D-gluconate + NAD(P)+ = 6-phospho-2-dehydro-D-gluconate + NAD(P)H + H+
Other name(s): 6-phosphogluconic dehydrogenase; phosphogluconate dehydrogenase; gluconate 6-phosphate dehydrogenase; 6-phosphogluconate dehydrogenase (NAD); 2-keto-6-phosphogluconate reductase
Systematic name: 6-phospho-D-gluconate:NAD(P)+ 2-oxidoreductase
References:
1.  Frampton, E.W. and Wood, W.A. Carbohydrate oxidation by Pseudomonas fluorescens. VI. Conversion of 2-keto-6-phosphogluconate to pyruvate. J. Biol. Chem. 236 (1961) 2571–2577. [PMID: 13894458]
[EC 1.1.1.43 created 1961]
 
 
EC 1.1.1.44     
Accepted name: phosphogluconate dehydrogenase (NADP+-dependent, decarboxylating)
Reaction: 6-phospho-D-gluconate + NADP+ = D-ribulose 5-phosphate + CO2 + NADPH + H+
Other name(s): phosphogluconic acid dehydrogenase; 6-phosphogluconic dehydrogenase; 6-phosphogluconic carboxylase; 6-phosphogluconate dehydrogenase (decarboxylating); 6-phospho-D-gluconate dehydrogenase
Systematic name: 6-phospho-D-gluconate:NADP+ 2-oxidoreductase (decarboxylating)
Comments: The enzyme participates in the oxidative branch of the pentose phosphate pathway, whose main purpose is to produce NADPH and pentose for biosynthetic reactions. Highly specific for NADP+. cf. EC 1.1.1.343, phosphogluconate dehydrogenase (NAD+-dependent, decarboxylating).
References:
1.  Dickens, F. and Glock, G.E. Direct oxidation of glucose-6-phosphate, 6-phosphogluconate and pentose-5-phosphate by enzymes of animal origin. Biochem. J. 50 (1951) 81–95. [PMID: 14904376]
2.  Pontremoli, S., de Flora, A., Grazi, E., Mangiarotti, G., Bonsignore, A. and Horecker, B.L. Purification and properties of β-L-hydroxy acid dehydrogenase. II. Isolation of β-keto-L-gluconic acid, an intermediate in L-xylulose biosynthesis. J. Biol. Chem. 236 (1961) 2975–2980. [PMID: 14487824]
3.  Scott, D.B.M. and Cohen, S.S. The oxidative pathway of carbohydrate metabolism in Escherichia coli. 1. The isolation and properties of glucose 6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase. Biochem. J. 55 (1953) 23–33. [PMID: 13093611]
4.  Scott, D.B.M. and Cohen, S.S. The oxidative pathway of carbohydrate metabolism in Escherichia coli. 5. Isolation and identification of ribulose phosphate produced from 6-phosphogluconate by the dehydrogenase of E. coli. Biochem. J. 65 (1957) 686–689. [PMID: 13426085]
5.  Bridges, R.B., Palumbo, M.P. and Wittenberger, C.L. Purification and properties of an NADP-specific 6-phosphogluconate dehydrogenase from Streptococcus faecalis. J. Biol. Chem. 250 (1975) 6093–6100. [PMID: 238996]
6.  Yoon, H., Anderson, C.D. and Anderson, B.M. Kinetic studies of Haemophilus influenzae 6-phosphogluconate dehydrogenase. Biochim. Biophys. Acta 994 (1989) 75–80. [PMID: 2783298]
7.  Zamboni, N., Fischer, E., Laudert, D., Aymerich, S., Hohmann, H.P. and Sauer, U. The Bacillus subtilis yqjI gene encodes the NADP+-dependent 6-P-gluconate dehydrogenase in the pentose phosphate pathway. J. Bacteriol. 186 (2004) 4528–4534. [PMID: 15231785]
[EC 1.1.1.44 created 1961, modified 2013]
 
 
EC 1.1.1.45     
Accepted name: L-gulonate 3-dehydrogenase
Reaction: L-gulonate + NAD+ = 3-dehydro-L-gulonate + NADH + H+
Other name(s): L-3-aldonate dehydrogenase; L-3-aldonic dehydrogenase; L-gulonic acid dehydrogenase; L-β-hydroxyacid dehydrogenase; L-β-hydroxy-acid-NAD-oxidoreductase; L-3-hydroxyacid dehydrogenase
Systematic name: L-gulonate:NAD+ 3-oxidoreductase
Comments: Also oxidizes other L-3-hydroxyacids.
References:
1.  Dworsky, P. and Hoffmann-Ostenhof, O. L-3-Aldonic acid dehydrogenase from Schwanniomyces occidentalis. Acta Biochim. Pol. 11 (1964) 269–277.
2.  Smiley, J.D. and Ashwell, G. Purification and properties of β-L-hydroxy acid dehydrogenase. II. Isolation of β-keto-L-gluconic acid, an intermediate in L-xylulose biosynthesis. J. Biol. Chem. 236 (1961) 357–364.
[EC 1.1.1.45 created 1961]
 
 
EC 1.1.1.46     
Accepted name: L-arabinose 1-dehydrogenase
Reaction: L-arabinose + NAD+ = L-arabinono-1,4-lactone + NADH + H+
Systematic name: L-arabinose:NAD+ 1-oxidoreductase
References:
1.  Weimberg, R. and Doudoroff, M. The oxidation of L-arabinose by Pseudomonas saccharophila. J. Biol. Chem. 217 (1955) 607–624. [PMID: 13271422]
[EC 1.1.1.46 created 1961]
 
 
EC 1.1.1.47     
Accepted name: glucose 1-dehydrogenase [NAD(P)+]
Reaction: D-glucose + NAD(P)+ = D-glucono-1,5-lactone + NAD(P)H + H+
Other name(s): D-glucose dehydrogenase (NAD(P)+); hexose phosphate dehydrogenase; β-D-glucose:NAD(P)+ 1-oxidoreductase; glucose 1-dehydrogenase
Systematic name: D-glucose:NAD(P)+ 1-oxidoreductase
Comments: This enzyme has similar activity with either NAD+ or NADP+. cf. EC 1.1.1.118, glucose 1-dehydrogenase (NAD+) and EC 1.1.1.119, glucose 1-dehydrogenase (NADP+).
References:
1.  Banauch, D., Brummer, W., Ebeling, W., Metz, H., Rindfrey, H., Lang, H., Leybold, K. and Rick, W. A glucose dehydrogenase for the determination of glucose concentrations in body fluids. Z. Klin. Chem. Klin. Biochem. 13 (1975) 101–107. [PMID: 810982]
2.  Brink, N.G. Beef liver glucose dehydrogenase. 1. Purification and properties. Acta Chem. Scand. 7 (1953) 1081–1089.
3.  Pauly, H.E. and Pfleiderer, G. D-Glucose dehydrogenase from Bacillus megaterium M 1286: purification, properties and structure. Hoppe-Seylers Z. Physiol. Chem. 356 (1975) 1613–1623. [PMID: 2530]
4.  Strecker, H.J. and Korkes, S. Glucose dehydrogenase. J. Biol. Chem. 196 (1952) 769–784. [PMID: 12981017]
5.  Thompson, R.E. and Carper, W.R. Glucose dehydrogenase from pig liver. I. Isolation and purification. Biochim. Biophys. Acta 198 (1970) 397–406. [PMID: 4392298]
6.  Fujita, Y., Ramaley, R. and Freese, E. Location and properties of glucose dehydrogenase in sporulating cells and spores of Bacillus subtilis. J. Bacteriol. 132 (1977) 282–293. [PMID: 21162]
[EC 1.1.1.47 created 1961, modified 2013]
 
 
EC 1.1.1.48     
Accepted name: D-galactose 1-dehydrogenase
Reaction: D-galactose + NAD+ = D-galactono-1,4-lactone + NADH + H+
Other name(s): D-galactose dehydrogenase; β-galactose dehydrogenase (ambiguous); NAD+-dependent D-galactose dehydrogenase
Systematic name: D-galactose:NAD+ 1-oxidoreductase
Comments: This enzyme is part of the De Ley-Doudoroff pathway, which is used by some bacteria during growth on D-galactose.
References:
1.  De Ley, J. and Doudoroff, M. The metabolism of D-galactose in Pseudomonas saccharophila. J. Biol. Chem. 227 (1957) 745–757. [PMID: 13462997]
2.  Hu, A.S.L. and Cline, A.L. The regulation of some sugar dehydrogenases in a pseudomonad. Biochim. Biophys. Acta 93 (1964) 237–245. [PMID: 14251301]
[EC 1.1.1.48 created 1961, modified 2011]
 
 
EC 1.1.1.49     
Accepted name: glucose-6-phosphate dehydrogenase (NADP+)
Reaction: D-glucose 6-phosphate + NADP+ = 6-phospho-D-glucono-1,5-lactone + NADPH + H+
Other name(s): NADP-glucose-6-phosphate dehydrogenase; Zwischenferment; D-glucose 6-phosphate dehydrogenase; glucose 6-phosphate dehydrogenase (NADP); NADP-dependent glucose 6-phosphate dehydrogenase; 6-phosphoglucose dehydrogenase; Entner-Doudoroff enzyme; glucose-6-phosphate 1-dehydrogenase; G6PDH; GPD; glucose-6-phosphate dehydrogenase
Systematic name: D-glucose-6-phosphate:NADP+ 1-oxidoreductase
Comments: The enzyme catalyses a step of the pentose phosphate pathway. The enzyme is specific for NADP+. cf. EC 1.1.1.363, glucose-6-phosphate dehydrogenase [NAD(P)+] and EC 1.1.1.388, glucose-6-phosphate dehydrogenase (NAD+).
References:
1.  Engel, H.J., Domschke, W., Alberti, M. and Domagk, G.F. Protein structure and enzymatic activity. II. Purification and properties of a crystalline glucose-6-phosphate dehydrogenase from Candida utilis. Biochim. Biophys. Acta 191 (1969) 509–516. [PMID: 5363983]
2.  Glaser, L. and Brown, D.H. Purification and properties of D-glucose-6-phosphate dehydrogenase. J. Biol. Chem. 216 (1955) 67–79. [PMID: 13252007]
3.  Julian, G.R., Wolfe, R.G. and Reithel, F.J. The enzymes of mammary gland. II. The preparation of glucose 6-phosphate dehydrogenase. J. Biol. Chem. 236 (1961) 754–758. [PMID: 13790996]
4.  Noltmann, E.A., Gubler, C.J. and Kuby, S.A. Glucose 6-phosphate dehydrogenase (Zwischenferment). I. Isolation of the crystalline enzyme from yeast. J. Biol. Chem. 236 (1961) 1225–1230. [PMID: 13729473]
5.  Miclet, E., Stoven, V., Michels, P.A., Opperdoes, F.R., Lallemand, J.-Y. and Duffieux, F. NMR spectroscopic analysis of the first two steps of the pentose-phosphate pathway elucidates the role of 6-phosphogluconolactonase. J. Biol. Chem. 276 (2001) 34840–34846. [PMID: 11457850]
6.  Olavarria, K., Valdes, D. and Cabrera, R. The cofactor preference of glucose-6-phosphate dehydrogenase from Escherichia coli – modeling the physiological production of reduced cofactors. FEBS J. 279 (2012) 2296–2309. [PMID: 22519976]
7.  Hansen, T., Schlichting, B. and Schonheit, P. Glucose-6-phosphate dehydrogenase from the hyperthermophilic bacterium Thermotoga maritima: expression of the g6pd gene and characterization of an extremely thermophilic enzyme. FEMS Microbiol. Lett. 216 (2002) 249–253. [PMID: 12435510]
8.  Ibraheem, O., Adewale, I.O. and Afolayan, A. Purification and properties of glucose 6-phosphate dehydrogenase from Aspergillus aculeatus. J. Biochem. Mol. Biol. 38 (2005) 584–590. [PMID: 16202239]
9.  Iyer, R.B., Wang, J. and Bachas, L.G. Cloning, expression, and characterization of the gsdA gene encoding thermophilic glucose-6-phosphate dehydrogenase from Aquifex aeolicus. Extremophiles 6 (2002) 283–289. [PMID: 12215813]
10.  Cho, S.W. and Joshi, J.G. Characterization of glucose-6-phosphate dehydrogenase isozymes from human and pig brain. Neuroscience 38 (1990) 819–828. [PMID: 2270145]
[EC 1.1.1.49 created 1961, modified 2013, modified 2015]
 
 
EC 1.1.1.50     
Accepted name: 3α-hydroxysteroid 3-dehydrogenase (Si-specific)
Reaction: a 3α-hydroxysteroid + NAD(P)+ = a 3-oxosteroid + NAD(P)H + H+
Other name(s): hydroxyprostaglandin dehydrogenase; 3α-hydroxysteroid oxidoreductase; sterognost 3α; 3α-hydroxysteroid dehydrogenase (B-specific); 3α-hydroxysteroid 3-dehydrogenase (B-specific); 3α-hydroxysteroid:NAD(P)+ 3-oxidoreductase (B-specific)
Systematic name: 3α-hydroxysteroid:NAD(P)+ 3-oxidoreductase (Si-specific)
Comments: The enzyme acts on androsterone and other 3α-hydroxysteroids and on 9-, 11- and 15-hydroxyprostaglandin. Si-specific with respect to NAD+ or NADP+. cf. EC 1.1.1.213, 3α-hydroxysteroid 3-dehydrogenase (Re-specific).
References:
1.  Jarabak, J. and Talalay, P. Stereospecificity of hydrogen transfer by pyridine nucleotide-linked hydroxysteroid hydrogenase. J. Biol. Chem. 235 (1960) 2147–2151. [PMID: 14406805]
2.  Kochakian, C.D., Carroll, B.R. and Uhri, B. Comparisons of the oxidation of C19-hydroxysteroids by guinea pig liver homogenates. J. Biol. Chem. 224 (1957) 811–818. [PMID: 13405910]
3.  Marcus, P.I. and Talalay, P. Induction and purification of α- and β-hydroxysteroid dehydrogenases. J. Biol. Chem. 218 (1956) 661–674. [PMID: 13295221]
4.  Penning, T.M. and Sharp, R.B. Prostaglandin dehydrogenase activity of purified rat liver 3α-hydroxysteroid dehydrogenase. Biochem. Biophys. Res. Commun. 148 (1987) 646–652. [PMID: 3479982]
[EC 1.1.1.50 created 1961, modified 1986, modified 1990, modified 2012, modified 2013]
 
 
EC 1.1.1.51     
Accepted name: 3(or 17)β-hydroxysteroid dehydrogenase
Reaction: testosterone + NAD(P)+ = androstenedione + NAD(P)H + H+
Glossary: androstenedione = androst-4-ene-3,17-dione
Other name(s): β-hydroxy steroid dehydrogenase; 17-ketoreductase; 17β-hydroxy steroid dehydrogenase; 3β-hydroxysteroid dehydrogenase; 3β-hydroxy steroid dehydrogenase
Systematic name: 3(or 17)β-hydroxysteroid:NAD(P)+ oxidoreductase
Comments: Also acts on other 3β- or 17β-hydroxysteroids. cf. EC 1.1.1.209 3(or 17)α-hydroxysteroid dehydrogenase.
References:
1.  Dahm, K. and Breuer, H. Anreicherung einer 17β-hydroxysteroid:NAD(P)-oxydoreduktase aus der Nebenniere der Ratte. Hoppe-Seyler's Z. Physiol. Chem. 336 (1964) 63–68. [PMID: 14214322]
2.  Lynn, W.S. and Brown, R.H. The conversion of progesterone to androgens by testes. J. Biol. Chem. 232 (1958) 1015–1030. [PMID: 13549484]
3.  Marcus, P.I. and Talalay, P. Induction and purification of α- and β-hydroxysteroid dehydrogenases. J. Biol. Chem. 218 (1956) 661–674. [PMID: 13295221]
4.  Schultz, R.M., Groman, F.V. and Engel, L.L. 3(17)β-Hydroxysteroid dehydrogenase of Pseudomonas testosteroni. A convenient purification and demonstration of multiple molecular forms. J. Biol. Chem. 252 (1977) 3775–3783. [PMID: 193845]
5.  Talalay, P. and Dobson, M.M. Purification and properties of a α-hydroxysteroid dehydrogenase. J. Biol. Chem. 205 (1953) 823–837. [PMID: 13129261]
[EC 1.1.1.51 created 1961]
 
 
EC 1.1.1.52     
Accepted name: 3α-hydroxycholanate dehydrogenase (NAD+)
Reaction: lithocholate + NAD+ = 3-oxo-5β-cholan-24-oate + NADH + H+
Glossary: lithocholate = 3α-hydroxy-5β-cholan-24-oate
Other name(s): α-hydroxy-cholanate dehydrogenase; lithocholate:NAD+ oxidoreductase; 3α-hydroxycholanate dehydrogenase
Systematic name: lithocholate:NAD+ 3-oxidoreductase
Comments: Also acts on other 3α-hydroxysteroids with an acidic side-chain. cf. EC 1.1.1.392, 3α-hydroxycholanate dehydrogenase (NADP+).
References:
1.  Hayaishi, O., Saito, Y., Jakoby, W.B. and Stohlman, E.F. Reversible enzymatic oxidation of bile acids. Arch. Biochem. Biophys. 56 (1955) 554–555. [PMID: 14377608]
[EC 1.1.1.52 created 1961, modified 1976, modified 2016]
 
 
EC 1.1.1.53     
Accepted name: 3α(or 20β)-hydroxysteroid dehydrogenase
Reaction: androstan-3α,17β-diol + NAD+ = 17β-hydroxyandrostan-3-one + NADH + H+
Other name(s): cortisone reductase; (R)-20-hydroxysteroid dehydrogenase; 20β-hydroxy steroid dehydrogenase; Δ4-3-ketosteroid hydrogenase; 20β-hydroxysteroid dehydrogenase; 3α,20β-hydroxysteroid:NAD+-oxidoreductase; NADH-20β-hydroxysteroid dehydrogenase; 20β-HSD
Systematic name: 3α(or 20β)-hydroxysteroid:NAD+ oxidoreductase
Comments: The 3α-hydroxy group or 20β-hydroxy group of pregnane and androstane steroids can act as donor.
References:
1.  Edwards, C.A.F. and Orr, J.C. Comparison of the 3α-and 20β-hydroxysteroid dehydrogenase activities of the cortisone reductase of Streptomyces hydrogenans. Biochemistry 17 (1978) 4370–4376. [PMID: 718844]
2.  Hübener, H.J. and Sahrholz, F.G. 20β-hydroxy-steroid-dehydrogenase. II. Darstellung und Kristallisation. Biochem. Z. 333 (1960) 95–105. [PMID: 14403761]
3.  Hübener, H.J., Sahrholz, F.G., Schmidt-Thomé, J., Nesemann, G. and Junk, R. 20β-Hydroxy-Steroid-Dehydrogenase, ein neues kristallines Enzym. Biochim. Biophys. Acta 35 (1959) 270–272. [PMID: 14403760]
4.  Lynn, W.S. and Brown, R.H. The conversion of progesterone to androgens by testes. J. Biol. Chem. 232 (1958) 1015–1030. [PMID: 13549484]
5.  Strickler, R.C., Covey, D.F. and Tobias, B. Study of 3α, 20 β-hydroxysteroid dehydrogenase with an enzyme-generated affinity alkylator: dual enzyme activity at a single active site. Biochemistry 19 (1980) 4950–4954. [PMID: 6936053]
6.  Sweet, F. and Samant, B.S. Bifunctional enzyme activity at the same active site: study of 3α and 20β activity by affinity alkylation of 3α, 20β-hydroxysteroid dehydrogenase with 17-(bromoacetoxy)steroids. Biochemistry 19 (1980) 978–986. [PMID: 6928375]
[EC 1.1.1.53 created 1961, modified 1986]
 
 
EC 1.1.1.54     
Accepted name: allyl-alcohol dehydrogenase
Reaction: allyl alcohol + NADP+ = acrolein + NADPH + H+
Systematic name: allyl-alcohol:NADP+ oxidoreductase
Comments: Also acts on saturated primary alcohols.
References:
1.  Otsuka, K. Triphosphopyridine nucleotide-allyl and -ethyl alcohol dehydrogenases from Escherichia coli. J. Gen. Appl. Microbiol. 4 (1958) 211–215.
[EC 1.1.1.54 created 1965]
 
 
EC 1.1.1.55     
Accepted name: lactaldehyde reductase (NADPH)
Reaction: propane-1,2-diol + NADP+ = L-lactaldehyde + NADPH + H+
Other name(s): lactaldehyde (reduced nicotinamide adenine dinucleotide phosphate) reductase; NADP-1,2-propanediol dehydrogenase; propanediol dehydrogenase; 1,2-propanediol:NADP+ oxidoreductase; lactaldehyde reductase (NADPH2)
Systematic name: propane-1,2-diol:NADP+ oxidoreductase
Comments: May be identical with EC 1.1.1.2 alcohol dehydrogenase (NADP+).
References:
1.  Gupta, N.K. and Robinson, W.G. The enzymatic conversion of lactaldehyde to propanediol. J. Biol. Chem. 235 (1960) 1609–1612. [PMID: 13830319]
[EC 1.1.1.55 created 1965]
 
 
EC 1.1.1.56     
Accepted name: ribitol 2-dehydrogenase
Reaction: ribitol + NAD+ = D-ribulose + NADH + H+
Other name(s): adonitol dehydrogenase; ribitol dehydrogenase A (wild type); ribitol dehydrogenase B (mutant enzyme with different properties); ribitol dehydrogenase D (mutant enzyme with different properties)
Systematic name: ribitol:NAD+ 2-oxidoreductase
References:
1.  Hollmann, S. and Touster, O. The L-xylulose-xylitol enzyme and other polyol dehydrogenases of guinea pig liver mitochondria. J. Biol. Chem. 225 (1957) 87–102. [PMID: 13416220]
2.  Nordlie, R.C. and Fromm, H.J. Ribitol dehydrogenase. II. Studies on the reaction mechanism. J. Biol. Chem. 234 (1959) 2523–2531. [PMID: 14427582]
3.  Wood, W.A., McDonough, M.J. and Jacobs, L.B. Ribitol and D-arabitol utilization by Aerobacter aerogenes. J. Biol. Chem. 236 (1961) 2190–2195. [PMID: 13786517]
[EC 1.1.1.56 created 1965]
 
 
EC 1.1.1.57     
Accepted name: fructuronate reductase
Reaction: D-mannonate + NAD+ = D-fructuronate + NADH + H+
Other name(s): mannonate oxidoreductase; mannonic dehydrogenase; D-mannonate dehydrogenase; D-mannonate:NAD oxidoreductase
Systematic name: D-mannonate:NAD+ 5-oxidoreductase
Comments: Also reduces D-tagaturonate.
References:
1.  Hickman, J. and Ashwell, G. Uronic acid metabolism in bacteria. II. Purification and properties of D-altronic acid and D-mannonic acid dehyrogenases in Escherichia coli. J. Biol. Chem. 235 (1960) 1566–1570. [PMID: 14401695]
2.  Kilgore, W.W. and Starr, M.P. Catabolism of galacturonic and glucuronic acids by Erwinia carotovora. J. Biol. Chem. 234 (1959) 2227–2235. [PMID: 14409051]
[EC 1.1.1.57 created 1965]
 
 
EC 1.1.1.58     
Accepted name: tagaturonate reductase
Reaction: D-altronate + NAD+ = D-tagaturonate + NADH + H+
Other name(s): altronic oxidoreductase; altronate oxidoreductase; TagUAR; altronate dehydrogenase; D-tagaturonate reductase
Systematic name: D-altronate:NAD+ 3-oxidoreductase
References:
1.  Hickman, J. and Ashwell, G. Uronic acid metabolism in bacteria. II. Purification and properties of D-altronic acid and D-mannonic acid dehyrogenases in Escherichia coli. J. Biol. Chem. 235 (1960) 1566–1570. [PMID: 14401695]
[EC 1.1.1.58 created 1965]
 
 
EC 1.1.1.59     
Accepted name: 3-hydroxypropionate dehydrogenase
Reaction: 3-hydroxypropanoate + NAD+ = 3-oxopropanoate + NADH + H+
Systematic name: 3-hydroxypropanoate:NAD+ oxidoreductase
References:
1.  Den, H., Robinson, W.G. and Coon, M.J. Enzymatic conversion of β-hydroxypropionate to malonic semialdehyde. J. Biol. Chem. 234 (1959) 1666–1671. [PMID: 13672942]
[EC 1.1.1.59 created 1965]
 
 
EC 1.1.1.60     
Accepted name: 2-hydroxy-3-oxopropionate reductase
Reaction: D-glycerate + NAD(P)+ = 2-hydroxy-3-oxopropanoate + NAD(P)H + H+
Other name(s): tartronate semialdehyde reductase; (R)-glycerate:NAD(P)+ oxidoreductase
Systematic name: D-glycerate:NAD(P)+ oxidoreductase
References:
1.  Gotto, A.M. and Kornberg, H.L. The metabolism of C2 compounds in micro-organisms. 7. Preparation and properties of crystalline tartronic semialdehyde reductase. Biochem. J. 81 (1961) 273–284. [PMID: 13900766]
[EC 1.1.1.60 created 1965]
 
 
EC 1.1.1.61     
Accepted name: 4-hydroxybutyrate dehydrogenase
Reaction: 4-hydroxybutanoate + NAD+ = succinate semialdehyde + NADH + H+
Other name(s): γ-hydroxybutyrate dehydrogenase
Systematic name: 4-hydroxybutanoate:NAD+ oxidoreductase
References:
1.  Nirenberg, M.W. and Jakoby, W.B. Enzymatic utilization of γ-hydroxybutyric acid. J. Biol. Chem. 235 (1960) 954–960. [PMID: 14427301]
[EC 1.1.1.61 created 1965]
 
 
EC 1.1.1.62     
Accepted name: 17β-estradiol 17-dehydrogenase
Reaction: 17β-estradiol + NAD(P)+ = estrone + NAD(P)H + H+
Other name(s): 20α-hydroxysteroid dehydrogenase; 17β,20α-hydroxysteroid dehydrogenase; 17β-estradiol dehydrogenase; estradiol dehydrogenase; estrogen 17-oxidoreductase; 17β-HSD; HSD17B7
Systematic name: 17β-estradiol:NAD(P)+ 17-oxidoreductase
Comments: The enzyme oxidizes or reduces the hydroxy/keto group on C17 of estrogens and androgens in mammals and regulates the biological potency of these steroids. The mammalian enzyme is bifunctional and also catalyses EC 1.1.1.270, 3β-hydroxysteroid 3-dehydrogenase [3]. The enzyme also acts on (S)-20-hydroxypregn-4-en-3-one and related compounds, oxidizing the (S)-20-group, but unlike EC 1.1.1.149, 20α-hydroxysteroid dehydrogenase, it is Si-specific with respect to NAD(P)+.
References:
1.  Kautsky, M.P. and Hagerman, D.D. 17β-Estradiol dehydrogenase of ovine ovaries. J. Biol. Chem. 245 (1970) 1978–1984. [PMID: 4314937]
2.  Langer, L.J., Alexander, J.A. and Engel, L.L. Human placental estradiol-17β dehydrogenase. II. Kinetics and substrate specificities. J. Biol. Chem. 234 (1959) 2609–2614. [PMID: 14413943]
3.  Marijanovic, Z., Laubner, D., Moller, G., Gege, C., Husen, B., Adamski, J. and Breitling, R. Closing the gap: identification of human 3-ketosteroid reductase, the last unknown enzyme of mammalian cholesterol biosynthesis. Mol. Endocrinol. 17 (2003) 1715–1725. [PMID: 12829805]
[EC 1.1.1.62 created 1965, modified 1983, modified 1986, modified 2012]
 
 
EC 1.1.1.63      
Transferred entry: testosterone 17β-dehydrogenase. Now EC 1.1.1.239, 3α(17β)-hydroxysteroid dehydrogenase (NAD+)
[EC 1.1.1.63 created 1965, deleted 2012]
 
 
EC 1.1.1.64     
Accepted name: testosterone 17β-dehydrogenase (NADP+)
Reaction: testosterone + NADP+ = androstenedione + NADPH + H+
Glossary: androstenedione = androst-4-ene-3,17-dione
Other name(s): 17-ketoreductase; NADP-dependent testosterone-17β-oxidoreductase; testosterone 17β-dehydrogenase (NADP)
Systematic name: 17β-hydroxysteroid:NADP+ 17-oxidoreductase
Comments: Also oxidizes 3-hydroxyhexobarbital to 3-oxohexobarbital.
References:
1.  Endahl, G.L., Kochakia, C.D. and Hamm, D. Separation of a triphosphopyridine nucleotide-specific from a diphosphopyridine-specific 17β-hydroxy (testosterone) dehydrogenase of guinea pig liver. J. Biol. Chem. 235 (1960) 2792–2796. [PMID: 13696735]
2.  Sweat, M.L., Samuels, L.T. and Lumry, R. Preparation and characterisation of the enzyme which converts testosterone to androstendione. J. Biol. Chem. 185 (1950) 75–84. [PMID: 15436478]
3.  Villee, C.A. and Spencer, J.M. Some properties of the pyridine nucleotide-specific 17β-hydroxy steroid dehydrogenase of guinea pig liver. J. Biol. Chem. 235 (1960) 3615–3619. [PMID: 13781425]
[EC 1.1.1.64 created 1965]
 
 
EC 1.1.1.65     
Accepted name: pyridoxine 4-dehydrogenase
Reaction: pyridoxine + NADP+ = pyridoxal + NADPH + H+
Other name(s): pyridoxin dehydrogenase; pyridoxol dehydrogenase; pyridoxine dehydrogenase
Systematic name: pyridoxine:NADP+ 4-oxidoreductase
Comments: Also oxidizes pyridoxine phosphate.
References:
1.  Holzer, H. and Schneider, S. Reinigung und charakterisierung einer TPN-abhängigen Pyridoxol-dehydrogenase aus bierhefe. Biochim. Biophys. Acta 48 (1961) 71–76. [PMID: 13715611]
[EC 1.1.1.65 created 1965, modified 1976]
 
 
EC 1.1.1.66     
Accepted name: ω-hydroxydecanoate dehydrogenase
Reaction: 10-hydroxydecanoate + NAD+ = 10-oxodecanoate + NADH + H+
Systematic name: 10-hydroxydecanoate:NAD+ 10-oxidoreductase
Comments: Also acts, more slowly, on 9-hydroxynonanoate and 11-hydroxyundecanoate.
References:
1.  Kamei, S., Wakabayashi, K. and Shimazono, M. ω-Oxidation of fatty acids in vitro. II. ω-Hydroxy fatty acid-NAD oxidoreductase. J. Biochem. (Tokyo) 56 (1964) 72–76. [PMID: 14202238]
2.  Mitz, M.A. and Henrikson, R.L. Omega hydroxy fatty acid dehydrogenase. Biochim. Biophys. Acta 46 (1961) 45–50. [PMID: 13771448]
[EC 1.1.1.66 created 1965]
 
 
EC 1.1.1.67     
Accepted name: mannitol 2-dehydrogenase
Reaction: D-mannitol + NAD+ = D-fructose + NADH + H+
Other name(s): D-mannitol dehydrogenase; mannitol dehydrogenase
Systematic name: D-mannitol:NAD+ 2-oxidoreductase
References:
1.  Martinez, G., Barker, H.A. and Horecker, B.L. A specific mannitol dehydrogenase from Lactobacillus brevis. J. Biol. Chem. 238 (1963) 1598–1603.
[EC 1.1.1.67 created 1965]
 
 
EC 1.1.1.68      
Transferred entry: 5,10-methylenetetrahydrofolate reductase. Now EC 1.5.1.20, methylenetetrahydrofolate reductase [NAD(P)H]
[EC 1.1.1.68 created 1965, deleted 1978 [transferred to EC 1.1.99.15, deleted 1980]]
 
 
EC 1.1.1.69     
Accepted name: gluconate 5-dehydrogenase
Reaction: D-gluconate + NAD(P)+ = 5-dehydro-D-gluconate + NAD(P)H + H+
Other name(s): 5-keto-D-gluconate 5-reductase; 5-keto-D-gluconate 5-reductase; 5-ketogluconate 5-reductase; 5-ketogluconate reductase; 5-keto-D-gluconate reductase
Systematic name: D-gluconate:NAD(P)+ 5-oxidoreductase
References:
1.  Ameyama, M. and Adachi, O. 5-Keto-D-gluconate reductase from Gluconobacter suboxydans. Methods Enzymol. 89 (1982) 198–202.
2.  De Ley, J. 5-Ketogluconic acid reductase. Methods Enzymol. 9 (1966) 200–203.
3.  Okamoto, K. Enzymic studies on the formation of 5-ketogluconic acid by Acetobacter suboxydans. II. 5-Ketogluconate reductase. J. Biochem. (Tokyo) 53 (1963) 448. [PMID: 13939777]
[EC 1.1.1.69 created 1965, modified 1976]
 
 
EC 1.1.1.70      
Deleted entry:  D-glucuronolactone dehydrogenase. Now included with EC 1.2.1.3 aldehyde dehydrogenase (NAD+)
[EC 1.1.1.70 created 1965, deleted 1978]
 
 
EC 1.1.1.71     
Accepted name: alcohol dehydrogenase [NAD(P)+]
Reaction: an alcohol + NAD(P)+ = an aldehyde + NAD(P)H + H+
Other name(s): retinal reductase (ambiguous); aldehyde reductase (NADPH/NADH); alcohol dehydrogenase [NAD(P)]
Systematic name: alcohol:NAD(P)+ oxidoreductase
Comments: Reduces aliphatic aldehydes of carbon chain length from 2 to 14, with greatest activity on C4, C6 and C8 aldehydes; also reduces retinal to retinol.
References:
1.  Fidge, N.H. and Goodman, D.S. The enzymatic reduction of retinal to retinol in rat intestine. J. Biol. Chem. 243 (1968) 4372–4379. [PMID: 4300551]
[EC 1.1.1.71 created 1972]
 
 
EC 1.1.1.72     
Accepted name: glycerol dehydrogenase (NADP+)
Reaction: glycerol + NADP+ = D-glyceraldehyde + NADPH + H+
Other name(s): glycerol dehydrogenase (NADP)
Systematic name: glycerol:NADP+ oxidoreductase
References:
1.  Kormann, A.W., Hurst, R.O. and Flynn, T.G. Purification and properties of an NADP+-dependent glycerol dehydrogenase from rabbit skeletal muscle. Biochim. Biophys. Acta 258 (1972) 40–55. [PMID: 4400494]
2.  Toews, C.J. The kinetics and reaction mechanism of the nicotinamide-adinine dinucleotide phosphate-specific glycerol dehydrogenase of rat skeletal muscle. Biochem. J. 105 (1967) 1067–1073. [PMID: 16742532]
[EC 1.1.1.72 created 1972]
 
 
EC 1.1.1.73     
Accepted name: octanol dehydrogenase
Reaction: octan-1-ol + NAD+ = octanal + NADH + H+
Other name(s): 1-octanol dehydrogenase; octanol:NAD+ oxidoreductase
Systematic name: octan-1-ol:NAD+ oxidoreductase
Comments: Acts, less rapidly, on other long-chain alcohols.
References:
1.  Roche, B. and Azoulay, E. Régulation des alcool-déshydrogénases chez Saccharomyces cerevisiae. Eur. J. Biochem. 8 (1969) 426–434. [PMID: 4308448]
[EC 1.1.1.73 created 1972]
 
 
EC 1.1.1.74      
Deleted entry:  D-aminopropanol dehydrogenase (reaction due to EC 1.1.1.4 (R,R)-butanediol dehydrogenase)
[EC 1.1.1.74 created 1972, deleted 1976]
 
 
EC 1.1.1.75     
Accepted name: (R)-aminopropanol dehydrogenase
Reaction: (R)-1-aminopropan-2-ol + NAD+ = aminoacetone + NADH + H+
Other name(s): L-aminopropanol dehydrogenase; 1-aminopropan-2-ol-NAD+ dehydrogenase; L(+)-1-aminopropan-2-ol:NAD+ oxidoreductase; 1-aminopropan-2-ol-dehydrogenase; DL-1-aminopropan-2-ol: NAD+ dehydrogenase; L(+)-1-aminopropan-2-ol-NAD/NADP oxidoreductase
Systematic name: (R)-1-aminopropan-2-ol:NAD+ oxidoreductase
Comments: Requires K+.
References:
1.  Dekker, E.E. and Swain, R.R. Formation of Dg-1-amino-2-propanol by a highly purified enzyme from Escherichia coli. Biochim. Biophys. Acta 158 (1968) 306–307. [PMID: 4385233]
2.  Turner, J.M. Microbial metabolism of amino ketones. Aminoacetone formation from 1-aminopropan-2-ol by a dehydrgenase in Escherichia coli. Biochem. J. 99 (1966) 427–433. [PMID: 5329339]
3.  Turner, J.M. Microbial metabolism of amino ketones. L-1-Aminopropan-2-ol dehydrogenase and L-threonine dehydrogenase in Escherichia coli. Biochem. J. 104 (1967) 112–121. [PMID: 5340733]
[EC 1.1.1.75 created 1972]
 
 
EC 1.1.1.76     
Accepted name: (S,S)-butanediol dehydrogenase
Reaction: (2S,3S)-butane-2,3-diol + NAD+ = (S)-acetoin + NADH + H+
Other name(s): L-butanediol dehydrogenase; L-BDH; L(+)-2,3-butanediol dehydrogenase (L-acetoin forming); (S)-acetoin reductase [(S,S)-butane-2,3-diol forming]
Systematic name: (S,S)-butane-2,3-diol:NAD+ oxidoreductase
Comments: This enzyme catalyses the reversible reduction of (S)-acetoin to (S,S)-butane-2,3-diol. It can also catalyse the irreversible reduction of diacetyl to (S)-acetoin.
References:
1.  Taylor, M.B. and Juni, E. Stereoisomeric specificities of 2,3-butanediol dehydrogenase. Biochim. Biophys. Acta 39 (1960) 448–457. [PMID: 13837186]
2.  Carballo, J., Martin, R., Bernardo, A. and Gonzalez, J. Purification, characterization and some properties of diacetyl(acetoin) reductase from Enterobacter aerogenes. Eur. J. Biochem. 198 (1991) 327–332. [PMID: 2040298]
3.  Takusagawa, Y., Otagiri, M., Ui, S., Ohtsuki, T., Mimura, A., Ohkuma, M. and Kudo, T. Purification and characterization of L-2,3-butanediol dehydrogenase of Brevibacterium saccharolyticum C-1012 expressed in Escherichia coli. Biosci. Biotechnol. Biochem. 65 (2001) 1876–1878. [PMID: 11577733]
[EC 1.1.1.76 created 1972, modified 2010]
 
 
EC 1.1.1.77     
Accepted name: lactaldehyde reductase
Reaction: (R)[or (S)]-propane-1,2-diol + NAD+ = (R)[or (S)]-lactaldehyde + NADH + H+
Other name(s): propanediol:nicotinamide adenine dinucleotide (NAD) oxidoreductase; L-lactaldehyde:propanediol oxidoreductase
Systematic name: (R)[or (S)]-propane-1,2-diol:NAD+ oxidoreductase
References:
1.  Ting, S.-M., Sellinger, O.Z. and Miller, O.N. The metabolism of lactaldehyde. VI. The reduction of D- and L-lactaldehyde in rat liver. Biochim. Biophys. Acta 89 (1964) 217–225. [PMID: 14203169]
[EC 1.1.1.77 created 1972]
 
 
EC 1.1.1.78     
Accepted name: methylglyoxal reductase (NADH)
Reaction: (R)-lactaldehyde + NAD+ = 2-oxopropanal + NADH + H+
Glossary: 2-oxopropanal = methylglyoxal
Other name(s): methylglyoxal reductase; D-lactaldehyde dehydrogenase; methylglyoxal reductase (NADH-dependent)
Systematic name: (R)-lactaldehyde:NAD+ oxidoreductase
Comments: This mammalian enzyme differs from the yeast enzyme, EC 1.1.1.283, methylglyoxal reductase (NADPH-dependent), by its coenzyme requirement, reaction direction, and enantiomeric preference.
References:
1.  Ting, S.-M., Miller, O.N. and Sellinger, O.Z. The metabolism of lactaldehyde. VII. The oxidation of D-lactaldehyde in rat liver. Biochim. Biophys. Acta 97 (1965) 407–415. [PMID: 14323585]
2.  Ray, M. and Ray, S. Purification and partial characterization of a methylglyoxal reductase from goat liver. Biochim. Biophys. Acta 802 (1984) 119–127. [PMID: 6386056]
[EC 1.1.1.78 created 1972, modified 2005, modified 2013]
 
 
EC 1.1.1.79     
Accepted name: glyoxylate reductase (NADP+)
Reaction: glycolate + NADP+ = glyoxylate + NADPH + H+
Other name(s): NADPH-glyoxylate reductase; glyoxylate reductase (NADP)
Systematic name: glycolate:NADP+ oxidoreductase
Comments: Also reduces hydroxypyruvate to glycerate; has some affinity for NAD+.
References:
1.  Cartwright, L.N. and Hullin, R.P. Purification and properties of two glyoxylate reductases from a species of Pseudomonas. Biochem. J. 101 (1966) 781–791. [PMID: 16742459]
2.  Kleczkowski, L.A., Randall, D.D. and Blevins, D.G. Purification and characterization of a novel NADPH(NADH)-dependent glyoxylate reductase from spinach leaves. Comparison of immunological properties of leaf glyoxylate reductase and hydroxypyruvate reductase. Biochem. J. 239 (1986) 653–659. [PMID: 3548703]
[EC 1.1.1.79 created 1972]
 
 
EC 1.1.1.80     
Accepted name: isopropanol dehydrogenase (NADP+)
Reaction: propan-2-ol + NADP+ = acetone + NADPH + H+
Other name(s): isopropanol dehydrogenase (NADP)
Systematic name: propan-2-ol:NADP+ oxidoreductase
Comments: Also acts on other short-chain secondary alcohols and, slowly, on primary alcohols.
References:
1.  Hoshino, K. Organism producing isopropanol from acetone. V. Enzymological [studies] on the oxidation-reduction of Lactobacillus brevis var. hofuensis. [in Japanese] Nippon Nogei Kagaku Kaishi 34 (1960) 608–615.
2.  Hoshino, K. and Udagawa, K. Organism producing isopropanol from acetone. VI. Isopropanol dehydrogenase and alcohol dehydrogenase of Lactobacillus brevis var. hofuensis. [in Japanese] Nippon Nogei Kagaku Kaishi 34 (1960) 616–619.
[EC 1.1.1.80 created 1972]
 
 
EC 1.1.1.81     
Accepted name: hydroxypyruvate reductase
Reaction: D-glycerate + NAD(P)+ = hydroxypyruvate + NAD(P)H + H+
Other name(s): β-hydroxypyruvate reductase; NADH:hydroxypyruvate reductase; D-glycerate dehydrogenase
Systematic name: D-glycerate:NADP+ 2-oxidoreductase
References:
1.  Kleczkowski, L.A. and Edwards, G.E. Identification of hydroxypyruvate and glyoxylate reductases in maize leaves. Plant Physiol. 91 (1989) 278–286. [PMID: 16667010]
2.  Kleczkowski, L.A. and Randall, D.D. Purification and characterization of a novel NADPH(NADH)-dependent hydroxypyruvate reductase from spinach leaves. Comparison of immunological properties of leaf hydroxypyruvate reductases. Biochem. J. 250 (1988) 145–152. [PMID: 3281657]
3.  Kohn, L.D. and Jakoby, W.B. Tartaric acid metabolism. VII. Crystalline hydroxypyruvate reductase (D-glycerate dehydrogenase). J. Biol. Chem. 243 (1968) 2494–2499. [PMID: 4385077]
[EC 1.1.1.81 created 1972]
 
 
EC 1.1.1.82     
Accepted name: malate dehydrogenase (NADP+)
Reaction: (S)-malate + NADP+ = oxaloacetate + NADPH + H+
Other name(s): NADP-malic enzyme; NADP-malate dehydrogenase; malic dehydrogenase (nicotinamide adenine dinucleotide phosphate); malate NADP dehydrogenase; NADP malate dehydrogenase; NADP-linked malate dehydrogenase; malate dehydrogenase (NADP)
Systematic name: (S)-malate:NADP+ oxidoreductase
Comments: Activated by light.
References:
1.  Connelly, J.L., Danner, D.J. and Bowden, J.A. Branched chain α-keto acid metabolism. I. Isolation, purification, and partial characterization of bovine liver α-ketoisocaproic:α-keto-β-methylvaleric acid dehydrogenase. J. Biol. Chem. 243 (1968) 1198–1203. [PMID: 5689906]
2.  Johnson, H.S. NADP-malate dehydrogenase: photoactivation in leaves of plants with Calvin cycle photosynthesis. Biochem. Biophys. Res. Commun. 43 (1971) 703–709. [PMID: 4397919]
3.  Johnson, H.S. and Hatch, M.D. Properties and regulation of leaf nicotinamide-adenine dinucleotide phosphate-malate dehydrogenase and 'malic' enzyme in plants with the C4-dicarboxylic acid pathway of photosynthesis. Biochem. J. 119 (1970) 273–280. [PMID: 4395182]
[EC 1.1.1.82 created 1972]
 
 
EC 1.1.1.83     
Accepted name: D-malate dehydrogenase (decarboxylating)
Reaction: (R)-malate + NAD+ = pyruvate + CO2 + NADH
Other name(s): D-malate dehydrogenase; D-malic enzyme; bifunctional L(+)-tartrate dehydrogenase-D(+)-malate (decarboxylating)
Systematic name: (R)-malate:NAD+ oxidoreductase (decarboxylating)
References:
1.  Stern, J.R. and O'Brien, R.W. Oxidation D-malic and β-alkylmalic acids wild-type and mutant strains of Salmonella typhimurium and by Aerobacter aerogenes. J. Bacteriol. 98 (1969) 147–151. [PMID: 4889267]
[EC 1.1.1.83 created 1972]
 
 
EC 1.1.1.84     
Accepted name: dimethylmalate dehydrogenase
Reaction: (R)-3,3-dimethylmalate + NAD+ = 3-methyl-2-oxobutanoate + CO2 + NADH
Other name(s): β,β-dimethylmalate dehydrogenase
Systematic name: (R)-3,3-dimethylmalate:NAD+ oxidoreductase (decarboxylating)
Comments: Requires K+ or NH4+ and Mn2+ or Co2+; also acts on (R)-malate.
References:
1.  Magee, P.T. and Snell, E.E. The bacterial degradation of pantothenic acid. IV. Enzymatic conversion of aldopantoate to α-ketoisovalerate. Biochemistry 5 (1966) 409–416. [PMID: 4287371]
[EC 1.1.1.84 created 1972]
 
 
EC 1.1.1.85     
Accepted name: 3-isopropylmalate dehydrogenase
Reaction: (2R,3S)-3-isopropylmalate + NAD+ = 4-methyl-2-oxopentanoate + CO2 + NADH + H+ (overall reaction)
(1a) (2R,3S)-3-isopropylmalate + NAD+ = (2S)-2-isopropyl-3-oxosuccinate + NADH + H+
(1b) (2S)-2-isopropyl-3-oxosuccinate = 4-methyl-2-oxopentanoate + CO2 (spontaneous)
Other name(s): β-isopropylmalic enzyme; β-isopropylmalate dehydrogenase; threo-Ds-3-isopropylmalate dehydrogenase; 3-carboxy-2-hydroxy-4-methylpentanoate:NAD+ oxidoreductase
Systematic name: (2R,3S)-3-isopropylmalate:NAD+ oxidoreductase
Comments: The product decarboxylates spontaneously to yield 4-methyl-2-oxopentanoate.
References:
1.  Burns, R.O., Umbarger, H.E. and Gross, S.R. The biosynthesis of leucine. III. The conversion of α-hydroxy-β-carboxyisocaproate to α-ketoisocaproate. Biochemistry 2 (1963) 1053. [PMID: 14087358]
2.  Parsons, S.J. and Burns, R.O. Purification and properties of β-isopropylmalate dehydrogenase. J. Biol. Chem. 244 (1969) 996–1003. [PMID: 4889950]
3.  Németh, A., Svingor, Á., Pócsik, M., Dobó, J., Magyar, C, Szilaaagyi, A., Gál, P. and Závodszky, P. Mirror image mutations reveal the significance of an intersubunit ion cluster in the stability of 3-isopropylmalate dehydrogenase. FEBS Lett. 468 (2000) 48–52. [PMID: 10683439]
4.  Calvo, J. M., Stevens, C. M., Kalyanpur, M. G., and Umbarger, H. E. The absolute configuration of α-hydroxy-β-carboxyisocaproic acid (3-isopropylmalic acid), an intermediate in leucine biosynthesis. Biochemistry 3 (1964) 2024–2027. [PMID: 14269331]
[EC 1.1.1.85 created 1972, modified 1976]
 
 
EC 1.1.1.86     
Accepted name: ketol-acid reductoisomerase (NADP+)
Reaction: (2R)-2,3-dihydroxy-3-methylbutanoate + NADP+ = (2S)-2-hydroxy-2-methyl-3-oxobutanoate + NADPH + H+
Glossary: (2S)-2-hydroxy-2-methyl-3-oxobutanoate = (2S)-2-acetolactate
Other name(s): dihydroxyisovalerate dehydrogenase (isomerizing); acetohydroxy acid isomeroreductase; ketol acid reductoisomerase; α-keto-β-hydroxylacyl reductoisomerase; 2-hydroxy-3-keto acid reductoisomerase; acetohydroxy acid reductoisomerase; acetolactate reductoisomerase; dihydroxyisovalerate (isomerizing) dehydrogenase; isomeroreductase; reductoisomerase; ketol-acid reductoisomerase; (R)-2,3-dihydroxy-3-methylbutanoate:NADP+ oxidoreductase (isomerizing)
Systematic name: (2R)-2,3-dihydroxy-3-methylbutanoate:NADP+ oxidoreductase (isomerizing)
Comments: Also catalyses the reduction of 2-ethyl-2-hydroxy-3-oxobutanoate to 2,3-dihydroxy-3-methylpentanoate. The enzyme, found in many bacteria and archaea, is specific for NADPH (cf. EC 1.1.1.382, ketol-acid reductoisomerase (NAD+) and EC 1.1.1.383, ketol-acid reductoisomerase [NAD(P)+]).
References:
1.  Arfin, S.M. and Umbarger, H.E. Purification and properties of the acetohydroxy acid isomeroreductase of Salmonella typhimurium. J. Biol. Chem. 244 (1969) 1118–1127. [PMID: 4388025]
2.  Hill, R.K., Sawada, S. and Arfin, S.M. Stereochemistry of valine and isoleucine biosynthesis. IV. Synthesis, configuration, and enzymatic specificity of α-acetolactate and α-aceto-α-hydroxybutyrate. Bioorg. Chem. 8 (1979) 175–189.
3.  Kiritani, K., Narise, S. and Wagner, R.P. The reductoisomerase of Neurospora crassa. J. Biol. Chem. 241 (1966) 2047–2051.
4.  Satyanarayana, T. and Radhakrishnan, A.N. Biosynthesis of valine and isoleucine in plants. 3. Reductoisomerase of Phaseolus radiatus. Biochim. Biophys. Acta 110 (1965) 380–388. [PMID: 5866387]
5.  Brinkmann-Chen, S., Cahn, J.K. and Arnold, F.H. Uncovering rare NADH-preferring ketol-acid reductoisomerases. Metab. Eng. 26C (2014) 17–22. [PMID: 25172159]
[EC 1.1.1.86 created 1972, modified 1976, modified 1981 (EC 1.1.1.89 created 1972, incorporated 1976), modified 2015]
 
 
EC 1.1.1.87     
Accepted name: homoisocitrate dehydrogenase
Reaction: (1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate + NAD+ = 2-oxoadipate + CO2 + NADH + H+
Glossary: homoisocitrate = (-)-threo-homoisocitrate = (1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate
Other name(s): 2-hydroxy-3-carboxyadipate dehydrogenase; 3-carboxy-2-hydroxyadipate dehydrogenase; homoisocitric dehydrogenase; (-)-1-hydroxy-1,2,4-butanetricarboxylate:NAD+ oxidoreductase (decarboxylating); 3-carboxy-2-hydroxyadipate:NAD+ oxidoreductase (decarboxylating); HICDH
Systematic name: (1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate:NAD+ oxidoreductase (decarboxylating)
Comments: Forms part of the lysine biosynthesis pathway in fungi [3].
References:
1.  Strassman, M. and Ceci, L.N. Enzymatic formation of α-ketoadipic acid from homoisocitric acid. J. Biol. Chem. 240 (1965) 4357–4361. [PMID: 4284830]
2.  Rowley, B. and Tucci, A.F. Homoisocitric dehydrogenase from yeast. Arch. Biochem. Biophys. 141 (1970) 499–510. [PMID: 4395693]
3.  Zabriskie, T.M. and Jackson, M.D. Lysine biosynthesis and metabolism in fungi. Nat. Prod. Rep. 17 (2000) 85–97. [PMID: 10714900]
[EC 1.1.1.87 created 1972 (EC 1.1.1.155 created 1976, incorporated 2004)]
 
 
EC 1.1.1.88     
Accepted name: hydroxymethylglutaryl-CoA reductase
Reaction: (R)-mevalonate + CoA + 2 NAD+ = 3-hydroxy-3-methylglutaryl-CoA + 2 NADH + 2 H+
Other name(s): β-hydroxy-β-methylglutaryl coenzyme A reductase (ambiguous); β-hydroxy-β-methylglutaryl CoA-reductase (ambiguous); 3-hydroxy-3-methylglutaryl coenzyme A reductase (ambiguous); hydroxymethylglutaryl coenzyme A reductase (ambiguous)
Systematic name: (R)-mevalonate:NAD+ oxidoreductase (CoA-acylating)
References:
1.  Fimognari, G.M. and Rodwell, V.W. Substrate-competitive inhibition of bacterial mevalonate:nicotinamide-adenine dinucleotide oxidoreductase (acylating CoA). Biochemistry 4 (1965) 2086–2090.
[EC 1.1.1.88 created 1972, modified 2002]
 
 
EC 1.1.1.89      
Deleted entry:  dihydroxyisovalerate dehydrogenase (isomerizing). Now included with EC 1.1.1.86 ketol-acid reductoisomerase
[EC 1.1.1.89 created 1972, deleted 1976]
 
 
EC 1.1.1.90     
Accepted name: aryl-alcohol dehydrogenase
Reaction: an aromatic alcohol + NAD+ = an aromatic aldehyde + NADH + H+
Other name(s): p-hydroxybenzyl alcohol dehydrogenase; benzyl alcohol dehydrogenase; coniferyl alcohol dehydrogenase
Systematic name: aryl-alcohol:NAD+ oxidoreductase
Comments: A group of enzymes with broad specificity towards primary alcohols with an aromatic or cyclohex-1-ene ring, but with low or no activity towards short-chain aliphatic alcohols.
References:
1.  Suhara, K., Takemori, S. and Katagiri, M. The purification and properties of benzylalcohol dehydrogenase from Pseudomonas sp. Arch. Biochem. Biophys. 130 (1969) 422–429. [PMID: 5778658]
2.  Yamanaka, K. and Minoshima, R. Identification and characterization of a nicotinamide adenine dinucleotide-dependent para-hydroxybenzyl alcohol-dehydrogenase from Rhodopseudomonas acidophila M402. Agric. Biol. Chem. 48 (1984) 1161–1171.
[EC 1.1.1.90 created 1972, modified 1989]
 
 
EC 1.1.1.91     
Accepted name: aryl-alcohol dehydrogenase (NADP+)
Reaction: an aromatic alcohol + NADP+ = an aromatic aldehyde + NADPH + H+
Other name(s): aryl alcohol dehydrogenase (nicotinamide adenine dinucleotide phosphate); coniferyl alcohol dehydrogenase; NADPH-linked benzaldehyde reductase; aryl-alcohol dehydrogenase (NADP)
Systematic name: aryl-alcohol:NADP+ oxidoreductase
Comments: Also acts on some aliphatic aldehydes, but cinnamaldehyde was the best substrate found.
References:
1.  Gross, G.G. and Zenk, M.H. Reduktionaromatische Säuren zu Aldehyden und Alkoholen im zellfreien System. 2. Reinigung und Eigenschaften von Aryl Alkohol:NADP-Oxidoreductase aus Neurospora crassa. Eur. J. Biochem. 8 (1969) 420–425. [PMID: 4389864]
[EC 1.1.1.91 created 1972]
 
 
EC 1.1.1.92     
Accepted name: oxaloglycolate reductase (decarboxylating)
Reaction: D-glycerate + NAD(P)+ + CO2 = 2-hydroxy-3-oxosuccinate + NAD(P)H + 2 H+
Systematic name: D-glycerate:NAD(P)+ oxidoreductase (carboxylating)
Comments: Also reduces hydroxypyruvate to D-glycerate and glyoxylate to glycolate.
References:
1.  Kohn, L.D. and Jakoby, W.B. Tartaric acid metabolism. VI. Crystalline oxaloglycolate reductive decarboxylase. J. Biol. Chem. 243 (1968) 2486–2493. [PMID: 4385076]
[EC 1.1.1.92 created 1972]
 
 
EC 1.1.1.93     
Accepted name: tartrate dehydrogenase
Reaction: tartrate + NAD+ = oxaloglycolate + NADH + H+
Other name(s): mesotartrate dehydrogenase
Systematic name: tartrate:NAD+ oxidoreductase
Comments: meso-tartrate and (R,R)-tartrate act as substrates. Requires Mn2+ and a monovalent cation.
References:
1.  Kohn, L.D., Packman, P.M., Allen, R.H. and Jakoby, W.B. Tartaric acid metabolism. V. Crystalline tartrate dehydrogenase. J. Biol. Chem. 243 (1968) 2479–2485. [PMID: 4297261]
[EC 1.1.1.93 created 1972]
 
 
EC 1.1.1.94     
Accepted name: glycerol-3-phosphate dehydrogenase [NAD(P)+]
Reaction: sn-glycerol 3-phosphate + NAD(P)+ = glycerone phosphate + NAD(P)H + H+
Glossary: glycerone phosphate = dihydroxyacetone phosphate = 3-hydroxy-2-oxopropyl phosphate
Other name(s): L-glycerol-3-phosphate:NAD(P) oxidoreductase; glycerol phosphate dehydrogenase (nicotinamide adenine dinucleotide (phosphate)); glycerol 3-phosphate dehydrogenase (NADP); glycerol-3-phosphate dehydrogenase [NAD(P)]
Systematic name: sn-glycerol-3-phosphate:NAD(P)+ 2-oxidoreductase
Comments: The enzyme from Escherichia coli shows specificity for the B side of NADPH.
References:
1.  Kito, M. and Pizer, L.I. Purification and regulatory properties of the biosynthetic L-glycerol 3-phosphate dehydrogenase from Escherichia coli. J. Biol. Chem. 244 (1969) 3316–3323. [PMID: 4389388]
2.  Edgar, J.R. and Bell, R.M. Biosynthesis in Escherichia coli of sn-glycerol 3-phosphate, a precursor of phospholipid. J. Biol. Chem. 253 (1978) 6348–6353. [PMID: 355254]
3.  Edgar, J.R. and Bell, R.M. Biosynthesis in Escherichia coli of sn-glycerol 3-phosphate, a precursor of phospholipid. Kinetic characterization of wild type and feedback-resistant forms of the biosynthetic sn-glycerol-3-phosphate dehydrogenase. J. Biol. Chem. 253 (1978) 6354–6363. [PMID: 28326]
4.  Edgar, J.R. and Bell, R.M. Biosynthesis in Escherichia coli of sn-glycerol-3-phosphate, a precursor of phospholipid. Further kinetic characterization of wild type and feedback-resistant forms of the biosynthetic sn-glycerol-3-phosphate dehydrogenase. J. Biol. Chem. 255 (1980) 3492–3497. [PMID: 6767719]
[EC 1.1.1.94 created 1972, modified 2005]
 
 
EC 1.1.1.95     
Accepted name: phosphoglycerate dehydrogenase
Reaction: 3-phospho-D-glycerate + NAD+ = 3-phosphooxypyruvate + NADH + H+
Other name(s): PHGDH (gene name); D-3-phosphoglycerate:NAD+ oxidoreductase; α-phosphoglycerate dehydrogenase; 3-phosphoglycerate dehydrogenase; 3-phosphoglyceric acid dehydrogenase; D-3-phosphoglycerate dehydrogenase; glycerate 3-phosphate dehydrogenase; glycerate-1,3-phosphate dehydrogenase; phosphoglycerate oxidoreductase; phosphoglyceric acid dehydrogenase; SerA; 3-phosphoglycerate:NAD+ 2-oxidoreductase; SerA 3PG dehydrogenase; 3PHP reductase
Systematic name: 3-phospho-D-glycerate:NAD+ 2-oxidoreductase
Comments: This enzyme catalyses the first committed and rate-limiting step in the phosphoserine pathway of serine biosynthesis. The reaction occurs predominantly in the direction of reduction. The enzyme from the bacterium Escherichia coli also catalyses the activity of EC 1.1.1.399, 2-oxoglutarate reductase [6].
References:
1.  Pizer, L.I. The pathway and control of serine biosynthesis in Escherichia coli. J. Biol. Chem. 238 (1963) 3934–3944. [PMID: 14086727]
2.  Walsh, D.A. and Sallach, H.J. Purification and properties of chicken liver D-3-phosphoglycerate dehydrogenase. Biochemistry 4 (1965) 1076–1085. [PMID: 4378782]
3.  Slaughter, J.C. and Davies, D.D. The isolation and characterization of 3-phosphoglycerate dehydrogenase from peas. Biochem. J. 109 (1968) 743–748. [PMID: 4386930]
4.  Sugimoto, E. and Pizer, L.I. The mechanism of end product inhibition of serine biosynthesis. I. Purification and kinetics of phosphoglycerate dehydrogenase. J. Biol. Chem. 243 (1968) 2081. [PMID: 4384871]
5.  Schuller, D.J., Grant, G.A. and Banaszak, L.J. The allosteric ligand site in the Vmax-type cooperative enzyme phosphoglycerate dehydrogenase. Nat. Struct. Biol. 2 (1995) 69–76. [PMID: 7719856]
6.  Zhao, G. and Winkler, M.E. A novel α-ketoglutarate reductase activity of the serA-encoded 3-phosphoglycerate dehydrogenase of Escherichia coli K-12 and its possible implications for human 2-hydroxyglutaric aciduria. J. Bacteriol. 178 (1996) 232–239. [PMID: 8550422]
7.  Achouri, Y., Rider, M.H., Schaftingen, E.V. and Robbi, M. Cloning, sequencing and expression of rat liver 3-phosphoglycerate dehydrogenase. Biochem. J. 323 (1997) 365–370. [PMID: 9163325]
8.  Dey, S., Grant, G.A. and Sacchettini, J.C. Crystal structure of Mycobacterium tuberculosis D-3-phosphoglycerate dehydrogenase: extreme asymmetry in a tetramer of identical subunits. J. Biol. Chem. 280 (2005) 14892–14899. [PMID: 15668249]
[EC 1.1.1.95 created 1972, modified 2006, modified 2016]
 
 
EC 1.1.1.96     
Accepted name: diiodophenylpyruvate reductase
Reaction: 3-(3,5-diiodo-4-hydroxyphenyl)lactate + NAD+ = 3-(3,5-diiodo-4-hydroxyphenyl)pyruvate + NADH + H+
Other name(s): aromatic α-keto acid; KAR; 2-oxo acid reductase
Systematic name: 3-(3,5-diiodo-4-hydroxyphenyl)lactate:NAD+ oxidoreductase
Comments: Substrates contain an aromatic ring with a pyruvate side chain. The most active substrates are halogenated derivatives. Compounds with hydroxy or amino groups in the 3 or 5 position are inactive.
References:
1.  Zannoni, V.G. and Weber, W.W. Isolation and properties of aromatic α-keto acid reductase. J. Biol. Chem. 241 (1966) 1340–1344. [PMID: 5935348]
[EC 1.1.1.96 created 1972]
 
 
EC 1.1.1.97     
Accepted name: 3-hydroxybenzyl-alcohol dehydrogenase
Reaction: 3-hydroxybenzyl alcohol + NADP+ = 3-hydroxybenzaldehyde + NADPH + H+
Other name(s): m-hydroxybenzyl alcohol dehydrogenase; m-hydroxybenzyl alcohol (NADP) dehydrogenase; m-hydroxybenzylalcohol dehydrogenase
Systematic name: 3-hydroxybenzyl-alcohol:NADP+ oxidoreductase
References:
1.  Forrester, P.I. and Gaucher, G.M. m-Hydroxybenzyl alcohol dehydrogenase from Penicillium urticae. Biochemistry 11 (1972) 1108–1114. [PMID: 4335290]
[EC 1.1.1.97 created 1972]
 
 
EC 1.1.1.98     
Accepted name: (R)-2-hydroxy-fatty-acid dehydrogenase
Reaction: (R)-2-hydroxystearate + NAD+ = 2-oxostearate + NADH + H+
Other name(s): D-2-hydroxy fatty acid dehydrogenase; 2-hydroxy fatty acid oxidase
Systematic name: (R)-2-hydroxystearate:NAD+ oxidoreductase
References:
1.  Levis, G.M. 2-Hydroxy fatty acid oxidases of rat kidney. Biochem. Biophys. Res. Commun. 38 (1970) 470–477. [PMID: 5443694]
[EC 1.1.1.98 created 1972]
 
 
EC 1.1.1.99     
Accepted name: (S)-2-hydroxy-fatty-acid dehydrogenase
Reaction: (S)-2-hydroxystearate + NAD+ = 2-oxostearate + NADH + H+
Other name(s): dehydrogenase, L-2-hydroxy fatty acid; L-2-hydroxy fatty acid dehydrogenase; 2-hydroxy fatty acid oxidase
Systematic name: (S)-2-hydroxystearate:NAD+ oxidoreductase
References:
1.  Levis, G.M. 2-Hydroxy fatty acid oxidases of rat kidney. Biochem. Biophys. Res. Commun. 38 (1970) 470–477. [PMID: 5443694]
[EC 1.1.1.99 created 1972]
 
 
EC 1.1.1.100     
Accepted name: 3-oxoacyl-[acyl-carrier-protein] reductase
Reaction: a (3R)-3-hydroxyacyl-[acyl-carrier protein] + NADP+ = a 3-oxoacyl-[acyl-carrier protein] + NADPH + H+
Other name(s): β-ketoacyl-[acyl-carrier protein](ACP) reductase; β-ketoacyl acyl carrier protein (ACP) reductase; β-ketoacyl reductase; β-ketoacyl thioester reductase; β-ketoacyl-ACP reductase; β-ketoacyl-acyl carrier protein reductase; 3-ketoacyl acyl carrier protein reductase; NADPH-specific 3-oxoacyl-[acylcarrier protein]reductase; 3-oxoacyl-[ACP]reductase; (3R)-3-hydroxyacyl-[acyl-carrier-protein]:NADP+ oxidoreductase
Systematic name: (3R)-3-hydroxyacyl-[acyl-carrier protein]:NADP+ oxidoreductase
Comments: Exhibits a marked preference for acyl-carrier-protein derivatives over CoA derivatives as substrates.
References:
1.  Prescott, D.J. and Vagelos, P.R. Acyl carrier protein. Adv. Enzymol. Relat. Areas Mol. Biol. 36 (1972) 269–311. [PMID: 4561013]
2.  Shimakata, T. and Stumpf, P.K. Purification and characterizations of β-ketoacyl-[acyl-carrier-protein] reductase, β-hydroxyacyl-[acylcarrier-protein] dehydrase, and enoyl-[acyl-carrier-protein] reductase from Spinacia oleracea leaves. Arch. Biochem. Biophys. 218 (1982) 77–91. [PMID: 6756317]
3.  Toomey, R.E. and Wakil, S.J. Studies on the mechanism of fatty acid synthesis. XV. Preparation and general properties of β-ketoacyl acyl carrier protein reductase from Escherichia coli. Biochim. Biophys. Acta 116 (1966) 189–197. [PMID: 4381013]
[EC 1.1.1.100 created 1972, modified 1976]
 
 
EC 1.1.1.101     
Accepted name: acylglycerone-phosphate reductase
Reaction: 1-palmitoylglycerol 3-phosphate + NADP+ = palmitoylglycerone phosphate + NADPH + H+
Other name(s): palmitoyldihydroxyacetone-phosphate reductase; palmitoyl dihydroxyacetone phosphate reductase; palmitoyl-dihydroxyacetone-phosphate reductase; acyldihydroxyacetone phosphate reductase; palmitoyl dihydroxyacetone phosphate reductase
Systematic name: 1-palmitoylglycerol-3-phosphate:NADP+ oxidoreductase
Comments: Also acts on alkylglycerone 3-phosphate and alkylglycerol 3-phosphate.
References:
1.  LaBelle, E.F., Jr. and Hajira, A.K. Enzymatic reduction of alkyl and acyl derivatives of dihydroxyacetone phosphate by reduced pyridine nucleotides. J. Biol. Chem. 247 (1972) 5825–5834. [PMID: 4403490]
[EC 1.1.1.101 created 1972, modified 1976]
 
 
EC 1.1.1.102     
Accepted name: 3-dehydrosphinganine reductase
Reaction: sphinganine + NADP+ = 3-dehydrosphinganine + NADPH + H+
Other name(s): D-3-dehydrosphinganine reductase; D-3-oxosphinganine reductase; DSR; 3-oxosphinganine reductase; 3-oxosphinganine:NADPH oxidoreductase; D-3-oxosphinganine:B-NADPH oxidoreductase
Systematic name: D-erythro-dihydrosphingosine:NADP+ 3-oxidoreductase
References:
1.  Stoffel, W., Le Kim, D. and Sticht, G. Biosynthesis of dihydrosphingosine in vitro. Hoppe-Seyler's Z. Physiol. Chem. 349 (1968) 664–670. [PMID: 4386961]
2.  Stoffel, W., Le Kim, D. and Sticht, G. Metabolism of sphingosine bases. 8. Distribution, isolation and properties of D-3-oxosphinganine reductase. Stereospecificity of the NADPH-dependent reaction of 3-oxodihydrospingosine (2-amino-1-hydroxyoctadecane-3-one). Hoppe-Seyler's Z. Physiol. Chem. 349 (1968) 1637–1644. [PMID: 4387676]
[EC 1.1.1.102 created 1972]
 
 
EC 1.1.1.103     
Accepted name: L-threonine 3-dehydrogenase
Reaction: L-threonine + NAD+ = L-2-amino-3-oxobutanoate + NADH + H+
Other name(s): L-threonine dehydrogenase; threonine 3-dehydrogenase; threonine dehydrogenase; TDH
Systematic name: L-threonine:NAD+ oxidoreductase
Comments: This enzyme acts in concert with EC 2.3.1.29, glycine C-acetyltransferase, in the degradation of threonine to glycine. This threonine-degradation pathway is common to prokaryotic and eukaryotic cells and the two enzymes involved form a complex [2]. In aqueous solution, the product L-2-amino-3-oxobutanoate can spontaneously decarboxylate to form aminoacetone.
References:
1.  Green, M.L. and Elliott, W.H. The enzymic formation of aminoacetone from threonine and its further metabolism. Biochem. J. 92 (1964) 537–549. [PMID: 4284408]
2.  Hartshorne, D. and Greenberg, D.M. Studies on liver threonine dehydrogenase. Arch. Biochem. Biophys. 105 (1964) 173–178. [PMID: 14165492]
3.  Newman, E.B., Kapoor, V. and Potter, R. Role of L-threonine dehydrogenase in the catabolism of threonine and synthesis of glycine by Escherichia coli. J. Bacteriol. 126 (1976) 1245–1249. [PMID: 7548]
4.  Epperly, B.R. and Dekker, E.E. L-Threonine dehydrogenase from Escherichia coli. Identification of an active site cysteine residue and metal ion studies. J. Biol. Chem. 266 (1991) 6086–6092. [PMID: 2007567]
[EC 1.1.1.103 created 1972]
 
 
EC 1.1.1.104     
Accepted name: 4-oxoproline reductase
Reaction: 4-hydroxy-L-proline + NAD+ = 4-oxoproline + NADH + H+
Other name(s): hydroxy-L-proline oxidase
Systematic name: 4-hydroxy-L-proline:NAD+ oxidoreductase
References:
1.  Smith, T.E. and Mitoma, C. Partial purification and some properties of 4-ketoproline reductase. J. Biol. Chem. 237 (1962) 1177–1180. [PMID: 13914427]
[EC 1.1.1.104 created 1972]
 
 
EC 1.1.1.105     
Accepted name: all-trans-retinol dehydrogenase (NAD+)
Reaction: all-trans-retinol—[cellular-retinol-binding-protein] + NAD+ = all-trans-retinal—[cellular-retinol-binding-protein] + NADH + H+
Other name(s): retinol (vitamin A1) dehydrogenase; MDR; microsomal retinol dehydrogenase; retinol dehydrogenase (misleading); retinal reductase (ambiguous); retinene reductase; epidermal retinol dehydrogenase 2; SDR16C5 (gene name); RDH16 (gene name)
Systematic name: all-trans retinol:NAD+ oxidoreductase
Comments: The enzyme recognizes all-trans-retinol and all-trans-retinal as substrates and exhibits a strong preference for NAD+/NADH as cofactors. Recognizes the substrate both in free form and when bound to cellular-retinol-binding-protein (CRBP1), but has higher affinity for the bound form [2]. No activity with 11-cis-retinol or 11-cis-retinal (cf. EC 1.1.1.315, 11-cis retinol dehydrogenase). Also active with 3α-hydroxysteroids [2].
References:
1.  Koen, A.L. and Shaw, C.R. Retinol and alcohol dehydrogenases in retina and liver. Biochim. Biophys. Acta 128 (1966) 48–54. [PMID: 5972368]
2.  Gough, W.H., VanOoteghem, S., Sint, T. and Kedishvili, N.Y. cDNA cloning and characterization of a new human microsomal NAD+-dependent dehydrogenase that oxidizes all-trans-retinol and 3α-hydroxysteroids. J. Biol. Chem. 273 (1998) 19778–19785. [PMID: 9677409]
3.  Matsuzaka, Y., Okamoto, K., Tsuji, H., Mabuchi, T., Ozawa, A., Tamiya, G. and Inoko, H. Identification of the hRDH-E2 gene, a novel member of the SDR family, and its increased expression in psoriatic lesion. Biochem. Biophys. Res. Commun. 297 (2002) 1171–1180. [PMID: 12372410]
4.  Lee, S.A., Belyaeva, O.V. and Kedishvili, N.Y. Biochemical characterization of human epidermal retinol dehydrogenase 2. Chem. Biol. Interact. 178 (2009) 182–187. [PMID: 18926804]
[EC 1.1.1.105 created 1972, modified 2011]
 
 
EC 1.1.1.106     
Accepted name: pantoate 4-dehydrogenase
Reaction: (R)-pantoate + NAD+ = (R)-4-dehydropantoate + NADH + H+
Glossary: pantoate = 2,4-dihydroxy-3,3-dimethylbutanoate
Other name(s): pantoate dehydrogenase; pantothenase; D-pantoate:NAD+ 4-oxidoreductase
Systematic name: (R)-pantoate:NAD+ 4-oxidoreductase
References:
1.  Goodhue, C.T. and Snell, E.E. The bacterial degradation of pantothenic acid. 3. Enzymatic formation of aldopantoic acid. Biochemistry 5 (1966) 403–408. [PMID: 4287370]
[EC 1.1.1.106 created 1972, modified 1976]
 
 
EC 1.1.1.107     
Accepted name: pyridoxal 4-dehydrogenase
Reaction: pyridoxal + NAD+ = 4-pyridoxolactone + NADH + H+
Other name(s): pyridoxal dehydrogenase
Systematic name: pyridoxal:NAD+ 4-oxidoreductase
Comments: The enzyme acts on the hemiacetal form of the substrate.
References:
1.  Burg, R.W. and Snell, E.E. The bacterial oxidation of vitamin B6. VI. Pyridoxal dehydrogenase and 4-pyridoxolactonase. J. Biol. Chem. 244 (1969) 2585–2589. [PMID: 4306030]
[EC 1.1.1.107 created 1972]
 
 
EC 1.1.1.108     
Accepted name: carnitine 3-dehydrogenase
Reaction: carnitine + NAD+ = 3-dehydrocarnitine + NADH + H+
Systematic name: carnitine:NAD+ 3-oxidoreductase
References:
1.  Aurich, H., Kleber, H.-P., Sorger, H. and Tauchert, H. Reinigung und Eigenschaften der Carnitindehydrogenase aus Pseudomonas aeruginosa. Eur. J. Biochem. 6 (1968) 196–201. [PMID: 4302217]
2.  Schöpp, W., Sorger, H., Kleber, H.-P. and Aurich, H. Kinetische Untersuchungen zum Reaktionmechanisms der Carnitindehydrogenase aus Pseudomonas aeruginosa. Eur. J. Biochem. 10 (1969) 56–60. [PMID: 4310279]
[EC 1.1.1.108 created 1972]
 
 
EC 1.1.1.109      
Transferred entry: 2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase. Now EC 1.3.1.28, 2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase
[EC 1.1.1.109 created 1972, deleted 1976]
 
 
EC 1.1.1.110     
Accepted name: aromatic 2-oxoacid reductase
Reaction: (1) (R)-3-(phenyl)lactate + NAD+ = 3-phenylpyruvate + NADH + H+
(2) (R)-3-(4-hydroxyphenyl)lactate + NAD+ = 3-(4-hydroxyphenyl)pyruvate + NADH + H+
(3) (R)-(indol-3-yl)lactate + NAD+ = (indol-3-yl)pyruvate + NADH + H+
Glossary: 3-phenylpyruvate = 2-oxo-3-phenylpropanoate
Other name(s): (R)-aromatic lactate dehydrogenase; (R)-4-hydroxyphenyllactate dehydrogenase; indolelactate:NAD+ oxidoreductase; indolelactate dehydrogenase; fldH (gene name); (indol-3-yl)lactate:NAD+ oxidoreductase
Systematic name: aromatic 2-oxoacid:NAD+ oxidoreductase
Comments: The enzymes from anaerobic bacteria such as Clostridium sporogenes participate in the fermentation pathways of L-phenylalanine, L-tyrosine and L-tryptophan. The enzyme from the yeast Candida maltosa has similar activity, but, unlike the bacterial enzyme, requires Mn2+ and can also use NADPH with lower activity.
References:
1.  Jean, M. and DeMoss, R.D. Indolelactate dehydrogenase from Clostridium sporogenes. Can. J. Microbiol. 14 (1968) 429–435. [PMID: 4384683]
2.  Giesel, H. and Simon, H. On the occurrence of enoate reductase and 2-oxo-carboxylate reductase in clostridia and some observations on the amino acid fermentation by Peptostreptococcus anaerobius. Arch. Microbiol. 135 (1983) 51–57. [PMID: 6354130]
3.  Bode, R., Lippoldt, A. and Birnbaum, D. Purification and properties of D-aromatic lactate dehydrogenase an enzyme involved in the catabolism of the aromatic amino acids of Candida maltosa. Biochem. Physiol. Pflanzen 181 (1986) 189–198.
4.  Dickert, S., Pierik, A.J., Linder, D. and Buckel, W. The involvement of coenzyme A esters in the dehydration of (R)-phenyllactate to (E)-cinnamate by Clostridium sporogenes. Eur. J. Biochem. 267 (2000) 3874–3884. [PMID: 10849007]
5.  Dodd, D., Spitzer, M.H., Van Treuren, W., Merrill, B.D., Hryckowian, A.J., Higginbottom, S.K., Le, A., Cowan, T.M., Nolan, G.P., Fischbach, M.A. and Sonnenburg, J.L. A gut bacterial pathway metabolizes aromatic amino acids into nine circulating metabolites. Nature 551 (2017) 648–652. [PMID: 29168502]
[EC 1.1.1.110 created 1972 (EC 1.1.1.222 created 2000, incorporated 2018), modified 2018]
 
 
EC 1.1.1.111     
Accepted name: 3-(imidazol-5-yl)lactate dehydrogenase
Reaction: (S)-3-(imidazol-5-yl)lactate + NAD(P)+ = 3-(imidazol-5-yl)pyruvate + NAD(P)H + H+
Other name(s): imidazol-5-yl lactate dehydrogenase
Systematic name: (S)-3-(imidazol-5-yl)lactate:NAD(P)+ oxidoreductase
References:
1.  Coote, J.G. and Hassall, H. The role of imidazol-5-yl-lactate-nicotinamide-adenine dinucleotide phosphate oxidoreductase and histidine-2-oxoglutarate aminotransferase in the degradation of imidazol-5-yl-lactate by Pseudomonas acidovorans. Biochem. J. 111 (1969) 237–239. [PMID: 4303364]
2.  Cortese, R., Brevet, J., Hedegaard, J. and Roche, J. [Identification and purification of an α-ketoacid aromatic reductase of Escherichia coli B] C.R. Seances Soc. Biol. Fil. 162 (1968) 390–395. [PMID: 4237631] (in French)
[EC 1.1.1.111 created 1972]
 
 
EC 1.1.1.112     
Accepted name: indanol dehydrogenase
Reaction: indan-1-ol + NAD(P)+ = indanone + NAD(P)H + H+
Systematic name: indan-1-ol:NAD(P)+ 1-oxidoreductase
Comments: 3(20)α-Hydroxysteroids are also oxidized, more slowly.
References:
1.  Billings, R.E., Sullivan, H.R. and McMahon, R.E. The dehydrogenation of 1-indanol by a soluble oxidoreductase from bovine liver. J. Biol. Chem. 246 (1971) 3512–3517. [PMID: 4397102]
2.  Hara, A., Nakagawa, M., Taniguchi, H. and Sawada, H. 3(20)α-Hydroxysteroid dehydrogenase activity of monkey liver indanol dehydrogenase. J. Biochem. (Tokyo) 106 (1989) 900–903. [PMID: 2559080]
[EC 1.1.1.112 created 1972]
 
 
EC 1.1.1.113     
Accepted name: L-xylose 1-dehydrogenase
Reaction: L-xylose + NADP+ = L-xylono-1,4-lactone + NADPH + H+
Other name(s): L-xylose dehydrogenase; NADPH-xylose reductase
Systematic name: L-xylose:NADP+ 1-oxidoreductase
Comments: Also oxidizes D-arabinose and D-lyxose.
References:
1.  Uehara, K. and Takeda, M. L-Xylose dehydrogenase in bakers' yeast. J. Biochem. (Tokyo) 52 (1962) 461–463. [PMID: 13995171]
[EC 1.1.1.113 created 1972]
 
 
EC 1.1.1.114     
Accepted name: apiose 1-reductase
Reaction: D-apiitol + NAD+ = D-apiose + NADH + H+
Other name(s): D-apiose reductase; D-apiitol reductase
Systematic name: D-apiitol:NAD+ 1-oxidoreductase
References:
1.  Hanna, R., Picken, M. and Mendicino, J. Purification of a specific D-apiitol dehydrogenase from a Micrococcus isolated from the surface of germinating parsley seeds. Biochim. Biophys. Acta 315 (1973) 259–271.
2.  Neal, D.L. and Kindel, P.K. D-Apiose reductase from Aerobacter aerogenes. J. Bacteriol. 101 (1970) 910–915. [PMID: 4314545]
[EC 1.1.1.114 created 1972]
 
 
EC 1.1.1.115     
Accepted name: ribose 1-dehydrogenase (NADP+)
Reaction: D-ribose + NADP+ + H2O = D-ribonate + NADPH + H+
Other name(s): D-ribose dehydrogenase (NADP+); NADP-pentose-dehydrogenase; ribose 1-dehydrogenase (NADP)
Systematic name: D-ribose:NADP+ 1-oxidoreductase
Comments: Also acts, more slowly, on D-xylose and other pentoses.
References:
1.  Scher, B.M. and Horecker, B.L. Pentose metabolism in Candida. 3. The triphosphopyridine nucleotide-specific polyol dehydrogenase of Candida utilis. Arch. Biochem. Biophys. 116 (1966) 117–128. [PMID: 4381350]
2.  Schiwara, H.W., Domschke, W. and Domagk, G.F. Über die Zucker-Dehydrogenase in der Säugetierleber. I. Differenzierung verschiedener Zucker-Dehydrogenasen in der Schweineleber durch Disk-Elektrophorese und Ionenaustausch-chromatographie. Hoppe-Seyler's Z. Physiol. Chem. 349 (1968) 1575–1581. [PMID: 4393642]
[EC 1.1.1.115 created 1972]
 
 
EC 1.1.1.116     
Accepted name: D-arabinose 1-dehydrogenase (NAD+)
Reaction: D-arabinose + NAD+ = D-arabinono-1,4-lactone + NADH + H+
Other name(s): NAD+-pentose-dehydrogenase; arabinose(fucose)dehydrogenase
Systematic name: D-arabinose:NAD+ 1-oxidoreductase
References:
1.  Palleroni, N.J. and Doudoroff, M. Metabolism of carbohydrates by Pseudomonas saccharophilla. III. Oxidation of D-arabinose. J. Bacteriol. 74 (1957) 180–185. [PMID: 13475218]
2.  Schiwara, H.W., Domschke, W. and Domagk, G.F. Über die Zucker-Dehydrogenase in der Säugetierleber. I. Differenzierung verschiedener Zucker-Dehydrogenasen in der Schweineleber durch Disk-Elektrophorese und Ionenaustausch-chromatographie. Hoppe-Seyler's Z. Physiol. Chem. 349 (1968) 1575–1581. [PMID: 4393642]
[EC 1.1.1.116 created 1972]
 
 
EC 1.1.1.117     
Accepted name: D-arabinose 1-dehydrogenase [NAD(P)+]
Reaction: D-arabinose + NAD(P)+ = D-arabinono-1,4-lactone + NAD(P)H + H+
Other name(s): D-arabinose 1-dehydrogenase [NAD(P)]
Systematic name: D-arabinose:NAD(P)+ 1-oxidoreductase
Comments: Also acts on L-galactose, 6-deoxy- and 3,6-dideoxy-L-galactose.
References:
1.  Cline, A.L. and Hu, A.S.L. The isolation of three sugar dehydrogenases from a psuedomonad. J. Biol. Chem. 240 (1965) 4488–4492. [PMID: 5845847]
2.  Cline, A.L. and Hu, A.S.L. Enzymatic characterization and comparison of three sugar dehydrogenases from a pseudomonad. J. Biol. Chem. 240 (1965) 4493–4497. [PMID: 5845848]
3.  Cline, A.L. and Hu, A.S.L. Some physical properties of three sugar dehydrogenases from a pseudomonad. J. Biol. Chem. 240 (1965) 4498–4502. [PMID: 5845849]
[EC 1.1.1.117 created 1972]
 
 
EC 1.1.1.118     
Accepted name: glucose 1-dehydrogenase (NAD+)
Reaction: D-glucose + NAD+ = D-glucono-1,5-lactone + NADH + H+
Other name(s): D-glucose:NAD oxidoreductase; D-aldohexose dehydrogenase; glucose 1-dehydrogenase (NAD)
Systematic name: D-glucose:NAD+ 1-oxidoreductase
References:
1.  Hu, A.S.L. and Cline, A.L. The regulation of some sugar dehydrogenases in a pseudomonad. Biochim. Biophys. Acta 93 (1964) 237–245. [PMID: 14251301]
[EC 1.1.1.118 created 1972, modified 1976]
 
 
EC 1.1.1.119     
Accepted name: glucose 1-dehydrogenase (NADP+)
Reaction: D-glucose + NADP+ = D-glucono-1,5-lactone + NADPH + H+
Other name(s): nicotinamide adenine dinucleotide phosphate-linked aldohexose dehydrogenase; NADP-linked aldohexose dehydrogenase; NADP-dependent glucose dehydrogenase; glucose 1-dehydrogenase (NADP)
Systematic name: D-glucose:NADP+ 1-oxidoreductase
Comments: Also oxidizes D-mannose, 2-deoxy-D-glucose and 2-amino-2-deoxy-D-mannose.
References:
1.  Adachi, O. and Ameyama, M. D-Glucose dehydrogenase from Gluconobacter suboxydans. Methods Enzymol. 89 (1982) 159–163.
2.  Avigad, G., Alroy, Y. and Englard, S. Purification and properties of a nicotinamide adenine dinucleotide phosphate-linked aldohexose dehydrogenase from Gluconobacter cerinus. J. Biol. Chem. 243 (1968) 1936–1941. [PMID: 4384672]
[EC 1.1.1.119 created 1972]
 
 
EC 1.1.1.120     
Accepted name: galactose 1-dehydrogenase (NADP+)
Reaction: D-galactose + NADP+ = D-galactono-1,5-lactone + NADPH + H+
Other name(s): D-galactose dehydrogenase (NADP+); galactose 1-dehydrogenase (NADP)
Systematic name: D-galactose:NADP+ 1-oxidoreductase
Comments: Also acts on L-arabinose, 6-deoxy- and 2-deoxy-D-galactose.
References:
1.  Cline, A.L. and Hu, A.S.L. The isolation of three sugar dehydrogenases from a psuedomonad. J. Biol. Chem. 240 (1965) 4488–4492. [PMID: 5845847]
2.  Cline, A.L. and Hu, A.S.L. Enzymatic characterization and comparison of three sugar dehydrogenases from a pseudomonad. J. Biol. Chem. 240 (1965) 4493–4497. [PMID: 5845848]
3.  Cline, A.L. and Hu, A.S.L. Some physical properties of three sugar dehydrogenases from a pseudomonad. J. Biol. Chem. 240 (1965) 4498–4502. [PMID: 5845849]
4.  Schiwara, H.W. and Domagk, G.F. Über den Abbau der Desoxyzucker durch Bakterienenzyme. V. Anreicherung und Charakterisierung einer NADP-abhängigen Abequosedehydrogenase aus Pseudomonas putida. Hoppe-Seyler's Z. Physiol. Chem. 349 (1968) 1321–1329. [PMID: 4387016]
[EC 1.1.1.120 created 1972]
 
 
EC 1.1.1.121     
Accepted name: aldose 1-dehydrogenase (NAD+)
Reaction: D-aldose + NAD+ = D-aldonolactone + NADH + H+
Other name(s): aldose dehydrogenase; D-aldohexose dehydrogenase; aldose 1-dehydrogenase
Systematic name: D-aldose:NAD+ 1-oxidoreductase
Comments: Acts on D-glucose, 2-deoxy- and 6-deoxy-D-glucose, D-galactose, 6-deoxy-D-galactose, 2-deoxy-L-arabinose and D-xylose.
References:
1.  Cline, A.L. and Hu, A.S.L. The isolation of three sugar dehydrogenases from a psuedomonad. J. Biol. Chem. 240 (1965) 4488–4492. [PMID: 5845847]
2.  Cline, A.L. and Hu, A.S.L. Enzymatic characterization and comparison of three sugar dehydrogenases from a pseudomonad. J. Biol. Chem. 240 (1965) 4493–4497. [PMID: 5845848]
3.  Cline, A.L. and Hu, A.S.L. Some physical properties of three sugar dehydrogenases from a pseudomonad. J. Biol. Chem. 240 (1965) 4498–4502. [PMID: 5845849]
[EC 1.1.1.121 created 1972]
 
 
EC 1.1.1.122     
Accepted name: D-threo-aldose 1-dehydrogenase
Reaction: a D-threo-aldose + NAD+ = a D-threo-aldono-1,5-lactone + NADH + H+
Other name(s): L-fucose dehydrogenase; (2S,3R)-aldose dehydrogenase; dehydrogenase, L-fucose; L-fucose (D-arabinose) dehydrogenase
Systematic name: D-threo-aldose:NAD+ 1-oxidoreductase
Comments: Acts on L-fucose, D-arabinose and L-xylose; the animal enzyme was also shown to act on L-arabinose, and the enzyme from Pseudomonas caryophylli on L-glucose.
References:
1.  Sasajima, K.-I. and Sinskey, A.J. Oxidation of L-glucose by a Pseudomonad. Biochim. Biophys. Acta 571 (1979) 120–126. [PMID: 40609]
2.  Schachter, H., Sarney, J., McGuire, E.J. and Roseman, S. Isolation of diphosphopyridine nucleotide-dependent L-fucose dehydrogenase from pork liver. J. Biol. Chem. 244 (1969) 4785–4792. [PMID: 4309152]
[EC 1.1.1.122 created 1972]
 
 
EC 1.1.1.123     
Accepted name: sorbose 5-dehydrogenase (NADP+)
Reaction: L-sorbose + NADP+ = 5-dehydro-D-fructose + NADPH + H+
Other name(s): 5-ketofructose reductase; 5-keto-D-fructose reductase; sorbose (nicotinamide adenine dinucleotide phosphate) dehydrogenase; reduced nicotinamide adenine dinucleotide phosphate-linked reductase; sorbose 5-dehydrogenase (NADP+)
Systematic name: L-sorbose:NADP+ 5-oxidoreductase
References:
1.  Englard, S., Kaysen, G. and Avigad, G. 5-keto-D-Fructose. VI. A specific reduced nicotinamide adenine dinucleotide phosphate-linked reductase from yeast. J. Biol. Chem. 245 (1970) 1311–1318. [PMID: 4392628]
[EC 1.1.1.123 created 1972, modified 1976]
 
 
EC 1.1.1.124     
Accepted name: fructose 5-dehydrogenase (NADP+)
Reaction: D-fructose + NADP+ = 5-dehydro-D-fructose + NADPH + H+
Other name(s): 5-ketofructose reductase (NADP); 5-keto-D-fructose reductase (NADP+); fructose 5-(nicotinamide adenine dinucleotide phosphate) dehydrogenase; D-(-)fructose:(NADP+) 5-oxidoreductase; fructose 5-dehydrogenase (NADP)
Systematic name: D-fructose:NADP+ 5-oxidoreductase
References:
1.  Ameyama, M., Matsushita, K., Shinagawa, E. and Adachi, O. 5-keto-D-Fructose reductase of Gluconobacter industrius. Purification, crystallization and properties. Agric. Biol. Chem. 45 (1981) 863–869.
2.  Avigad, G., Englard, S. and Pifco, S. 5-keto-D-Fructose. IV. A specific reduced nicotinamide adenine dinucleotide phosphate-linked reductase from Gluconobacter cerinus. J. Biol. Chem. 241 (1966) 373–378. [PMID: 4379259]
[EC 1.1.1.124 created 1972, modified 1976]
 
 
EC 1.1.1.125     
Accepted name: 2-deoxy-D-gluconate 3-dehydrogenase
Reaction: 2-deoxy-D-gluconate + NAD+ = 3-dehydro-2-deoxy-D-gluconate + NADH + H+
Other name(s): 2-deoxygluconate dehydrogenase
Systematic name: 2-deoxy-D-gluconate:NAD+ 3-oxidoreductase
References:
1.  Eichhorn, M.M. and Cynkin, M.A. Microbial metabolism of 2-deoxyglucose; 2-deoxyglucose acid dehydrogenase. Biochemistry 4 (1965) 159–165. [PMID: 14285233]
[EC 1.1.1.125 created 1972]
 
 
EC 1.1.1.126     
Accepted name: 2-dehydro-3-deoxy-D-gluconate 6-dehydrogenase
Reaction: 2-dehydro-3-deoxy-D-gluconate + NADP+ = (4S,5S)-4,5-dihydroxy-2,6-dioxohexanoate + NADPH + H+
Other name(s): 2-keto-3-deoxy-D-gluconate dehydrogenase (ambiguous); 2-keto-3-deoxygluconate dehydrogenase (ambiguous)
Systematic name: 2-dehydro-3-deoxy-D-gluconate:NADP+ 6-oxidoreductase
References:
1.  Preiss, J. and Ashwell, G. Alginic acid metabolism in bacteria. II. The enzymatic reduction of 4-deoxy-L-erythro-5-hexoseulose uronic acid to 2-keto-3-deoxy-D-gluconic acid. J. Biol. Chem. 237 (1962) 317–321. [PMID: 14488585]
[EC 1.1.1.126 created 1972]
 
 
EC 1.1.1.127     
Accepted name: 2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase
Reaction: 2-dehydro-3-deoxy-D-gluconate + NAD+ = (4S)-4,6-dihydroxy-2,5-dioxohexanoate + NADH + H+
Other name(s): 2-keto-3-deoxygluconate 5-dehydrogenase; 2-keto-3-deoxy-D-gluconate dehydrogenase (ambiguous); 2-keto-3-deoxygluconate (nicotinamide adenine dinucleotide (phosphate)) dehydrogenase; 2-keto-3-deoxy-D-gluconate (3-deoxy-D-glycero-2,5-hexodiulosonic acid) dehydrogenase (ambiguous)
Systematic name: 2-dehydro-3-deoxy-D-gluconate:NAD+ 5-oxidoreductase
Comments: The enzyme from Pseudomonas acts equally well on NAD+ or NADP+, while that from Erwinia chrysanthemi and Escherichia coli is more specific for NAD+.
References:
1.  Condemine, G., Hugouvieux-Cotte-Pattat, N. and Robert-Baudouy, J. An enzyme in the pectolytic pathway of Erwinia chrysanthemi: 3-keto-3-deoxygluconate oxidoreductase. J. Gen. Microbiol. 130 (1984) 2839–2844.
2.  Preiss, J. and Ashwell, G. Polygalacturonic acid metabolism in bacteria. II. Formation and metabolism of 3-deoxy-D-glycero-2,5-hexodiulosonic acid. J. Biol. Chem. 238 (1963) 1577–1583. [PMID: 13986017]
[EC 1.1.1.127 created 1972, modified 1976, modified 1989]
 
 
EC 1.1.1.128      
Deleted entry: L-idonate 2-dehydrogenase. The reaction described is covered by EC 1.1.1.264.
[EC 1.1.1.128 created 1972, modified 1976, deleted 2012]
 
 
EC 1.1.1.129     
Accepted name: L-threonate 3-dehydrogenase
Reaction: L-threonate + NAD+ = 3-dehydro-L-erythronate + NADH + H+
Other name(s): threonate dehydrogenase; L-threonic acid dehydrogenase
Systematic name: L-threonate:NAD+ 3-oxidoreductase
References:
1.  Aspen, A.J. and Jakoby, W.B. L-Threonic acid dehydrogenase: purification and properties. J. Biol. Chem. 239 (1964) 710–713. [PMID: 14154441]
[EC 1.1.1.129 created 1972]
 
 
EC 1.1.1.130     
Accepted name: 3-dehydro-L-gulonate 2-dehydrogenase
Reaction: 3-dehydro-L-gulonate + NAD(P)+ = (4R,5S)-4,5,6-trihydroxy-2,3-dioxohexanoate + NAD(P)H + H+
Other name(s): 3-keto-L-gulonate dehydrogenase; 3-ketogulonate dehydrogenase; 3-keto-L-gulonate dehydrogenase; 3-ketogulonate dehydrogenase
Systematic name: 3-dehydro-L-gulonate:NAD(P)+ 2-oxidoreductase
References:
1.  Volk, W.A. and Larsen, J.L. β-Keto-L-gulonic acid as an intermediate in the bacterial metabolism of ascorbic acid. J. Biol. Chem. 237 (1962) 2454–2457. [PMID: 13926592]
[EC 1.1.1.130 created 1972]
 
 
EC 1.1.1.131     
Accepted name: mannuronate reductase
Reaction: D-mannonate + NAD(P)+ = D-mannuronate + NAD(P)H + H+
Other name(s): mannonate dehydrogenase; mannonate (nicotinamide adenine dinucleotide (phosphate))dehydrogenase; mannonate dehydrogenase; mannuronate reductase; mannonate dehydrogenase (NAD(P)+); D-mannonate:nicotinamide adenine dinucleotide (phosphate oxidoreductase (D-mannuronate-forming))
Systematic name: D-mannonate:NAD(P)+ 6-oxidoreductase
References:
1.  Farmer, J.J., III and Eagon, R.G. Aldohexuronic acid catabolism by a soil Aeromonas. J. Bacteriol. 97 (1969) 97–106. [PMID: 4388117]
[EC 1.1.1.131 created 1972 (EC 1.2.1.34 created 1972, incorporated 1983; EC 1.1.1.180 created 1983, incorporated 1984)]
 
 
EC 1.1.1.132     
Accepted name: GDP-mannose 6-dehydrogenase
Reaction: GDP-D-mannose + 2 NAD+ + H2O = GDP-D-mannuronate + 2 NADH + 2 H+
Other name(s): guanosine diphosphomannose dehydrogenase; GDP-mannose dehydrogenase; guanosine diphosphomannose dehydrogenase; guanosine diphospho-D-mannose dehydrogenase
Systematic name: GDP-D-mannose:NAD+ 6-oxidoreductase
Comments: Also acts on the corresponding deoxynucleoside diphosphate derivative as a substrate.
References:
1.  Preiss, J. Sugar nucleotide reaction in Arthrobacter. II. Biosynthesis of guanosine diphosphomannuronate. J. Biol. Chem. 239 (1964) 3127–3132. [PMID: 14245351]
[EC 1.1.1.132 created 1972]
 
 
EC 1.1.1.133     
Accepted name: dTDP-4-dehydrorhamnose reductase
Reaction: dTDP-β-L-rhamnose + NADP+ = dTDP-4-dehydro-β-L-rhamnose + NADPH + H+
Glossary: dTDP-4-dehydro-β-L-rhamnose = dTDP-4-dehydro-6-deoxy-β-L-mannose
dTDP-4-β-L-rhamnose = dTDP-6-deoxy-β-L-mannose
Other name(s): dTDP-4-keto-L-rhamnose reductase; dTDP-4-ketorhamnose reductase; TDP-4-keto-rhamnose reductase; thymidine diphospho-4-ketorhamnose reductase; dTDP-6-deoxy-L-mannose:NADP+ 4-oxidoreductase; dTDP-6-deoxy-β-L-mannose:NADP+ 4-oxidoreductase
Systematic name: dTDP-β-L-rhamnose:NADP+ 4-oxidoreductase
Comments: In the reverse direction, reduction on the 4-position of the hexose moiety takes place only while the substrate is bound to another enzyme that catalyses epimerization at C-3 and C-5; the complex has been referred to as dTDP-L-rhamnose synthase.
References:
1.  Melo, A. and Glaser, L. The mechanism of 6-deoxyhexose synthesis. II. Conversion of deoxythymidine diphosphate 4-keto-6-deoxy-D-glucose to deoxythymidine diphosphate L-rhamnose. J. Biol. Chem. 243 (1968) 1475–1478. [PMID: 4384782]
[EC 1.1.1.133 created 1972]
 
 
EC 1.1.1.134     
Accepted name: dTDP-6-deoxy-L-talose 4-dehydrogenase (NADP+)
Reaction: dTDP-6-deoxy-β-L-talose + NADP+ = dTDP-4-dehydro-β-L-rhamnose + NADPH + H+
Glossary: dTDP-4-dehydro-β-L-rhamnose = dTDP-4-dehydro-6-deoxy-β-L-mannose
dTDP-6-deoxy-β-L-talose = dTDP-β-L-pneumose
Other name(s): thymidine diphospho-6-deoxy-L-talose dehydrogenase; TDP-6-deoxy-L-talose dehydrogenase; dTDP-6-deoxy-L-talose dehydrogenase (4-reductase); dTDP-6-deoxy-L-talose:NADP+ 4-oxidoreductase
Systematic name: dTDP-6-deoxy-β-L-talose:NADP+ 4-oxidoreductase
Comments: Oxidation on the 4-position of the hexose moiety takes place only while the substrate is bound to another enzyme that catalyses epimerization at C-3 and C-5.
References:
1.  Gaugler, R.W. and Gabriel, O. Biological mechanisms involved in the formation of deoxy sugars. VII. Biosynthesis of 6-deoxy-L-talose. J. Biol. Chem. 248 (1973) 6041–6049. [PMID: 4199258]
[EC 1.1.1.134 created 1972]
 
 
EC 1.1.1.135     
Accepted name: GDP-6-deoxy-D-talose 4-dehydrogenase
Reaction: GDP-6-deoxy-α-D-talose + NAD(P)+ = GDP-4-dehydro-α-D-rhamnose + NAD(P)H + H+
Glossary: GDP-4-dehydro-α-D-rhamnose = GDP-4-dehydro-6-deoxy-α-D-mannose
GDP-6-deoxy-α-D-talose = GDP-α-D-pneumose
Other name(s): guanosine diphospho-6-deoxy-D-talose dehydrogenase; GDP-6-deoxy-D-talose:NAD(P)+ 4-oxidoreductase
Systematic name: GDP-6-deoxy-α-D-talose:NAD(P)+ 4-oxidoreductase
References:
1.  Markovitz, A. Biosynthesis of guanosine diphosphate D-rhamnose and guanosine diphosphate D-talomethylose from guanosine diphosphate α-D-mannose. J. Biol. Chem. 239 (1964) 2091–2098. [PMID: 14209931]
[EC 1.1.1.135 created 1972, modified 1976]
 
 
EC 1.1.1.136     
Accepted name: UDP-N-acetylglucosamine 6-dehydrogenase
Reaction: UDP-N-acetyl-α-D-glucosamine + 2 NAD+ + H2O = UDP-2-acetamido-2-deoxy-α-D-glucuronate + 2 NADH + 2 H+
Other name(s): uridine diphosphoacetylglucosamine dehydrogenase; UDP-acetylglucosamine dehydrogenase; UDP-2-acetamido-2-deoxy-D-glucose:NAD oxidoreductase; UDP-GlcNAc dehydrogenase; WbpA; WbpO
Systematic name: UDP-N-acetyl-α-D-glucosamine:NAD+ 6-oxidoreductase
Comments: This enzyme participates in the biosynthetic pathway for UDP-α-D-ManNAc3NAcA (UDP-2,3-diacetamido-2,3-dideoxy-α-D-mannuronic acid), an important precursor of B-band lipopolysaccharide.
References:
1.  Fan, D.-F., John, C.E., Zalitis, J. and Feingold, D.S. UDPacetylglucosamine dehydrogenase from Achromobacter georgiopolitanum. Arch. Biochem. Biophys. 135 (1969) 45–49. [PMID: 4312076]
2.  Miller, W.L., Wenzel, C.Q., Daniels, C., Larocque, S., Brisson, J.R. and Lam, J.S. Biochemical characterization of WbpA, a UDP-N-acetyl-D-glucosamine 6-dehydrogenase involved in O-antigen biosynthesis in Pseudomonas aeruginosa PAO1. J. Biol. Chem. 279 (2004) 37551–37558. [PMID: 15226302]
[EC 1.1.1.136 created 1972, modified 2012]
 
 
EC 1.1.1.137     
Accepted name: ribitol-5-phosphate 2-dehydrogenase
Reaction: D-ribitol 5-phosphate + NAD(P)+ = D-ribulose 5-phosphate + NAD(P)H + H+
Other name(s): ribitol 5-phosphate dehydrogenase
Systematic name: D-ribitol-5-phosphate:NAD(P)+ 2-oxidoreductase
Comments: The enzyme, characterized from the bacterium Lactobacillus plantarum, can use both NAD+ and NADP+ as electron acceptor [cf. EC 1.1.1.405, ribitol-5-phosphate 2-dehydrogenase (NADP+)].
References:
1.  Glaser, L. Ribitol-5-phosphate dehydrogenase from Lactobacillus plantarum. Biochim. Biophys. Acta 67 (1963) 525–530. [PMID: 13948358]
[EC 1.1.1.137 created 1972, modified 2017]
 
 
EC 1.1.1.138     
Accepted name: mannitol 2-dehydrogenase (NADP+)
Reaction: D-mannitol + NADP+ = D-fructose + NADPH + H+
Other name(s): mannitol 2-dehydrogenase (NADP)
Systematic name: D-mannitol:NADP+ 2-oxidoreductase
References:
1.  Edmundowicz, J.M. and Wriston, J.C., Jr. Mannitol dehydrogenase from Agaricus campestris. J. Biol. Chem. 238 (1963) 3539–3541. [PMID: 14109183]
2.  Strobel, G.A. and Kosuge, T. Polyol metabolism in Diplodia viticola Desm. Arch. Biochem. Biophys. 109 (1965) 622–626. [PMID: 14320506]
[EC 1.1.1.138 created 1972]
 
 
EC 1.1.1.139      
Deleted entry: polyol dehydrogenase (NADP+). Now included with EC 1.1.1.21 aldehyde reductase
[EC 1.1.1.139 created 1972, deleted 1978]
 
 
EC 1.1.1.140     
Accepted name: sorbitol-6-phosphate 2-dehydrogenase
Reaction: D-sorbitol 6-phosphate + NAD+ = D-fructose 6-phosphate + NADH + H+
Other name(s): ketosephosphate reductase; ketosephosphate reductase; D-sorbitol 6-phosphate dehydrogenase; D-sorbitol-6-phosphate dehydrogenase; sorbitol-6-P-dehydrogenase; D-glucitol-6-phosphate dehydrogenase
Systematic name: D-sorbitol-6-phosphate:NAD+ 2-oxidoreductase
References:
1.  Du Toit, P.J. and Kotzé, J.P. The isolation and characterization of sorbitol-6-phosphate dehydrogenase from Clostridium pasteurianum. Biochim. Biophys. Acta 206 (1970) 333–342. [PMID: 4318899]
2.  Liss, M., Horwitz, S.B. and Kaplan, N.O. D-Mannitol 1-phosphate dehydrogenase and D-sorbitol 6-phosphate dehydrogenase in Aerobacter aerogenes. J. Biol. Chem. 237 (1962) 1342–1350. [PMID: 14465816]
[EC 1.1.1.140 created 1972]
 
 
EC 1.1.1.141     
Accepted name: 15-hydroxyprostaglandin dehydrogenase (NAD+)
Reaction: (5Z,13E,15S)-11α,15-dihydroxy-9-oxoprost-5,13-dienoate + NAD+ = (5Z,13E)-11α-hydroxy-9,15-dioxoprost-5,13-dienoate + NADH + H+
Other name(s): NAD+-dependent 15-hydroxyprostaglandin dehydrogenase (type I); PGDH; 11α,15-dihydroxy-9-oxoprost-13-enoate:NAD+ 15-oxidoreductase; 15-OH-PGDH; 15-hydroxyprostaglandin dehydrogenase; 15-hydroxyprostanoic dehydrogenase; NAD+-specific 15-hydroxyprostaglandin dehydrogenase; prostaglandin dehydrogenase; 15-hydroxyprostaglandin dehydrogenase (NAD+); (5Z,13E)-(15S)-11α,15-dihydroxy-9-oxoprost-13-enoate:NAD+ 15-oxidoreductase
Systematic name: (5Z,13E,15S)-11α,15-dihydroxy-9-oxoprost-5,13-dienoate:NAD+ 15-oxidoreductase
Comments: Acts on prostaglandin E2, F and B1, but not on prostaglandin D2. cf. EC 1.1.1.196 15-hydroxyprostaglandin-D dehydrogenase (NADP+) and EC 1.1.1.197 15-hydroxyprostaglandin dehydrogenase (NADP+).
References:
1.  Änggaard, E. and Samuelsson, B. Purification and properties of a 15-hydroxyprostaglandin dehydrogenase from swine lung. Prostaglandins 25 (1996) 293–300.
2.  Braithwaite, S.S. and Jarabak, J. Studies on a 15-hydroxyprostaglandin dehydrogenase from human placenta. Purification and partial characterization. J. Biol. Chem. 250 (1975) 2315–2318. [PMID: 1117007]
3.  Lee, S.-C. and Levine, L. Prostaglandin metabolism. II. Identification of two 15-hydroxyprostaglandin dehydrogenase types. J. Biol. Chem. 250 (1975) 548–552. [PMID: 234431]
4.  Lee, S.-C., Pong, S.-S., Katzen, D., Wu, K.-Y. and Levine, L. Distribution of prostaglandin E 9-ketoreductase and types I and II 15-hydroxyprostaglandin dehydrogenase in swine kidney medulla and cortex. Biochemistry 14 (1975) 142–145. [PMID: 803247]
[EC 1.1.1.141 created 1972]
 
 
EC 1.1.1.142     
Accepted name: D-pinitol dehydrogenase
Reaction: 1D-3-O-methyl-chiro-inositol + NADP+ = 2D-5-O-methyl-2,3,5/4,6-pentahydroxycyclohexanone + NADPH + H+
Other name(s): 5D-5-O-methyl-chiro-inositol:NADP+ oxidoreductase
Systematic name: 1D-3-O-methyl-chiro-inositol:NADP+ oxidoreductase
References:
1.  Ruis, H. and Hoffmann-Ostenhof, O. Enzymic epimerization of sequoyitol to D-pinitol in Trifolium incarnatum. Eur. J. Biochem. 7 (1969) 442–448. [PMID: 4389340]
[EC 1.1.1.142 created 1972]
 
 
EC 1.1.1.143     
Accepted name: sequoyitol dehydrogenase
Reaction: 5-O-methyl-myo-inositol + NAD+ = 2D-5-O-methyl-2,3,5/4,6-pentahydroxycyclohexanone + NADH + H+
Other name(s): D-pinitol dehydrogenase
Systematic name: 5-O-methyl-myo-inositol:NAD+ oxidoreductase
References:
1.  Ruis, H. and Hoffmann-Ostenhof, O. Enzymic epimerization of sequoyitol to D-pinitol in Trifolium incarnatum. Eur. J. Biochem. 7 (1969) 442–448. [PMID: 4389340]
[EC 1.1.1.143 created 1972]
 
 
EC 1.1.1.144     
Accepted name: perillyl-alcohol dehydrogenase
Reaction: perillyl alcohol + NAD+ = perillyl aldehyde + NADH + H+
Other name(s): perillyl alcohol dehydrogenase
Systematic name: perillyl-alcohol:NAD+ oxidoreductase
Comments: Oxidizes a number of primary alcohols with the alcohol group allylic to an endocyclic double bond and a 6-membered ring, either aromatic or hydroaromatic.
References:
1.  Ballal, N.R., Bhattacharyya, P.K. and Rangachari, P.N. Perillyl alcohol dehydrogenase from a soil pseudomonad. Biochem. Biophys. Res. Commun. 23 (1966) 473–478. [PMID: 4289759]
[EC 1.1.1.144 created 1972]
 
 
EC 1.1.1.145     
Accepted name: 3β-hydroxy-Δ5-steroid dehydrogenase
Reaction: a 3β-hydroxy-Δ5-steroid + NAD+ = a 3-oxo-Δ5-steroid + NADH + H+
Other name(s): progesterone reductase; Δ5-3β-hydroxysteroid dehydrogenase; 3β-hydroxy-5-ene steroid dehydrogenase; 3β-hydroxy steroid dehydrogenase/isomerase; 3β-hydroxy-Δ5-C27-steroid dehydrogenase/isomerase; 3β-hydroxy-Δ5-C27-steroid oxidoreductase; 3β-hydroxy-5-ene-steroid oxidoreductase; steroid-Δ5-3β-ol dehydrogenase; 3β-HSDH; 5-ene-3-β-hydroxysteroid dehydrogenase; 3β-hydroxy-5-ene-steroid dehydrogenase
Systematic name: 3β-hydroxy-Δ5-steroid:NAD+ 3-oxidoreductase
Comments: This activity is found in several bifunctional enzymes that catalyse the oxidative conversion of Δ5-3-hydroxy steroids to a Δ4-3-oxo configuration. This conversion is carried out in two separate, sequential reactions; in the first reaction, which requires NAD+, the enzyme catalyses the dehydrogenation of the 3β-hydroxy steroid to a 3-oxo intermediate. In the second reaction the reduced coenzyme, which remains attached to the enzyme, activates the isomerization of the Δ5 form to a Δ4 form (cf. EC 5.3.3.1, steroid Δ-isomerase). Substrates include dehydroepiandrosterone (which is converted into androst-5-ene-3,17-dione), pregnenolone (converted to progesterone) and cholest-5-en-3-one, an intermediate of cholesterol degradation.
References:
1.  Cheatum, S.G. and Warren, J.C. Purification and properties of 3-β-hydroxysteroid dehydrogenase and Δ-5-3-ketosteroid isomerase from bovine corpora lutea. Biochim. Biophys. Acta 122 (1966) 1–13. [PMID: 4226148]
2.  Koritz, S.B. The conversion of prepnenolone to progesterone by small particle from rat adrenal. Biochemistry 3 (1964) 1098–1102. [PMID: 14220672]
3.  Neville, A.M., Orr, J.C. and Engel, L.L. Δ5-3β-Hydroxy steroid dehydrogenase activities of bovine adrenal cortex. Biochem. J. 107 (1968) 20.
[EC 1.1.1.145 created 1972]
 
 
EC 1.1.1.146     
Accepted name: 11β-hydroxysteroid dehydrogenase
Reaction: an 11β-hydroxysteroid + NADP+ = an 11-oxosteroid + NADPH + H+
Other name(s): corticosteroid 11β-dehydrogenase; β-hydroxysteroid dehydrogenase; 11β-hydroxy steroid dehydrogenase; corticosteroid 11-reductase; dehydrogenase, 11β-hydroxy steroid
Systematic name: 11β-hydroxysteroid:NADP+ 11-oxidoreductase
References:
1.  Agarwal, A.K., Monder, C., Eckstein, B. and White, P.C. Cloning and expression of rat cDNA encoding corticosteroid 11β-dehydrogenase. J. Biol. Chem. 264 (1989) 18939–18943. [PMID: 2808402]
2.  Bush, I.E., Hunter, S.A. and Meigs, R.A. Metabolism of 11-oxygenated steroids. Metabolism in vitro by preparations of liver. Biochem. J. 107 (1968) 239–258. [PMID: 4384445]
3.  Lakshmi, V. and Monder, C. Purification and characterization of the corticosteroid 11β-dehydrogenase component of the rat liver 11β-hydroxysteroid dehydrogenase complex. Endocrinology 123 (1988) 2390–2398. [PMID: 3139396]
4.  Phillips, D.M., Lakshmi, V. and Monder, C. Corticosteroid 11β-dehydrogenase in rat testis. Endocrinology 125 (1989) 209–216. [PMID: 2661206]
[EC 1.1.1.146 created 1972]
 
 
EC 1.1.1.147     
Accepted name: 16α-hydroxysteroid dehydrogenase
Reaction: a 16α-hydroxysteroid + NAD(P)+ = a 16-oxosteroid + NAD(P)H + H+
Other name(s): 16α-hydroxy steroid dehydrogenase
Systematic name: 16α-hydroxysteroid:NAD(P)+ 16-oxidoreductase
References:
1.  Meigs, R.A. and Ryan, K.J. 16-α-Hydroxysteroid dehydrogenase of rat kidney. Purification, assay, and properties. J. Biol. Chem. 241 (1966) 4011–4015. [PMID: 4380686]
[EC 1.1.1.147 created 1972]
 
 
EC 1.1.1.148     
Accepted name: estradiol 17α-dehydrogenase
Reaction: estradiol-17α + NAD(P)+ = estrone + NAD(P)H + H+
Other name(s): 17α-estradiol dehydrogenase; 17α-hydroxy steroid dehydrogenase; 17α-hydroxy steroid oxidoreductase; 17α-hydroxysteroid oxidoreductase; estradiol 17α-oxidoreductase
Systematic name: 17α-hydroxysteroid:NAD(P)+ 17-oxidoreductase
References:
1.  Renwick, A.G.C. and Engel, L.L. The partial purification of 17α- and 17β-estradiol dehydrogenase activities from chicken liver. Biochim. Biophys. Acta 146 (1967) 336–348. [PMID: 4383682]
[EC 1.1.1.148 created 1972]
 
 
EC 1.1.1.149     
Accepted name: 20α-hydroxysteroid dehydrogenase
Reaction: 17α,20α-dihydroxypregn-4-en-3-one + NAD(P)+ = 17α-hydroxyprogesterone + NAD(P)H + H+
Other name(s): 20α-hydroxy steroid dehydrogenase; 20α-HSD; 20α-HSDH
Systematic name: 20α-hydroxysteroid:NAD(P)+ 20-oxidoreductase
Comments: Re-specific with respect to NAD(P)+ (cf. EC 1.1.1.62 17β-estradiol 17-dehydrogenase).
References:
1.  Shikita, M., Inano, H. and Tamaoki, B. Further studies on 20α-hydroxysteroid dehydrogenase of rat testes. Biochemistry 6 (1967) 1760–1764. [PMID: 4382486]
2.  Strickler, R.C., Tobias, B. and Covey, D.F. Human placental 17β-estradiol dehydrogenase and 20α-hydroxysteroid dehydrogenase. Two activities at a single enzyme active site. J. Biol. Chem. 256 (1981) 316–321. [PMID: 6935192]
[EC 1.1.1.149 created 1972, deleted 1983, reinstated 1986]
 
 
EC 1.1.1.150     
Accepted name: 21-hydroxysteroid dehydrogenase (NAD+)
Reaction: pregnan-21-ol + NAD+ = pregnan-21-al + NADH + H+
Other name(s): 21-hydroxysteroid dehydrogenase (NAD)
Systematic name: 21-hydroxysteroid:NAD+ 21-oxidoreductase
Comments: Acts on a number of 21-hydroxycorticosteroids.
References:
1.  Monder, C. and White, A. The 21-hydroxysteroid dehydrogenases of liver. A nicotinamide adenine dinucleotide phosphate dehydrogenase and two nicotinamide adenine dinucleotide dehydrogenases. J. Biol. Chem. 240 (1965) 71–77. [PMID: 14253469]
[EC 1.1.1.150 created 1972]
 
 
EC 1.1.1.151     
Accepted name: 21-hydroxysteroid dehydrogenase (NADP+)
Reaction: pregnan-21-ol + NADP+ = pregnan-21-al + NADPH + H+
Other name(s): 21-hydroxy steroid dehydrogenase; 21-hydroxy steroid (nicotinamide adenine dinucleotide phosphate) dehydrogenase; 21-hydroxy steroid dehydrogenase (nicotinamide adenine dinucleotide phosphate); NADP-21-hydroxysteroid dehydrogenase; 21-hydroxysteroid dehydrogenase (NADP)
Systematic name: 21-hydroxysteroid:NADP+ 21-oxidoreductase
Comments: Acts on a number of 21-hydroxycorticosteroids.
References:
1.  Monder, C. and White, A. The 21-hydroxysteroid dehydrogenases of liver. A nicotinamide adenine dinucleotide phosphate dehydrogenase and two nicotinamide adenine dinucleotide dehydrogenases. J. Biol. Chem. 240 (1965) 71–77. [PMID: 14253469]
[EC 1.1.1.151 created 1972]
 
 
EC 1.1.1.152     
Accepted name: 3α-hydroxy-5β-androstane-17-one 3α-dehydrogenase
Reaction: 3α-hydroxy-5β-androstane-17-one + NAD+ = 5β-androstane-3,17-dione + NADH + H+
Other name(s): etiocholanolone 3α-dehydrogenase; etiocholanolone 3α-dehydrogenase; 3α-hydroxy-5β-steroid dehydrogenase
Systematic name: 3α-hydroxy-5β-steroid:NAD+ 3-oxidoreductase
References:
1.  Roe, C.R. and Kaplan, N.O. Purification and substrate specificities of bacterial hydroxysteroid dehydrogenases. Biochemistry 8 (1969) 5093–5103. [PMID: 5365796]
[EC 1.1.1.152 created 1972]
 
 
EC 1.1.1.153     
Accepted name: sepiapterin reductase (L-erythro-7,8-dihydrobiopterin forming)
Reaction: (1) L-erythro-7,8-dihydrobiopterin + NADP+ = sepiapterin + NADPH + H+
(2) L-erythro-tetrahydrobiopterin + 2 NADP+ = 6-pyruvoyl-5,6,7,8-tetrahydropterin + 2 NADPH + 2 H+
Glossary: sepiapterin = 2-amino-6-lactoyl-7,8-dihydropteridin-4(3H)-one
tetrahydrobiopterin = 5,6,7,8-tetrahydrobiopterin = 2-amino-6-(1,2-dihydroxypropyl)-5,6,7,8-tetrahydropteridin-4(3H)-one
Other name(s): SR
Systematic name: L-erythro-7,8-dihydrobiopterin:NADP+ oxidoreductase
Comments: This enzyme catalyses the final step in the de novo synthesis of tetrahydrobiopterin from GTP. The enzyme, which is found in higher animals and some fungi and bacteria, produces the erythro form of tetrahydrobiopterin. cf. EC 1.1.1.325, sepiapterin reductase (L-threo-7,8-dihydrobiopterin forming).
References:
1.  Katoh, S. Sepiapterin reductase from horse liver: purification and properties of the enzyme. Arch. Biochem. Biophys. 146 (1971) 202–214. [PMID: 4401291]
2.  Matsubara, M., Katoh, S., Akino, M. and Kaufman, S. Sepiapterin reductase. Biochim. Biophys. Acta 122 (1966) 202–212. [PMID: 5969298]
3.  Werner, E.R., Schmid, M., Werner-Felmayer, G., Mayer, B. and Wachter, H. Synthesis and characterization of 3H-labelled tetrahydrobiopterin. Biochem. J. 304 (1994) 189–193. [PMID: 7528005]
4.  Kim, Y.A., Chung, H.J., Kim, Y.J., Choi, Y.K., Hwang, Y.K., Lee, S.W. and Park, Y.S. Characterization of recombinant Dictyostelium discoideum sepiapterin reductase expressed in E. coli. Mol. Cells 10 (2000) 405–410. [PMID: 10987137]
[EC 1.1.1.153 created 1972, modified 2012]
 
 
EC 1.1.1.154     
Accepted name: ureidoglycolate dehydrogenase
Reaction: (S)-ureidoglycolate + NAD(P)+ = oxalureate + NAD(P)H + H+
Systematic name: (S)-ureidoglycolate:NAD(P)+ oxidoreductase
References:
1.  van der Drift, C., van Helvoort, P.E. and Vogels, G.D. S-Ureidoglycolate dehydrogenase: purification and properties. Arch. Biochem. Biophys. 145 (1971) 465–469. [PMID: 4399430]
[EC 1.1.1.154 created 1976]
 
 
EC 1.1.1.155      
Deleted entry: homoisocitrate dehydrogenase. The enzyme is identical to EC 1.1.1.87, homoisocitrate dehydrogenase
[EC 1.1.1.155 created 1976, deleted 2004]
 
 
EC 1.1.1.156     
Accepted name: glycerol 2-dehydrogenase (NADP+)
Reaction: glycerol + NADP+ = glycerone + NADPH + H+
Other name(s): dihydroxyacetone reductase; dihydroxyacetone (reduced nicotinamide adenine dinucleotide phosphate) reductase; dihydroxyacetone reductase (NADPH); DHA oxidoreductase; glycerol 2-dehydrogenase (NADP)
Systematic name: glycerol:NADP+ 2-oxidoreductase (glycerone-forming)
References:
1.  Ben-Amotz, A. and Avron, M. NADP specific dihydroxyacetone reductase from Dunaliella parva. FEBS Lett. 29 (1973) 153–155. [PMID: 4146296]
[EC 1.1.1.156 created 1976]
 
 
EC 1.1.1.157     
Accepted name: 3-hydroxybutyryl-CoA dehydrogenase
Reaction: (S)-3-hydroxybutanoyl-CoA + NADP+ = 3-acetoacetyl-CoA + NADPH + H+
Other name(s): β-hydroxybutyryl coenzyme A dehydrogenase; L(+)-3-hydroxybutyryl-CoA dehydrogenase; BHBD; dehydrogenase, L-3-hydroxybutyryl coenzyme A (nicotinamide adenine dinucleotide phosphate); L-(+)-3-hydroxybutyryl-CoA dehydrogenase; β-hydroxybutyryl-CoA dehydrogenase
Systematic name: (S)-3-hydroxybutanoyl-CoA:NADP+ oxidoreductase
References:
1.  Madan, V.K., Hillmer, P. and Gottschalk, G. Purification and properties of NADP-dependent L(+)-3-hydroxybutyryl-CoA dehydrogenase from Clostridium kluyveri. Eur. J. Biochem. 32 (1973) 51–56. [PMID: 4405720]
[EC 1.1.1.157 created 1976]
 
 
EC 1.1.1.158      
Transferred entry: UDP-N-acetylmuramate dehydrogenase. Now EC 1.3.1.98, UDP-N-acetylmuramate dehydrogenase
[EC 1.1.1.158 created 1976, modified 1983, modified 2002, deleted 2013]
 
 
EC 1.1.1.159     
Accepted name: 7α-hydroxysteroid dehydrogenase
Reaction: cholate + NAD+ = 3α,12α-dihydroxy-7-oxo-5β-cholan-24-oate + NADH + H+
Glossary: cholate = 3α,7α,12α-trihydroxy-5β-cholan-24-oate
Other name(s): 7α-hydroxy steroid dehydrogenase; 7α-HSDH
Systematic name: 7α-hydroxysteroid:NAD+ 7-oxidoreductase
Comments: Catalyses the oxidation of the 7α-hydroxy group of bile acids and alcohols both in their free and conjugated forms. The Bacteroides fragilis and Clostridium enzymes can also utilize NADP+.
References:
1.  Haslewood, E.S. and Haslewood, G.A.D. The specificity of a 7α-hydroxy steroid dehydrogenase from Escherichia coli. Biochem. J. 157 (1976) 207–210. [PMID: 786279]
2.  Macdonald, I.A. and Roach, P.D. Bile induction of 7α- and 7β-hydroxysteroid dehydrogenases in Clostridium absonum. Biochim. Biophys. Acta 665 (1981) 262–269. [PMID: 6945134]
3.  Macdonald, I.A., Williams, C.N. and Mahony, D.E. 7α-Hydroxysteroid dehydrogenase from Escherichia coli B: preliminary studies. Biochim. Biophys. Acta 309 (1973) 243–253. [PMID: 4581498]
4.  Macdonald, I.A., Williams, C.N., Mahony, D.E. and Christie, W.M. NAD- and NADP-dependent 7α-hydroxysteroid dehydrogenases from Bacteroides fragilis. Biochim. Biophys. Acta 384 (1975) 12–24. [PMID: 236764]
[EC 1.1.1.159 created 1976, modified 1980]
 
 
EC 1.1.1.160     
Accepted name: dihydrobunolol dehydrogenase
Reaction: (±)-5-[(tert-butylamino)-2′-hydroxypropoxy]-1,2,3,4-tetrahydro-1-naphthol + NADP+ = (±)-5-[(tert-butylamino)-2′-hydroxypropoxy]-3,4-dihydro-1(2H)-naphthalenone + NADPH + H+
Other name(s): bunolol reductase
Systematic name: (±)-5-[(tert-butylamino)-2′-hydroxypropoxy]-1,2,3,4-tetrahydro-1-naphthol:NADP+ oxidoreductase
Comments: Also acts, more slowly, with NAD+.
References:
1.  Leinweber, F.-J., Greenough, R.C., Schwender, C.F., Kaplan, H.R. and DiCarlo, F.J. Bunolol metabolism by cell-free preparations of human liver: biosynthesis of dihydrobunolol. Xenobiotica 2 (1972) 191–202. [PMID: 4560367]
[EC 1.1.1.160 created 1976]
 
 
EC 1.1.1.161      
Deleted entry: cholestanetetraol 26-dehydrogenase. The activity is part of EC 1.14.13.15, cholestanetriol 26-monooxygenase
[EC 1.1.1.161 created 1976, deleted 2012]
 
 
EC 1.1.1.162     
Accepted name: erythrulose reductase
Reaction: D-threitol + NADP+ = D-erythrulose + NADPH + H+
Other name(s): D-erythrulose reductase; erythritol:NADP+ oxidoreductase
Systematic name: D-threitol:NADP+ oxidoreductase
Comments: NAD+ is also utilized, but more slowly.
References:
1.  Uehara, K., Tanimoto, T. and Sato, H. Studies on D-tetrose metabolism. IV. Purification and some properties of D-erythrulose reductase from beef liver. J. Biochem. (Tokyo) 75 (1974) 333–345. [PMID: 4152124]
2.  Uehara, K. and Hosomi, S. D-Erythrulose reductase from beef liver. Methods Enzymol. 89 (1982) 232–237. [PMID: 6292658]
[EC 1.1.1.162 created 1976]
 
 
EC 1.1.1.163     
Accepted name: cyclopentanol dehydrogenase
Reaction: cyclopentanol + NAD+ = cyclopentanone + NADH + H+
Systematic name: cyclopentanol:NAD+ oxidoreductase
Comments: 4-Methylcyclohexanol and cyclohexanol can also act as substrates.
References:
1.  Griffin, M. and Trudgill, P.W. The metabolism of cyclopentanol by Pseudomonas N.C.I.B. 9872. Biochem. J. 129 (1972) 595–603. [PMID: 4349113]
2.  Iwaki, H., Hasegawa, Y., Wang, S., Kayser, M.M. and Lau, P.C. Cloning and characterization of a gene cluster involved in cyclopentanol metabolism in Comamonas sp. strain NCIMB 9872 and biotransformations effected by Escherichia coli-expressed cyclopentanone 1,2-monooxygenase. Appl. Environ. Microbiol. 68 (2002) 5671–5684. [PMID: 12406764]
[EC 1.1.1.163 created 1976]
 
 
EC 1.1.1.164     
Accepted name: hexadecanol dehydrogenase
Reaction: hexadecanol + NAD+ = hexadecanal + NADH + H+
Systematic name: hexadecanol:NAD+ oxidoreductase
Comments: The liver enzyme acts on long-chain alcohols from C8 to C16. The Euglena enzyme also oxidizes the corresponding aldehydes to fatty acids.
References:
1.  Kolattukuday, P.E. Reduction of fatty acids to alcohols by cell-free preparations of Euglena gracilis. Biochemistry 9 (1970) 1095–1102. [PMID: 4313936]
2.  Stoffel, W., Le Kim, D. and Heyn, G. Metabolism of sphingosine bases. XIV. Sphinganine (dihydrosphingosine), an effective donor of the alk-1-enyl chain of plasmalogens. Hoppe-Seyler's Z. Physiol. Chem. 351 (1970) 875–883. [PMID: 5432753]
[EC 1.1.1.164 created 1976]
 
 
EC 1.1.1.165     
Accepted name: 2-alkyn-1-ol dehydrogenase
Reaction: 2-butyne-1,4-diol + NAD+ = 4-hydroxy-2-butynal + NADH + H+
Systematic name: 2-butyne-1,4-diol:NAD+ 1-oxidoreductase
Comments: Acts on a variety of 2-alkyn-1-ols, and also on 1,4-butanediol. NADP+ also acts as acceptor, but more slowly.
References:
1.  Miyoshi, T., Sato, H. and Harada, T. Purification and characterization of 2-alkyne-1-ol dehydrogenase induced by 2-butene-1,4-diol in Fusarium merismoides B11. Biochim. Biophys. Acta 358 (1974) 231–239.
[EC 1.1.1.165 created 1976]
 
 
EC 1.1.1.166     
Accepted name: hydroxycyclohexanecarboxylate dehydrogenase
Reaction: (1S,3R,4S)-3,4-dihydroxycyclohexane-1-carboxylate + NAD+ = (1S,4S)-4-hydroxy-3-oxocyclohexane-1-carboxylate + NADH + H+
Other name(s): dihydroxycyclohexanecarboxylate dehydrogenase; (-)t-3,t-4-dihydroxycyclohexane-c-1-carboxylate-NAD+ oxidoreductase
Systematic name: (1S,3R,4S)-3,4-dihydroxycyclohexane-1-carboxylate:NAD+ 3-oxidoreductase
Comments: Acts on hydroxycyclohexanecarboxylates that have an equatorial carboxy group at C-1, an axial hydroxy group at C-3 and an equatorial hydroxy or carbonyl group at C-4, including (-)-quinate and (-)-shikimate.
References:
1.  Whiting, G.C. and Coggins, R.A. A new nicotinamide-adenine dinucleotide-dependent hydroaromatic dehydrogenase of Lactobacillus plantarum and its role in formation of (-)t-3,t-4-dihydroxycyclohexane-c-1-carboxylate. Biochem. J. 141 (1974) 35–42. [PMID: 4375976]
[EC 1.1.1.166 created 1976]
 
 
EC 1.1.1.167     
Accepted name: hydroxymalonate dehydrogenase
Reaction: hydroxymalonate + NAD+ = oxomalonate + NADH + H+
Systematic name: hydroxymalonate:NAD+ oxidoreductase
References:
1.  Jukova, N.I., Klunova, S.M. and Philippovich, Y.B. Biochemistry of Insects, issue 17. , V.I. Lenin State Pedagogical Institute, Moscow, 1971, p. 56.
[EC 1.1.1.167 created 1976]
 
 
EC 1.1.1.168     
Accepted name: 2-dehydropantolactone reductase (Re-specific)
Reaction: (R)-pantolactone + NADP+ = 2-dehydropantolactone + NADPH + H+
Other name(s): 2-oxopantoyl lactone reductase; ketopantoyl lactone reductase; 2-ketopantoyl lactone reductase; 2-dehydropantoyl-lactone reductase (A-specific); (R)-pantolactone:NADP+ oxidoreductase (A-specific); 2-dehydropantolactone reductase (A-specific)
Systematic name: (R)-pantolactone:NADP+ oxidoreductase (Re-specific)
Comments: The yeast enzyme differs from that from Escherichia coli [EC 1.1.1.214 2-dehydropantolactone reductase (Si-specific)], which is specific for the Si-face of NADP+, and in receptor requirements from EC 1.1.99.26 3-hydroxycyclohexanone dehydrogenase.
References:
1.  King, H.L., Jr., Dyar, R.E. and Wilken, D.R. Ketopantoyl lactone and ketopantoic acid reductases. Characterization of the reactions and purification of two forms of ketopantoyl lactone reductase. J. Biol. Chem. 247 (1972) 4689–4695. [PMID: 4603075]
2.  Wilken, D.R., King, H.L., Jr. and Dyar, R.E. Ketopantoic acid and ketopantoyl lactone reductases. Stereospecificity of transfer of hydrogen from reduced nicotinamide adenine dinucleotide phosphate. J. Biol. Chem. 250 (1975) 2311–2314. [PMID: 234966]
[EC 1.1.1.168 created 1976, modified 1986, modified 1999]
 
 
EC 1.1.1.169     
Accepted name: 2-dehydropantoate 2-reductase
Reaction: (R)-pantoate + NADP+ = 2-dehydropantoate + NADPH + H+
Glossary: pantoate = 2,4-dihydroxy-3,3-dimethylbutanoate
Other name(s): 2-oxopantoate reductase; 2-ketopantoate reductase; 2-ketopantoic acid reductase; ketopantoate reductase; ketopantoic acid reductase
Systematic name: (R)-pantoate:NADP+ 2-oxidoreductase
References:
1.  King, H.L., Jr., Dyar, R.E. and Wilken, D.R. Ketopantoyl lactone and ketopantoic acid reductases. Characterization of the reactions and purification of two forms of ketopantoyl lactone reductase. J. Biol. Chem. 247 (1972) 4689–4695. [PMID: 4603075]
[EC 1.1.1.169 created 1976]
 
 
EC 1.1.1.170     
Accepted name: 3β-hydroxysteroid-4α-carboxylate 3-dehydrogenase (decarboxylating)
Reaction: a 3β-hydroxysteroid-4α-carboxylate + NAD(P)+ = a 3-oxosteroid + CO2 + NAD(P)H
Other name(s): 3β-hydroxy-4β-methylcholestenecarboxylate 3-dehydrogenase (decarboxylating); 3β-hydroxy-4β-methylcholestenoate dehydrogenase; sterol 4α-carboxylic decarboxylase; sterol-4α-carboxylate 3-dehydrogenase (decarboxylating) (ambiguous); ERG26 (gene name); NSDHL (gene name)
Systematic name: 3β-hydroxysteroid-4α-carboxylate:NAD(P)+ 3-oxidoreductase (decarboxylating)
Comments: The enzyme participates in the biosynthesis of several important sterols such as ergosterol and cholesterol. It is part of a three enzyme system that removes methyl groups from the C-4 position of steroid molecules. The first enzyme, EC 1.14.18.9, 4α-methylsterol monooxygenase, catalyses three successive oxidations of the methyl group, resulting in a carboxyl group; the second enzyme, EC 1.1.1.170, catalyses an oxidative decarboxylation that results in a reduction of the 3β-hydroxy group at the C-3 carbon to an oxo group; and the last enzyme, EC 1.1.1.270, 3β-hydroxysteroid 3-dehydrogenase, reduces the 3-oxo group back to a 3β-hydroxyl. If a second methyl group remains at the C-4 position, this enzyme also catalyses its epimerization from 4β to 4α orientation, so it could serve as a substrate for a second round of demethylation. cf. EC 1.1.1.418, plant 3β-hydroxysteroid-4α-carboxylate 3-dehydrogenase (decarboxylating).
References:
1.  Sharpless, K.B., Snyder, T.E., Spencer, T.A., Maheshwari, K.K. and Nelson, J.A. Biological demethylation of 4,4-dimethyl sterols, Evidence for enzymic epimerization of the 4β-methyl group prior to its oxidative removal. J. Am. Chem. Soc. 91 (1969) 3394–3396. [PMID: 5791927]
2.  Rahimtula, A.D. and Gaylor, J.L. Partial purification of a microsomal sterol 4α-carboxylic acid decarboxylase. J. Biol. Chem. 247 (1972) 9–15. [PMID: 4401584]
3.  Brady, D.R., Crowder, R.D. and Hayes, W.J. Mixed function oxidases in sterol metabolism. Source of reducing equivalents. J. Biol. Chem. 255 (1980) 10624–10629. [PMID: 7430141]
4.  Gachotte, D., Barbuch, R., Gaylor, J., Nickel, E. and Bard, M. Characterization of the Saccharomyces cerevisiae ERG26 gene encoding the C-3 sterol dehydrogenase (C-4 decarboxylase) involved in sterol biosynthesis. Proc. Natl. Acad. Sci. USA 95 (1998) 13794–13799. [PMID: 9811880]
5.  Caldas, H. and Herman, G.E. NSDHL, an enzyme involved in cholesterol biosynthesis, traffics through the Golgi and accumulates on ER membranes and on the surface of lipid droplets. Hum. Mol. Genet. 12 (2003) 2981–2991. [PMID: 14506130]
[EC 1.1.1.170 created 1978, modified 2002, modified 2012, modified 2019]
 
 
EC 1.1.1.171      
Transferred entry: methylenetetrahydrofolate reductase (NADPH). Now EC 1.5.1.20, methylenetetrahydrofolate reductase [NAD(P)H]
[EC 1.1.1.171 created 1978, deleted 1984]
 
 
EC 1.1.1.172     
Accepted name: 2-oxoadipate reductase
Reaction: 2-hydroxyadipate + NAD+ = 2-oxoadipate + NADH + H+
Other name(s): 2-ketoadipate reductase; α-ketoadipate reductase; 2-ketoadipate reductase
Systematic name: 2-hydroxyadipate:NAD+ 2-oxidoreductase
References:
1.  Suda, T., Robinson, J.C. and Fjellstedt, T.A. Purification and properties of α-ketoadipate reductase, a newly discovered enzyme from human placenta. Arch. Biochem. Biophys. 176 (1976) 610–620. [PMID: 185965]
[EC 1.1.1.172 created 1978]
 
 
EC 1.1.1.173     
Accepted name: L-rhamnose 1-dehydrogenase
Reaction: L-rhamnofuranose + NAD+ = L-rhamno-1,4-lactone + NADH + H+
Systematic name: L-rhamnofuranose:NAD+ 1-oxidoreductase
References:
1.  Rigo, L.U., Maréchal, L.R., Vieira, M.M. and Veiga, L.A. Oxidative pathway for L-rhamnose degradation in Pallularia pullulans. Can. J. Microbiol. 31 (1985) 817–822.
2.  Rigo, L.U., Nakano, M., Veiga, L.A. and Feingold, D.S. L-Rhamnose dehydrogenase of Pullularia pullulans. Biochim. Biophys. Acta 445 (1976) 286–293. [PMID: 8142]
[EC 1.1.1.173 created 1978]
 
 
EC 1.1.1.174     
Accepted name: cyclohexane-1,2-diol dehydrogenase
Reaction: trans-cyclohexane-1,2-diol + NAD+ = 2-hydroxycyclohexan-1-one + NADH + H+
Systematic name: trans-cyclohexane-1,2-diol:NAD+ 1-oxidoreductase
Comments: Also oxidizes, more slowly, the cis isomer and 2-hydroxycyclohexanone.
References:
1.  Davey, J.F. and Trudgill, P.W. The metabolism of trans-cyclohexan-1,2-diol by an Acinetobacter species. Eur. J. Biochem. 74 (1977) 115–127. [PMID: 856571]
[EC 1.1.1.174 created 1978]
 
 
EC 1.1.1.175     
Accepted name: D-xylose 1-dehydrogenase
Reaction: D-xylose + NAD+ = D-xylonolactone + NADH + H+
Other name(s): NAD-D-xylose dehydrogenase; D-xylose dehydrogenase; (NAD)-linked D-xylose dehydrogenase
Systematic name: D-xylose:NAD+ 1-oxidoreductase
References:
1.  Yamanaka, K., Gino, M. and Kaneda, R. A specific NAD-D-xylose dehydrogenase from Arthrobacter sp. Agric. Biol. Chem. 41 (1977) 1493–1499.
[EC 1.1.1.175 created 1978]
 
 
EC 1.1.1.176     
Accepted name: 12α-hydroxysteroid dehydrogenase
Reaction: cholate + NADP+ = 3α,7α-dihydroxy-12-oxo-5β-cholan-24-oate + NADPH + H+
Glossary: cholate = 3α,7α,12α-trihydroxy-5β-cholan-24-oate
Other name(s): 12α-hydroxy steroid dehydrogenase; NAD+-dependent 12α-hydroxysteroid dehydrogenase; NADP+-12α-hydroxysteroid dehydrogenase
Systematic name: 12α-hydroxysteroid:NADP+ 12-oxidoreductase
Comments: Catalyses the oxidation of the 12α-hydroxy group of bile acids, both in their free and conjugated form. Also acts on bile alcohols.
References:
1.  Macdonald, I.A., Mahony, D.E., Jellett, J.F. and Meier, C.E. NAD-dependent 3α- and 12α-hydroxysteroid dehydrogenase activities from Eubacterium lentum ATCC no. 25559. Biochim. Biophys. Acta 489 (1977) 466–476. [PMID: 201289]
2.  Mahony, D.E., Meier, C.E., Macdonald, I.A. and Holdeman, L.V. Bile salt degradation by nonfermentative clostridia. Appl. Environ. Microbiol. 34 (1977) 419–423. [PMID: 921266]
[EC 1.1.1.176 created 1978]
 
 
EC 1.1.1.177     
Accepted name: glycerol-3-phosphate 1-dehydrogenase (NADP+)
Reaction: sn-glycerol 3-phosphate + NADP+ = D-glyceraldehyde 3-phosphate + NADPH + H+
Other name(s): glycerol phosphate (nicotinamide adenine dinucleotide phosphate) dehydrogenase; L-glycerol 3-phosphate:NADP+ oxidoreductase; glycerin-3-phosphate dehydrogenase; NADPH-dependent glycerin-3-phosphate dehydrogenase; NADP-specific glycerol 3-phosphate 1-dehydrogenase
Systematic name: sn-glycerol-3-phosphate:NADP+ 1-oxidoreductase
References:
1.  Glushankov, P.E., Epifanova, V.E. and Kolotilova, A.I. Pentose phosphate pathway of carbohydrate metabolism and NADP-dependent glycerol 3-phosphate dehydrogenase activity in some white rat tissues. Biokhimiya 41 (1976) 1788–1790. [PMID: 1024580] (in Russian)
2.  Wood, T. Catalysis of pentose phosphate pathway reactions by cytoplasmic fractions from muscle, uterus and liver of the rat, and the presence of a reduced nicotinamide-adenine dinucleotide phosphate-triose phosphate oxidoreductase in rat muscle. Biochem. J. 138 (1974) 71–76. [PMID: 4152128]
[EC 1.1.1.177 created 1980, modified 1980]
 
 
EC 1.1.1.178     
Accepted name: 3-hydroxy-2-methylbutyryl-CoA dehydrogenase
Reaction: (2S,3S)-3-hydroxy-2-methylbutanoyl-CoA + NAD+ = 2-methylacetoacetyl-CoA + NADH + H+
Other name(s): 2-methyl-3-hydroxybutyryl coenzyme A dehydrogenase; 2-methyl-3-hydroxybutyryl coenzyme A dehydrogenase; 2-methyl-3-hydroxy-butyryl CoA dehydrogenase
Systematic name: (2S,3S)-3-hydroxy-2-methylbutanoyl-CoA:NAD+ oxidoreductase
Comments: Also acts, more slowly, on (2S,3S)-2-hydroxy-3-methylpentanoyl-CoA.
References:
1.  Conrad, R.S., Massey, L.K. and Sokatch, J.R. D- and L-isoleucine metabolism and regulation of their pathways in Pseudomonas putida. J. Bacteriol. 118 (1974) 103–111. [PMID: 4150713]
[EC 1.1.1.178 created 1981]
 
 
EC 1.1.1.179     
Accepted name: D-xylose 1-dehydrogenase (NADP+, D-xylono-1,5-lactone-forming)
Reaction: D-xylose + NADP+ = D-xylono-1,5-lactone + NADPH + H+
Other name(s): D-xylose (nicotinamide adenine dinucleotide phosphate) dehydrogenase (ambiguous); D-xylose-NADP dehydrogenase (ambiguous); D-xylose:NADP+ oxidoreductase (ambiguous); D-xylose 1-dehydrogenase (NADP) (ambiguous)
Systematic name: D-xylose:NADP+ 1-oxidoreductase (D-xylono-1,5-lactone-forming)
Comments: The enzyme, characterized from pig arterial vessels and eye lens, also acts, more slowly, on L-arabinose and D-ribose. cf. EC 1.1.1.424, D-xylose 1-dehydrogenase (NADP+, D-xylono-1,4-lactone-forming).
References:
1.  Wissler, J.H. D-Xylose:NADP oxidoreductase of arterial vessels and eye lens: a new enzyme and a final link in ATP-independent cycling of reducing eqivalents in aldose-polyol-ketose interconversion. Hoppe-Seyler's Z. Physiol. Chem. 358 (1977) 1300–1301.
2.  Wissler, J.H. Direct spectrophotometric and specific quantitative determination of free and bound D-xylose by analytical application of a new enzyme, D-xylose:NADP-oxidoreductase. Fresenius' Z. Anal. Chem. 290 (1978) 179–180.
[EC 1.1.1.179 created 1982, modified 2020]
 
 
EC 1.1.1.180      
Deleted entry:  mannonate dehydrogenase (NAD(P)+). Now included with EC 1.1.1.131 mannuronate reductase
[EC 1.1.1.180 created 1983, deleted 1984]
 
 
EC 1.1.1.181     
Accepted name: cholest-5-ene-3β,7α-diol 3β-dehydrogenase
Reaction: cholest-5-ene-3β,7α-diol + NAD+ = 7α-hydroxycholest-4-en-3-one + NADH + H+
Other name(s): 3β-hydroxy-Δ5-C27-steroid oxidoreductase (ambiguous)
Systematic name: cholest-5-ene-3β,7α-diol:NAD+ 3-oxidoreductase
Comments: Highly specific for 3β,7α-dihydroxy-C27-steroids with Δ5-double bond.
References:
1.  Wikvall, K. Purification and properties of a 3β-hydroxy-Δ5-C27-steroid oxidoreductase from rabbit liver microsomes. J. Biol. Chem. 256 (1981) 3376–3380. [PMID: 6937465]
2.  Schwarz, M., Wright, A.C., Davis, D.L., Nazer, H., Bjorkhem, I. and Russell, D.W. The bile acid synthetic gene 3β-hydroxy-Δ5-C27-steroid oxidoreductase is mutated in progressive intrahepatic cholestasis. J. Clin. Invest. 106 (2000) 1175–1184. [PMID: 11067870]
[EC 1.1.1.181 created 1983]
 
 
EC 1.1.1.182      
Deleted entry:  fenchol dehydrogenase. Now included with EC 1.1.1.198 (+)-borneol dehydrogenase, EC 1.1.1.227 (-)-borneol dehydrogenase and EC 1.1.1.228 (+)-sabinol dehydrogenase
[EC 1.1.1.182 created 1983, deleted 1990]
 
 
EC 1.1.1.183     
Accepted name: geraniol dehydrogenase (NADP+)
Reaction: geraniol + NADP+ = geranial + NADPH + H+
Systematic name: geraniol:NADP+ oxidoreductase
Comments: Also acts, more slowly on farnesol but not on nerol. The enzyme produces a mixture known as citral, which includes geranial and neral. It is still not known whether neral is produced directly by the enzyme, or by isomerization of geranial.
References:
1.  Potty, V.H. and Bruemmer, J.H. Oxidation of geraniol by an enzyme system from orange. Phytochemistry 9 (1970) 1001–1007.
2.  Sekiwa-Iijima, Y., Aizawa, Y. and Kubota, K. Geraniol dehydrogenase activity related to aroma formation in ginger (Zingiber officinale Roscoe). J. Agric. Food Chem. 49 (2001) 5902–5906. [PMID: 11743782]
3.  Saito, Y., Ito, S., Koltunow, A.M. and Sakai, H. Crystallization and preliminary X-ray analysis of geraniol dehydrogenase from Backhousia citriodora (lemon myrtle). Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 67 (2011) 665–667. [PMID: 21636906]
[EC 1.1.1.183 created 1983]
 
 
EC 1.1.1.184     
Accepted name: carbonyl reductase (NADPH)
Reaction: R-CHOH-R′ + NADP+ = R-CO-R′ + NADPH + H+
Other name(s): aldehyde reductase 1; prostaglandin 9-ketoreductase; xenobiotic ketone reductase; NADPH-dependent carbonyl reductase; ALR3; carbonyl reductase; nonspecific NADPH-dependent carbonyl reductase; carbonyl reductase (NADPH2)
Systematic name: secondary-alcohol:NADP+ oxidoreductase
Comments: Acts on a wide range of carbonyl compounds, including quinones, aromatic aldehydes, ketoaldehydes, daunorubicin and prostaglandins E and F, reducing them to the corresponding alcohol. Si-specific with respect to NADPH [cf. EC 1.1.1.2 alcohol dehydrogenase (NADP+)].
References:
1.  Ahmed, N.K., Felsted, R.L. and Bachur, N.R. Heterogeneity of anthracycline antibiotic carbonyl reductases in mammalian livers. Biochem. Pharmacol. 27 (1978) 2713–2719. [PMID: 31888]
2.  Lin, Y.M. and Jarabak, J. Isolation of two proteins with 9-ketoprostaglandin reductase and NADP-linked 15-hydroxyprostaglandin dehydrogenase activities and studies on their inhibition. Biochem. Biophys. Res. Commun. 81 (1978) 1227–1234. [PMID: 666816]
3.  Wermuth, B. Purification and properties of an NADPH-dependent carbonyl reductase from human brain. Relationship to prostaglandin 9-ketoreductase and xenobiotic ketone reductase. J. Biol. Chem. 256 (1981) 1206–1213. [PMID: 7005231]
[EC 1.1.1.184 created 1983]
 
 
EC 1.1.1.185     
Accepted name: L-glycol dehydrogenase
Reaction: an L-glycol + NAD(P)+ = a 2-hydroxycarbonyl compound + NAD(P)H + H+
Other name(s): glycol (nicotinamide adenine dinucleotide (phosphate)) dehydrogenase; L-(+)-glycol:NAD(P) oxidoreductase; L-glycol:NAD(P) dehydrogenase
Systematic name: L-glycol:NAD(P)+ oxidoreductase
Comments: The 2-hydroxycarbonyl compound formed can be further oxidized to a vicinal dicarbonyl compound. In the reverse direction, vicinal diketones, glyceraldehyde, glyoxal, methylglyoxal, 2-oxo-hydroxyketones and 2-ketoacid esters can be reduced.
References:
1.  Bernardo, A., Burgos, J. and Martin, R. Purification and some properties of L-glycol dehydrogenase from hen's muscle. Biochim. Biophys. Acta 659 (1981) 189–198. [PMID: 7018582]
[EC 1.1.1.185 created 1984]
 
 
EC 1.1.1.186     
Accepted name: dTDP-galactose 6-dehydrogenase
Reaction: dTDP-D-galactose + 2 NADP+ + H2O = dTDP-D-galacturonate + 2 NADPH + 2 H+
Other name(s): thymidine-diphosphate-galactose dehydrogenase
Systematic name: dTDP-D-galactose:NADP+ 6-oxidoreductase
References:
1.  Katan, R. and Avigad, G. NADP dependent oxidation of TDP-glucose by an enzyme system from sugar beets. Biochem. Biophys. Res. Commun. 24 (1966) 18–24. [PMID: 4381717]
[EC 1.1.1.186 created 1984, modified 2002]
 
 
EC 1.1.1.187     
Accepted name: GDP-4-dehydro-D-rhamnose reductase
Reaction: (1) GDP-α-D-rhamnose + NAD(P)+ = GDP-4-dehydro-α-D-rhamnose + NAD(P)H + H+
(2) GDP-6-deoxy-α-D-talose + NAD(P)+ = GDP-4-dehydro-α-D-rhamnose + NAD(P)H + H+
Glossary: GDP-α-D-rhamnose = GDP-6-deoxy-α-D-mannose
GDP-4-dehydro-α-D-rhamnose = GDP-4-dehydro-6-deoxy-α-D-mannose
GDP-6-deoxy-α-D-talose = GDP-α-D-pneumose
Other name(s): GDP-4-keto-6-deoxy-D-mannose reductase; GDP-4-keto-D-rhamnose reductase; guanosine diphosphate-4-keto-D-rhamnose reductase; GDP-6-deoxy-D-mannose:NAD(P)+ 4-oxidoreductase; GDP-6-deoxy-α-D-mannose:NAD(P)+ 4-oxidoreductase
Systematic name: GDP-4-dehydro-α-D-rhamnose:NAD(P)+ 4-oxidoreductase
Comments: The enzyme, which operates in the opposite direction to that shown, forms a mixture of GDP-α-D-rhamnose and its C-4 epimer, GDP-6-deoxy-α-D-talose. cf. EC 1.1.1.281, GDP-4-dehydro-6-deoxy-D-mannose reductase and EC 1.1.1.135, GDP-6-deoxy-D-talose 4-dehydrogenase.
References:
1.  Barber, G.A. The synthesis of guanosine 5′-diphosphate D-rhamnose by enzymes of a higher plant. Biochim. Biophys. Acta 165 (1968) 68–75. [PMID: 4386238]
2.  Winkler, N.W. and Markovitz, A. Guanosine diphosphate-4-keto-D-rhamnose reductase. A non-stereoselective enzyme. J. Biol. Chem. 246 (1971) 5868–5876. [PMID: 4398966]
[EC 1.1.1.187 created 1984]
 
 
EC 1.1.1.188     
Accepted name: prostaglandin-F synthase
Reaction: (5Z,13E)-(15S)-9α,11α,15-trihydroxyprosta-5,13-dienoate + NADP+ = (5Z,13E)-(15S)-9α,15-dihydroxy-11-oxoprosta-5,13-dienoate + NADPH + H+
Other name(s): prostaglandin-D2 11-reductase; reductase, 15-hydroxy-11-oxoprostaglandin; PGD2 11-ketoreductase; PGF synthetase; prostaglandin 11-ketoreductase; prostaglandin D2-ketoreductase; prostaglandin F synthase; prostaglandin F synthetase; synthetase, prostaglandin F; PGF synthetase; NADPH-dependent prostaglandin D2 11-keto reductase; prostaglandin 11-keto reductase
Systematic name: (5Z,13E)-(15S)-9α,11α,15-trihydroxyprosta-5,13-dienoate:NADP+ 11-oxidoreductase
Comments: Reduces prostaglandin D2 and prostaglandin H2 to prostaglandin F2; prostaglandin D2 is not an intermediate in the reduction of prostaglandin H2. Also catalyses the reduction of a number of carbonyl compounds, such as 9,10-phenanthroquinone and 4-nitroacetophenone.
References:
1.  Reingold, D.F., Kawasaki, A. and Needleman, P. A novel prostaglandin 11-keto reductase found in rabbit liver. Biochim. Biophys. Acta 659 (1981) 179–188. [PMID: 7248318]
2.  Watanabe, K., Shimizu, T. and Hayaishi, O. Enzymatic conversion of prostaglandin-D2 to prostaglandin-F in the rat lung. Biochem. Int. 2 (1981) 603–610.
3.  Watanabe, K., Yoshida, R., Shimizu, T. and Hayaishi, O. Enzymatic formation of prostaglandin F from prostaglandin H2 and D2. Purification and properties of prostaglandin F synthetase from bovine lung. J. Biol. Chem. 260 (1985) 7035–7041. [PMID: 3858278]
4.  Wong, P.Y.-K. Purification and partial characterization of prostaglandin D2 11-keto reductase in rabbit liver. Biochim. Biophys. Acta 659 (1981) 169–178. [PMID: 7248317]
5.  Wong, P.Y.-K. Purification of PGD2 11-ketoreductase from rabbit liver. Methods Enzymol. 86 (1982) 117–125. [PMID: 7132748]
[EC 1.1.1.188 created 1984, modified 1989, modified 1990]
 
 
EC 1.1.1.189     
Accepted name: prostaglandin-E2 9-reductase
Reaction: (5Z,13E)-(15S)-9α,11α,15-trihydroxyprosta-5,13-dienoate + NADP+ = (5Z,13E)-(15S)-11α,15-dihydroxy-9-oxoprosta-5,13-dienoate + NADPH + H+
Other name(s): PGE2-9-OR; reductase, 15-hydroxy-9-oxoprostaglandin; 9-keto-prostaglandin E2 reductase; 9-ketoprostaglandin reductase; PGE-9-ketoreductase; PGE2 9-oxoreductase; PGE2-9-ketoreductase; prostaglandin 9-ketoreductase; prostaglandin E 9-ketoreductase; prostaglandin E2-9-oxoreductase
Systematic name: (5Z,13E)-(15S)-9α,11α,15-trihydroxyprosta-5,13-dienoate:NADP+ 9-oxidoreductase
Comments: Reduces prostaglandin E2 to prostaglandin F2α. A number of other 9-oxo- and 15-oxo-prostaglandin derivatives can also be reduced to the corresponding hydroxy compounds. May be identical with EC 1.1.1.197 15-hydroxyprostaglandin dehydrogenase (NADP+).
References:
1.  Lee, S.-C. and Levine, L. Purification and regulatory properties of chicken heart prostaglandin E 9-ketoreductase. J. Biol. Chem. 250 (1975) 4549–4555. [PMID: 166995]
2.  Schlegel, W., Krüger, S. and Korte, K. Purification of prostaglandin E2 9-oxoreductase from human decidua vera. FEBS Lett. 171 (1984) 141–144. [PMID: 6586494]
3.  Tai, H.-H. and Yuan, B. Purification and assay of 9-hydroxyprostaglandin dehydrogenase from rat kidney. Methods Enzymol. 86 (1982) 113–117. [PMID: 7132747]
4.  Watkins, J.D. and Jarabak, J. The effect of NaCl intake on 9-ketoprostaglandin reductase activity in the rabbit kidney. Prostaglandins 30 (1985) 335–349. [PMID: 3901124]
[EC 1.1.1.189 created 1984, modified 1989]
 
 
EC 1.1.1.190     
Accepted name: indole-3-acetaldehyde reductase (NADH)
Reaction: (indol-3-yl)ethanol + NAD+ = (indol-3-yl)acetaldehyde + NADH + H+
Other name(s): indoleacetaldehyde reductase; indole-3-acetaldehyde reductase (NADH); indole-3-ethanol:NAD+ oxidoreductase
Systematic name: (indol-3-yl)ethanol:NAD+ oxidoreductase
References:
1.  Brown, H.M. and Purves, W.K. Isolation and characterization of indole-3-acetaldehyde reductases from Cucumis sativus. J. Biol. Chem. 251 (1976) 907–913. [PMID: 2607]
[EC 1.1.1.190 created 1984]
 
 
EC 1.1.1.191     
Accepted name: indole-3-acetaldehyde reductase (NADPH)
Reaction: (indol-3-yl)ethanol + NADP+ = (indol-3-yl)acetaldehyde + NADPH + H+
Other name(s): indoleacetaldehyde (reduced nicotinamide adenine dinucleotide phosphate) reductase; indole-3-acetaldehyde reductase (NADPH); indole-3-ethanol:NADP+ oxidoreductase
Systematic name: (indol-3-yl)ethanol:NADP+ oxidoreductase
References:
1.  Brown, H.M. and Purves, W.K. Isolation and characterization of indole-3-acetaldehyde reductases from Cucumis sativus. J. Biol. Chem. 251 (1976) 907–913. [PMID: 2607]
[EC 1.1.1.191 created 1984]
 
 
EC 1.1.1.192     
Accepted name: long-chain-alcohol dehydrogenase
Reaction: a long-chain alcohol + 2 NAD+ + H2O = a long-chain carboxylate + 2 NADH + 2 H+
Other name(s): long-chain alcohol dehydrogenase; fatty alcohol oxidoreductase
Systematic name: long-chain-alcohol:NAD+ oxidoreductase
Comments: Hexadecanol is a good substrate.
References:
1.  Lee, T.-C. Characterization of fatty alcohol:NAD+ oxidoreductase from rat liver. J. Biol. Chem. 254 (1979) 2892–2896. [PMID: 34610]
[EC 1.1.1.192 created 1984]
 
 
EC 1.1.1.193     
Accepted name: 5-amino-6-(5-phosphoribosylamino)uracil reductase
Reaction: 5-amino-6-(5-phospho-D-ribitylamino)uracil + NADP+ = 5-amino-6-(5-phospho-D-ribosylamino)uracil + NADPH + H+
Other name(s): aminodioxyphosphoribosylaminopyrimidine reductase
Systematic name: 5-amino-6-(5-phospho-D-ribitylamino)uracil:NADP+ 1′-oxidoreductase
References:
1.  Burrows, R.B. and Brown, G.M. Presence of Escherichia coli of a deaminase and a reductase involved in biosynthesis of riboflavin. J. Bacteriol. 136 (1978) 657–667. [PMID: 30756]
[EC 1.1.1.193 created 1984, modified 2011]
 
 
EC 1.1.1.194     
Accepted name: coniferyl-alcohol dehydrogenase
Reaction: coniferyl alcohol + NADP+ = coniferyl aldehyde + NADPH + H+
Other name(s): CAD (ambiguous)
Systematic name: coniferyl-alcohol:NADP+ oxidoreductase
Comments: Specific for coniferyl alcohol; does not act on cinnamyl alcohol, 4-coumaryl alcohol or sinapyl alcohol.
References:
1.  Mansell, R.L., Babbel, G.R. and Zenk, M.H. Multiple forms and specificity of coniferyl alcohol dehydrogenase from cambial regions of higher plants. Phytochemistry 15 (1976) 1849–1853.
2.  Wyrambik, D. and Grisebach, H. Purification and properties of isoenzymes of cinnamyl-alcohol dehydrogenase from soybean-cell-suspension cultures. Eur. J. Biochem. 59 (1975) 9–15. [PMID: 1250]
[EC 1.1.1.194 created 1984]
 
 
EC 1.1.1.195     
Accepted name: cinnamyl-alcohol dehydrogenase
Reaction: cinnamyl alcohol + NADP+ = cinnamaldehyde + NADPH + H+
Other name(s): cinnamyl alcohol dehydrogenase; CAD (ambiguous)
Systematic name: cinnamyl-alcohol:NADP+ oxidoreductase
Comments: Acts on coniferyl alcohol, sinapyl alcohol, 4-coumaryl alcohol and cinnamyl alcohol (cf. EC 1.1.1.194 coniferyl-alcohol dehydrogenase).
References:
1.  Sarni, F., Grand, C. and Baudet, A.M. Purification and properties of cinnamoyl-CoA reductase and cinnamyl alcohol dehydrogenase from poplar stems (Populus X euramericana). Eur. J. Biochem. 139 (1984) 259–265. [PMID: 6365550]
2.  Wyrambik, D. and Grisebach, H. Purification and properties of isoenzymes of cinnamyl-alcohol dehydrogenase from soybean-cell-suspension cultures. Eur. J. Biochem. 59 (1975) 9–15. [PMID: 1250]
3.  Wyrambik, D. and Grisebach, H. Enzymic synthesis of lignin precursors. Further studies on cinnamyl-alcohol dehydrogenase from soybean-cell-suspension cultures. Eur. J. Biochem. 97 (1979) 503–509. [PMID: 572771]
[EC 1.1.1.195 created 1984]
 
 
EC 1.1.1.196     
Accepted name: 15-hydroxyprostaglandin-D dehydrogenase (NADP+)
Reaction: (5Z,13E)-(15S)-9α,15-dihydroxy-11-oxoprosta-5,13-dienoate + NADP+ = (5Z,13E)-9α-hydroxy-11,15-dioxoprosta-5,13-dienoate + NADPH + H+
Other name(s): prostaglandin-D 15-dehydrogenase (NADP); dehydrogenase, prostaglandin D2; NADP-PGD2 dehydrogenase; dehydrogenase, 15-hydroxyprostaglandin (nicotinamide adenine dinucleotide phosphate); 15-hydroxy PGD2 dehydrogenase; 15-hydroxyprostaglandin dehydrogenase (NADP); NADP-dependent 15-hydroxyprostaglandin dehydrogenase; prostaglandin D2 dehydrogenase; NADP-linked 15-hydroxyprostaglandin dehydrogenase; NADP-specific 15-hydroxyprostaglandin dehydrogenase; NADP-linked prostaglandin D2 dehydrogenase; 15-hydroxyprostaglandin-D dehydrogenase (NADP)
Systematic name: (5Z,13E)-(15S)-9α,15-dihydroxy-11-oxoprosta-5,13-dienoate:NADP+ 15-oxidoreductase
Comments: Specific for prostaglandins D [cf. EC 1.1.1.141 15-hydroxyprostaglandin dehydrogenase (NAD+) and EC 1.1.1.197 15-hydroxyprostaglandin dehydrogenase (NADP+)].
References:
1.  Watanabe, K., Shimizu, T., Iguchi, S., Wakatsuka, H., Hayashi, M. and Hayaishi, O. An NADP-linked prostaglandin D dehydrogenase in swine brain. J. Biol. Chem. 255 (1980) 1779–1882. [PMID: 7354056]
[EC 1.1.1.196 created 1984, modified 1990]
 
 
EC 1.1.1.197     
Accepted name: 15-hydroxyprostaglandin dehydrogenase (NADP+)
Reaction: (13E)-(15S)-11α,15-dihydroxy-9-oxoprost-13-enoate + NADP+ = (13E)-11α-hydroxy-9,15-dioxoprost-13-enoate + NADPH + H+
Other name(s): NADP-dependent 15-hydroxyprostaglandin dehydrogenase; NADP-linked 15-hydroxyprostaglandin dehydrogenase; NADP-specific 15-hydroxyprostaglandin dehydrogenase; type II 15-hydroxyprostaglandin dehydrogenase; 15-hydroxyprostaglandin dehydrogenase (NADP)
Systematic name: (13E)-(15S)-11α,15-dihydroxy-9-oxoprost-13-enoate:NADP+ 15-oxidoreductase
Comments: Acts on prostaglandins E2, F and B1, but not on prostaglandin D2 [cf. EC 1.1.1.141 15-hydroxyprostaglandin dehydrogenase (NAD+) and EC 1.1.1.196 15-hydroxyprostaglandin-D dehydrogenase (NADP+)]. May be identical with EC 1.1.1.189 prostaglandin-E2 9-reductase.
References:
1.  Lee, S.-C. and Levine, L. Prostaglandin metabolism. II. Identification of two 15-hydroxyprostaglandin dehydrogenase types. J. Biol. Chem. 250 (1975) 548–552. [PMID: 234431]
2.  Lee, S.-C., Pong, S.-S., Katzen, D., Wu, K.-Y. and Levine, L. Distribution of prostaglandin E 9-ketoreductase and types I and II 15-hydroxyprostaglandin dehydrogenase in swine kidney medulla and cortex. Biochemistry 14 (1975) 142–145. [PMID: 803247]
[EC 1.1.1.197 created 1984]
 
 
EC 1.1.1.198     
Accepted name: (+)-borneol dehydrogenase
Reaction: (+)-borneol + NAD+ = (+)-camphor + NADH + H+
Other name(s): bicyclic monoterpenol dehydrogenase
Systematic name: (+)-borneol:NAD+ oxidoreductase
Comments: NADP+ can also act, but more slowly.
References:
1.  Croteau, R., Hooper, C.L. and Felton, M. Biosynthesis of monoterpenes. Partial purification and characterization of a bicyclic monoterpenol dehydrogenase from sage (Salvia officinalis). Arch. Biochem. Biophys. 188 (1978) 182–193. [PMID: 677891]
2.  Dehal, S.S. and Croteau, R. Metabolism of monoterpenes: specificity of the dehydrogenases responsible for the biosynthesis of camphor, 3-thujone, and 3-isothujone. Arch. Biochem. Biophys. 258 (1987) 287–291. [PMID: 3310901]
[EC 1.1.1.198 created 1984, modified 1990 (EC 1.1.1.182 created 1983, part incorporated 1990)]
 
 
EC 1.1.1.199     
Accepted name: (S)-usnate reductase
Reaction: (6R)-2-acetyl-6-(3-acetyl-2,4,6-trihydroxy-5-methylphenyl)-3-hydroxy-6-methyl-2,4-cyclohexadien-1-one + NAD+ = (S)-usnate + NADH + H+
Glossary: reduced (S)-usnate = reduced (-)-usnate = (6R)-2-acetyl-6-(3-acetyl-2,4,6-trihydroxy-5-methylphenyl)-3-hydroxy-6-methyl-2,4-cyclohexadien-1-one
Other name(s): L-usnic acid dehydrogenase
Systematic name: reduced-(S)-usnate:NAD+ oxidoreductase (ether-bond-forming)
References:
1.  Estevéz, M.P., Legaz, E., Olmeda, L., Pérez, F.J. and Vincente, C. Purification and properties of a new enzyme from Evernia prunastri, which reduces L-usnic acid. Z. Naturforsch. C: Biosci. 36 (1981) 35–39.
[EC 1.1.1.199 created 1984]
 
 
EC 1.1.1.200     
Accepted name: aldose-6-phosphate reductase (NADPH)
Reaction: D-sorbitol 6-phosphate + NADP+ = D-glucose 6-phosphate + NADPH + H+
Other name(s): aldose 6-phosphate reductase; NADP-dependent aldose 6-phosphate reductase; A6PR; aldose-6-P reductase; aldose-6-phosphate reductase; alditol 6-phosphate:NADP 1-oxidoreductase; aldose-6-phosphate reductase (NADPH2)
Systematic name: D-aldose-6-phosphate:NADP+ 1-oxidoreductase
Comments: In the reverse reaction, acts also on D-galactose 6-phosphate and, more slowly, on D-mannose 6-phosphate and 2-deoxy-D-glucose 6-phosphate.
References:
1.  Negm, F.B. and Loescher, W.H. Characterization and partial-purification of aldose-6-phosphate reductase (alditol-6-phosphate-NADP 1-oxidoreductase) from apple leaves. Plant Physiol. 67 (1981) 139–142. [PMID: 16661614]
[EC 1.1.1.200 created 1984]
 
 
EC 1.1.1.201     
Accepted name: 7β-hydroxysteroid dehydrogenase (NADP+)
Reaction: a 7β-hydroxysteroid + NADP+ = a 7-oxosteroid + NADPH + H+
Other name(s): NADP-dependent 7β-hydroxysteroid dehydrogenase; 7β-hydroxysteroid dehydrogenase (NADP)
Systematic name: 7β-hydroxysteroid:NADP+ 7-oxidoreductase
Comments: Catalyses the oxidation of the 7β-hydroxy group of bile acids such as ursodeoxycholate.
References:
1.  Hirano, S. and Masuda, N. Characterization of NADP-dependent 7β-hydroxysteroid dehydrogenases from Peptostreptococcus productus and Eubacterium aerofaciens. Appl. Environ. Microbiol. 43 (1982) 1057–1063. [PMID: 6954878]
2.  Macdonald, I.A. and Roach, P.D. Bile induction of 7α- and 7β-hydroxysteroid dehydrogenases in Clostridium absonum. Biochim. Biophys. Acta 665 (1981) 262–269. [PMID: 6945134]
3.  Macdonald, I.A., Rochon, Y.P., Hutchison, D.M. and Holdeman, L.V. Formation of ursodeoxycholic acid from chenodeoxycholic acid by a 7β-hydroxysteroid dehydrogenase-elaborating Eubacterium aerofaciens strain cocultured with 7α-hydroxysteroid dehydrogenase-elaborating organisms. Appl. Environ. Microbiol. 44 (1982) 1187–1195. [PMID: 6758698]
[EC 1.1.1.201 created 1984]
 
 
EC 1.1.1.202     
Accepted name: 1,3-propanediol dehydrogenase
Reaction: propane-1,3-diol + NAD+ = 3-hydroxypropanal + NADH + H+
Other name(s): 3-hydroxypropionaldehyde reductase; 1,3-PD:NAD+ oxidoreductase; 1,3-propanediol:NAD+ oxidoreductase; 1,3-propanediol dehydrogenase
Systematic name: propane-1,3-diol:NAD+ 1-oxidoreductase
References:
1.  Abeles, R.H., Brownstein, A.M. and Randles, C.H. α-Hydroxypropionaldehyde, an intermediate in the formation of 1,3-propanediol by Aerobacter melanogaster. Biochim. Biophys. Acta 41 (1960) 530. [PMID: 13791444]
2.  Forage, R.G. and Foster, M.A. Glycerol fermentation in Klebsiella pneumoniae: functions of the coenzyme B12-dependent glycerol and diol dehydratases. J. Bacteriol. 149 (1982) 413–419. [PMID: 7035429]
[EC 1.1.1.202 created 1984]
 
 
EC 1.1.1.203     
Accepted name: uronate dehydrogenase
Reaction: (1) β-D-galacturonate + NAD+ = D-galactaro-1,5-lactone + NADH + H+
(2) β-D-glucuronate + NAD+ = D-glucaro-1,5-lactone + NADH + H+
Other name(s): uronate:NAD-oxidoreductase; uronic acid dehydrogenase
Systematic name: uronate:NAD+ 1-oxidoreductase
Comments: Requires Mg2+. The enzyme, characterized from the bacterium Agrobacterium fabrum, participates in oxidative degradation pathways for galacturonate and glucuronate. The enzyme can only accept the β anomeric form of the substrate [4]. The 1,5-lactone product is rather stable at cytosolic pH and does not hydrolyse spontaneously at a substantial rate.
References:
1.  Kilgore, W.W. and Starr, M.P. Uronate oxidation by phytopathogenic pseudomonads. Nature (Lond.) 183 (1959) 1412–1413. [PMID: 13657147]
2.  Boer, H., Maaheimo, H., Koivula, A., Penttila, M. and Richard, P. Identification in Agrobacterium tumefaciens of the D-galacturonic acid dehydrogenase gene. Appl. Microbiol. Biotechnol. 86 (2010) 901–909. [PMID: 19921179]
3.  Andberg, M., Maaheimo, H., Boer, H., Penttila, M., Koivula, A. and Richard, P. Characterization of a novel Agrobacterium tumefaciens galactarolactone cycloisomerase enzyme for direct conversion of D-galactarolactone to 3-deoxy-2-keto-L-threo-hexarate. J. Biol. Chem. 287 (2012) 17662–17671. [PMID: 22493433]
4.  Parkkinen, T., Boer, H., Janis, J., Andberg, M., Penttila, M., Koivula, A. and Rouvinen, J. Crystal structure of uronate dehydrogenase from Agrobacterium tumefaciens. J. Biol. Chem. 286 (2011) 27294–27300. [PMID: 21676870]
[EC 1.1.1.203 created 1972 as EC 1.2.1.35, transferred 1984 to EC 1.1.1.203, modified 2014]
 
 
EC 1.1.1.204      
Transferred entry: xanthine dehydrogenase. Now EC 1.17.1.4, xanthine dehydrogenase. The enzyme was incorrectly classified as acting on a CH-OH group
[EC 1.1.1.204 created 1972 as EC 1.2.1.37, transferred 1984 to EC 1.1.1.204, modified 1989, deleted 2004]
 
 
EC 1.1.1.205     
Accepted name: IMP dehydrogenase
Reaction: IMP + NAD+ + H2O = XMP + NADH + H+
Glossary: IMP = inosine 5′-phosphate
XMP = xanthosine 5′-phosphate
Other name(s): inosine-5′-phosphate dehydrogenase; inosinic acid dehydrogenase; inosinate dehydrogenase; inosine 5′-monophosphate dehydrogenase; inosine monophosphate dehydrogenase; IMP oxidoreductase; inosine monophosphate oxidoreductase
Systematic name: IMP:NAD+ oxidoreductase
Comments: The enzyme acts on the hydroxy group of the hydrated derivative of the substrate.
References:
1.  Magasanik, B., Moyed, H.S. and Gehring, L.B. Enzymes essential for the biosynthesis of nucleic acid guanine; inosine 5′-phosphate dehydrogenase of Aerobacter aerogenes. J. Biol. Chem. 226 (1957) 339–350. [PMID: 13428767]
2.  Turner, J.F. and King, J.E. Inosine 5-phosphate dehydrogenase of pea seeds. Biochem. J. 79 (1961) 147. [PMID: 13778733]
[EC 1.1.1.205 created 1961 as EC 1.2.1.14, transferred 1984 to EC 1.1.1.205]
 
 
EC 1.1.1.206     
Accepted name: tropinone reductase I
Reaction: tropine + NADP+ = tropinone + NADPH + H+
Glossary: tropine = 3α-hydroxytropane = tropan-3-endo-ol
Other name(s): tropine dehydrogenase; tropinone reductase (ambiguous); TR-I
Systematic name: tropine:NADP+ 3α-oxidoreductase
Comments: Also oxidizes other tropan-3α-ols, but not the corresponding β-derivatives [1]. This enzyme along with EC 1.1.1.236, tropinone reductase II, represents a branch point in tropane alkaloid metabolism [4]. Tropine (the product of EC 1.1.1.206) is incorporated into hyoscyamine and scopolamine whereas pseudotropine (the product of EC 1.1.1.236) is the first specific metabolite on the pathway to the calystegines [4]. Both enzymes are always found together in any given tropane-alkaloid-producing species, have a common substrate, tropinone, and are strictly stereospecific [3].
References:
1.  Koelen, K.J. and Gross, G.G. Partial purification and properties of tropine dehydrogenase from root cultures of Datura stramonium. Planta Med. 44 (1982) 227–230. [PMID: 17402126]
2.  Couladis, M.M, Friesen, J.B., Landgrebe, M.E. and Leete, E. Enzymes catalysing the reduction of tropinone to tropine and ψ-tropine isolated from the roots of Datura innoxia. Pytochemistry 30 (1991) 801–805.
3.  Nakajima, K., Hashimoto, T. and Yamada, Y. Two tropinone reductases with different stereospecificities are short-chain dehydrogenases evolved from a common ancestor. Proc. Natl. Acad. Sci. USA 90 (1993) 9591–9595. [PMID: 8415746]
4.  Dräger, B. Tropinone reductases, enzymes at the branch point of tropane alkaloid metabolism. Phytochemistry 67 (2006) 327–337. [PMID: 16426652]
[EC 1.1.1.206 created 1984, modified 2007]
 
 
EC 1.1.1.207     
Accepted name: (-)-menthol dehydrogenase
Reaction: (-)-menthol + NADP+ = (-)-menthone + NADPH + H+
Other name(s): monoterpenoid dehydrogenase
Systematic name: (-)-menthol:NADP+ oxidoreductase
Comments: Not identical with EC 1.1.1.208 (+)-neomenthol dehydrogenase. Acts also on a number of other cyclohexanols and cyclohexenols.
References:
1.  Kjonaas, R., Martinkus-Taylor, C. and Croteau, R. Metabolism of monoterpenes: conversion of l-menthone to l-menthol and d-neomenthol by stereospecific dehydrogenases from peppermint (Mentha piperita) leaves. Plant Physiol. 69 (1982) 1013–1017. [PMID: 16662335]
[EC 1.1.1.207 created 1984]
 
 
EC 1.1.1.208     
Accepted name: (+)-neomenthol dehydrogenase
Reaction: (+)-neomenthol + NADP+ = (-)-menthone + NADPH + H+
Other name(s): monoterpenoid dehydrogenase
Systematic name: (+)-neomenthol:NADP+ oxidoreductase
Comments: Not identical with EC 1.1.1.207 (-)-menthol dehydrogenase. Acts also on a number of other cyclohexanols and cyclohexenols.
References:
1.  Kjonaas, R., Martinkus-Taylor, C. and Croteau, R. Metabolism of monoterpenes: conversion of l-menthone to l-menthol and d-neomenthol by stereospecific dehydrogenases from peppermint (Mentha piperita) leaves. Plant Physiol. 69 (1982) 1013–1017. [PMID: 16662335]
[EC 1.1.1.208 created 1984]
 
 
EC 1.1.1.209     
Accepted name: 3(or 17)α-hydroxysteroid dehydrogenase
Reaction: androsterone + NAD(P)+ = 5α-androstane-3,17-dione + NAD(P)H + H+
Other name(s): 3(17)α-hydroxysteroid dehydrogenase
Systematic name: 3(or 17)α-hydroxysteroid:NAD(P)+ oxidoreductase
Comments: Acts on the 3α-hydroxy group of androgens of the 5α-androstane series; and also, more slowly, on the 17α-hydroxy group of both androgenic and estrogenic substrates (cf. EC 1.1.1.51 3(or 17)β-hydroxysteroid dehydrogenase).
References:
1.  Lau, P.C.K., Layne, D.S. and Williamson, D.G. A 3(17)α-hydroxysteroid dehydrogenase of female rabbit kidney cytosol. Purification and characterization of multiple forms of the enzyme. J. Biol. Chem. 257 (1982) 9444–9449. [PMID: 6955302]
2.  Lau, P.C.K., Layne, D.S. and Williamson, D.G. Comparison of the multiple forms of the soluble 3(17)α-hydroxysteroid dehydrogenases of female rabbit kidney and liver. J. Biol. Chem. 257 (1982) 9450–9456. [PMID: 6955303]
[EC 1.1.1.209 created 1986]
 
 
EC 1.1.1.210     
Accepted name: 3β(or 20α)-hydroxysteroid dehydrogenase
Reaction: 5α-androstan-3β,17β-diol + NADP+ = 17β-hydroxy-5α-androstan-3-one + NADPH + H+
Other name(s): progesterone reductase; dehydrogenase, 3β,20α-hydroxy steroid; 3β,20α-hydroxysteroid oxidoreductase
Systematic name: 3β(or 20α)-hydroxysteroid:NADP+ oxidoreductase
Comments: Also acts on 20α-hydroxysteroids.
References:
1.  Sharaf, M.A. and Sweet, F. Dual activity at an enzyme active site: 3β,20α-hydroxysteroid oxidoreductase from fetal blood. Biochemistry 21 (1982) 4615–4620. [PMID: 6958329]
[EC 1.1.1.210 created 1986]
 
 
EC 1.1.1.211     
Accepted name: long-chain-3-hydroxyacyl-CoA dehydrogenase
Reaction: a long-chain (S)-3-hydroxyacyl-CoA + NAD+ = a long-chain 3-oxoacyl-CoA + NADH + H+
Glossary: a long-chain acyl-CoA = an acyl-CoA thioester where the acyl chain contains 13 to 22 carbon atoms.
Other name(s): β-hydroxyacyl-CoA dehydrogenase; long-chain 3-hydroxyacyl coenzyme A dehydrogenase; 3-hydroxyacyl-CoA dehydrogenase; LCHAD
Systematic name: long-chain-(S)-3-hydroxyacyl-CoA:NAD+ oxidoreductase
Comments: This enzyme was purified from the mitochondrial inner membrane. The enzyme has a preference for long-chain substrates, and activity with a C16 substrate was 6- to 15-fold higher than with a C4 substrate (cf. EC 1.1.1.35 3-hydroxyacyl-CoA dehydrogenase).
References:
1.  El-Fakhri, M. and Middleton, B. The existence of an inner-membrane-bound, long acyl-chain-specific 3-hydroxyacyl-CoA dehydrogenase in mammalian mitochondria. Biochim. Biophys. Acta 713 (1982) 270–279. [PMID: 7150615]
[EC 1.1.1.211 created 1986]
 
 
EC 1.1.1.212     
Accepted name: 3-oxoacyl-[acyl-carrier-protein] reductase (NADH)
Reaction: a (3R)-3-hydroxyacyl-[acyl-carrier protein] + NAD+ = a 3-oxoacyl-[acyl-carrier protein] + NADH + H+
Other name(s): 3-oxoacyl-[acyl carrier protein] (reduced nicotinamide adenine dinucleotide) reductase; 3-oxoacyl-[acyl-carrier-protein] reductase (NADH); (3R)-3-hydroxyacyl-[acyl-carrier-protein]:NAD+ oxidoreductase
Systematic name: (3R)-3-hydroxyacyl-[acyl-carrier protein]:NAD+ oxidoreductase
Comments: Forms part of the fatty acid synthase system in plants. Can be separated from EC 1.1.1.100, 3-oxoacyl-[acyl-carrier-protein] reductase.
References:
1.  Caughey, I. and Kekwick, R.G.O. The characteristics of some components of the fatty acid synthetase system in the plastids from the mesocarp of avocado (Persea americana) fruit. Eur. J. Biochem. 123 (1982) 553–561. [PMID: 7075600]
[EC 1.1.1.212 created 1986]
 
 
EC 1.1.1.213     
Accepted name: 3α-hydroxysteroid 3-dehydrogenase (Re-specific)
Reaction: a 3α-hydroxysteroid + NAD(P)+ = a 3-oxosteroid + NAD(P)H + H+
Other name(s): 3α-hydroxysteroid dehydrogenase; 3α-hydroxysteroid:NAD(P)+ 3-oxidoreductase (A-specific); 3α-hydroxysteroid 3-dehydrogenase (A-specific)
Systematic name: 3α-hydroxysteroid:NAD(P)+ 3-oxidoreductase (Re-specific)
Comments: The enzyme acts on multiple 3α-hydroxysteroids. Re-specific with respect to NAD+ or NADP+ [cf. EC 1.1.1.50, 3α-hydroxysteroid 3-dehydrogenase (Si-specific)]. Enzymes whose stereo-specificity with respect to NAD+ or NADP+ is not known are described by EC 1.1.1.357, 3α-hydroxysteroid 3-dehydrogenase.
References:
1.  Björkhem, I. and Danielsson, H. Stereochemistry of hydrogen transfer from pyridine nucleotides catalyzed by Δ4-3-oxosteroid 5-β-reductase and 3-α-hydroxysteroid dehydrogenase from rat liver. Eur. J. Biochem. 12 (1970) 80–84. [PMID: 4392180]
2.  Tomkins, G.M. A mammalian 3α-hydroxysteroid dehydrogenase. J. Biol. Chem. 218 (1956) 437–447. [PMID: 13278351]
[EC 1.1.1.213 created 1986, modified 2012]
 
 
EC 1.1.1.214     
Accepted name: 2-dehydropantolactone reductase (Si-specific)
Reaction: (R)-pantolactone + NADP+ = 2-dehydropantolactone + NADPH + H+
Other name(s): 2-oxopantoyl lactone reductase; 2-ketopantoyl lactone reductase; ketopantoyl lactone reductase; 2-dehydropantoyl-lactone reductase (B-specific); (R)-pantolactone:NADP+ oxidoreductase (B-specific); 2-dehydropantolactone reductase (B-specific)
Systematic name: (R)-pantolactone:NADP+ oxidoreductase (Si-specific)
Comments: The Escherichia coli enzyme differs from that from yeast [EC 1.1.1.168 2-dehydropantolactone reductase (Re-specific)], which is specific for the Re-face of NADP+, and in receptor requirements from EC 1.1.99.26 3-hydroxycyclohexanone dehydrogenase.
References:
1.  Wilken, D.R., King, H.L., Jr. and Dyar, R.E. Ketopantoic acid and ketopantoyl lactone reductases. Stereospecificity of transfer of hydrogen from reduced nicotinamide adenine dinucleotide phosphate. J. Biol. Chem. 250 (1975) 2311–2314. [PMID: 234966]
[EC 1.1.1.214 created 1986, modified 1999, modified 2013]
 
 
EC 1.1.1.215     
Accepted name: gluconate 2-dehydrogenase
Reaction: D-gluconate + NADP+ = 2-dehydro-D-gluconate + NADPH + H+
Other name(s): 2-keto-D-gluconate reductase; 2-ketogluconate reductase
Systematic name: D-gluconate:NADP+ oxidoreductase
Comments: Also acts on L-idonate, D-galactonate and D-xylonate.
References:
1.  Adachi, O., Chiyonobu, T., Shinagawa, E., Matsushita, K. and Ameyama, M. Crystalline 2-ketogluconate reductase from Acetobacter ascendens, the second instance of crystalline enzyme in genus Acetobacter. Agric. Biol. Chem. 42 (1978) 2057.
2.  Chiyonobu, T., Shinagawa, E., Adachi, O. and Ameyama, M. Purification, crystallization and properties of 2-ketogluconate reductase from Acetobacter rancens. Agric. Biol. Chem. 40 (1976) 175–184.
[EC 1.1.1.215 created 1989]
 
 
EC 1.1.1.216     
Accepted name: farnesol dehydrogenase (NADP+)
Reaction: (2E,6E)-farnesol + NADP+ = (2E,6E)-farnesal + NADPH + H+
Other name(s): NADP+-farnesol dehydrogenase; farnesol (nicotinamide adenine dinucleotide phosphate) dehydrogenase
Systematic name: (2E,6E)-farnesol:NADP+ 1-oxidoreductase
Comments: Also acts, more slowly, on (2Z,6E)-farnesol, geraniol, citronerol and nerol.
References:
1.  Inoue, H., Tsuji, H. and Uritani, I. Characterization and activity change of farnesol dehydrogenase in black rot fungus-infected sweet-potato. Agric. Biol. Chem. 48 (1984) 733–738.
[EC 1.1.1.216 created 1989]
 
 
EC 1.1.1.217     
Accepted name: benzyl-2-methyl-hydroxybutyrate dehydrogenase
Reaction: benzyl (2R,3S)-2-methyl-3-hydroxybutanoate + NADP+ = benzyl 2-methyl-3-oxobutanoate + NADPH + H+
Other name(s): benzyl 2-methyl-3-hydroxybutyrate dehydrogenase
Systematic name: benzyl-(2R,3S)-2-methyl-3-hydroxybutanoate:NADP+ 3-oxidoreductase
Comments: Also acts on benzyl (2S,3S)-2-methyl-3-hydroxybutanoate; otherwise highly specific.
References:
1.  Furuichi, A., Akita, H., Matsukura, H., Oishi, T. and Horikoshi, K. Purification and properties of an asymmetric reduction enzyme of 2-methyl-3-oxobutyrate in baker's yeast. Agric. Biol. Chem. 49 (1985) 2563–2570.
[EC 1.1.1.217 created 1989]
 
 
EC 1.1.1.218     
Accepted name: morphine 6-dehydrogenase
Reaction: morphine + NAD(P)+ = morphinone + NAD(P)H + H+
Other name(s): naloxone reductase
Systematic name: morphine:NAD(P)+ 6-oxidoreductase
Comments: Also acts on some other alkaloids, including codeine, normorphine and ethylmorphine, but only very slowly on 7,8-saturated derivatives such as dihydromorphine and dihydrocodeine. In the reverse direction, also reduces naloxone to the 6α-hydroxy analogue. Activated by 2-sulfanylethan-1-ol (2-mercaptoethanol).
References:
1.  Yamano, S., Kaguera, E., Ishida, T. and Toki, S. Purification and characterization of guinea pig liver morphine 6-dehydrogenase. J. Biol. Chem. 260 (1985) 5259–5264. [PMID: 2580834]
2.  Yamano, S., Nishida, F. and Toki, S. Guinea-pig liver morphine 6-dehydrogenase as a naloxone reductase. Biochem. Pharmacol. 35 (1986) 4321–4326. [PMID: 3539118]
[EC 1.1.1.218 created 1989, modified 1990]
 
 
EC 1.1.1.219     
Accepted name: dihydroflavonol 4-reductase
Reaction: a (2R,3S,4S)-leucoanthocyanidin + NADP+ = a (2R,3R)-dihydroflavonol + NADPH + H+
Other name(s): dihydrokaempferol 4-reductase; dihydromyricetin reductase; NADPH-dihydromyricetin reductase; dihydroquercetin reductase; DFR (gene name); cis-3,4-leucopelargonidin:NADP+ 4-oxidoreductase; dihydroflavanol 4-reductase (incorrect)
Systematic name: (2R,3S,4S)-leucoanthocyanidin:NADP+ 4-oxidoreductase
Comments: This plant enzyme, involved in the biosynthesis of anthocyanidins, is known to act on (+)-dihydrokaempferol, (+)-taxifolin, and (+)-dihydromyricetin, although some enzymes may act only on a subset of these compounds. Each dihydroflavonol is reduced to the corresponding cis-flavan-3,4-diol. NAD+ can act instead of NADP+, but more slowly.
References:
1.  Heller, W., Forkmann, G., Britsch, L. and Grisebach, H. Enzymatic reduction of (+)-dihydroflavonols to flavan-3,4-cis- diols with flower extracts from Matthiola incana and its role in anthocyanin biosynthesis. Planta 165 (1985) 284–287. [PMID: 24241054]
2.  Stafford, H.A. and Lester, H.H. Flavan-3-ol biosynthesis the conversion of (+)-dihydromyricetin to its flavan-3,4-diol (leucodelphinidin) and to (+)-gallocatechin by reductases extracted from tissue-cultures of Ginkgo biloba and Pseudotsuga-menziesii. Plant Physiol. 78 (1985) 791–794. [PMID: 16664326]
3.  Fischer, D., Stich, K., Britsch, L. and Grisebach, H. Purification and characterization of (+)dihydroflavonol (3-hydroxyflavanone) 4-reductase from flowers of Dahlia variabilis. Arch. Biochem. Biophys. 264 (1988) 40–47. [PMID: 3293532]
4.  Li, H., Qiu, J., Chen, F., Lv, X., Fu, C., Zhao, D., Hua, X. and Zhao, Q. Molecular characterization and expression analysis of dihydroflavonol 4-reductase (DFR) gene in Saussurea medusa. Mol. Biol. Rep. 39 (2012) 2991–2999. [PMID: 21701830]
[EC 1.1.1.219 created 1989, modified 2016]
 
 
EC 1.1.1.220     
Accepted name: 6-pyruvoyltetrahydropterin 2′-reductase
Reaction: 6-lactoyl-5,6,7,8-tetrahydropterin + NADP+ = 6-pyruvoyltetrahydropterin + NADPH + H+
Other name(s): 6-pyruvoyltetrahydropterin reductase; 6PPH4(2′-oxo) reductase; 6-pyruvoyl tetrahydropterin (2′-oxo)reductase; 6-pyruvoyl-tetrahydropterin 2′-reductase; pyruvoyl-tetrahydropterin reductase
Systematic name: 6-lactoyl-5,6,7,8-tetrahydropterin:NADP+ 2′-oxidoreductase
Comments: Not identical with EC 1.1.1.153 sepiapterin reductase.
References:
1.  Milstien, S. and Kaufman, S. Biosynthesis of tetrahydrobiopterin: conversion of dihydroneopterin triphosphate to tetrahydropterin intermediates. Biochem. Biophys. Res. Commun. 128 (1985) 1099–1107. [PMID: 4004850]
[EC 1.1.1.220 created 1989]
 
 
EC 1.1.1.221     
Accepted name: vomifoliol dehydrogenase
Reaction: (6S,9R)-6-hydroxy-3-oxo-α-ionol + NAD+ = (6S)-6-hydroxy-3-oxo-α-ionone + NADH + H+
Glossary: (6S,9R)-6-hydroxy-3-oxo-α-ionol = vomifoliol = (4S)-4-hydroxy-4-[(1E,3R)-3-hydroxybut-1-en-1-yl]-3,5,5-trimethylcyclohex-2-en-1-one
(6S)-6-hydroxy-3-oxo-α-ionone = dehydrovomifoliol = (4S)-4-hydroxy-3,5,5-trimethyl-4-[(1E)-3-oxobut-1-en-1-yl]cyclohex-2-en-1-one
Other name(s): vomifoliol 4′-dehydrogenase; vomifoliol:NAD+ 4′-oxidoreductase
Systematic name: (6S,9R)-6-hydroxy-3-oxo-α-ionol:NAD+ oxidoreductase
Comments: Oxidizes vomifoliol to dehydrovomifoliol; involved in the metabolism of abscisic acid in Corynebacterium sp.
References:
1.  Hasegawa, S., Poling, S.M., Maier, V.P. and Bennett, R.D. Metabolism of abscisic-acid bacterial conversion to dehydrovomifoliol and vomifoliol dehydrogenase-activity. Phytochemistry 23 (1984) 2769–2771.
[EC 1.1.1.221 created 1989]
 
 
EC 1.1.1.222      
Transferred entry: (R)-4-hydroxyphenyllactate dehydrogenase. Now included with EC 1.1.1.110, aromatic 2-oxoacid reductase
[EC 1.1.1.222 created 1989, deleted 2018]
 
 
EC 1.1.1.223     
Accepted name: isopiperitenol dehydrogenase
Reaction: (-)-trans-isopiperitenol + NAD+ = (-)-isopiperitenone + NADH + H+
Systematic name: (-)-trans-isopiperitenol:NAD+ oxidoreductase
Comments: Acts on (-)-trans-isopiperitenol, (+)-trans-piperitenol and (+)-trans-pulegol. Involved in the biosynthesis of menthol and related monoterpenes in peppermint (Mentha piperita) leaves.
References:
1.  Kjonaas, R.B., Venkatachalam, K.V. and Croteau, R. Metabolism of monoterpenes: oxidation of isopiperitenol to isopiperitenone, and subsequent isomerization to piperitenone by soluble enzyme preparations from peppermint (Mentha piperita) leaves. Arch. Biochem. Biophys. 238 (1985) 49–60. [PMID: 3885858]
[EC 1.1.1.223 created 1989]
 
 
EC 1.1.1.224     
Accepted name: mannose-6-phosphate 6-reductase
Reaction: D-mannitol 1-phosphate + NADP+ = D-mannose 6-phosphate + NADPH + H+
Other name(s): NADPH-dependent mannose 6-phosphate reductase; mannose-6-phosphate reductase; 6-phosphomannose reductase; NADP-dependent mannose-6-P:mannitol-1-P oxidoreductase; NADPH-dependent M6P reductase; NADPH-mannose-6-P reductase
Systematic name: D-mannitol-1-phosphate:NADP+ 6-oxidoreductase
Comments: Involved in the biosynthesis of mannitol in celery (Apium graveolens) leaves.
References:
1.  Rumpho, M.E., Edwards, G.E. and Loescher, W.H. A pathway for photosynthetic carbon flow to mannitol in celery leaves. Activity and localization of key enzymes. Plant Physiol. 73 (1983) 869–873. [PMID: 16663332]
[EC 1.1.1.224 created 1989]
 
 
EC 1.1.1.225     
Accepted name: chlordecone reductase
Reaction: chlordecone alcohol + NADP+ = chlordecone + NADPH + H+
Other name(s): CDR
Systematic name: chlordecone-alcohol:NADP+ 2-oxidoreductase
Comments: Chlordecone is an organochlorine pesticide.
References:
1.  Molowa, D.T., Shayne, A.G. and Guzelian, P.S. Purification and characterization of chlordecone reductase from human liver. J. Biol. Chem. 261 (1986) 12624–12627. [PMID: 2427522]
[EC 1.1.1.225 created 1989]
 
 
EC 1.1.1.226     
Accepted name: 4-hydroxycyclohexanecarboxylate dehydrogenase
Reaction: trans-4-hydroxycyclohexanecarboxylate + NAD+ = 4-oxocyclohexanecarboxylate + NADH + H+
Other name(s): trans-4-hydroxycyclohexanecarboxylate dehydrogenase
Systematic name: trans-4-hydroxycyclohexanecarboxylate:NAD+ 4-oxidoreductase
Comments: The enzyme from Corynebacterium cyclohexanicum is highly specific for the trans-4-hydroxy derivative.
References:
1.  Obata, H., Uebayashi, M. and Kaneda, T. Purification and properties of 4-hydroxycyclohexanecarboxylate dehydrogenase from Corynebacterium cyclohexanicum. Eur. J. Biochem. 174 (1988) 451–458. [PMID: 3292236]
[EC 1.1.1.226 created 1990]
 
 
EC 1.1.1.227     
Accepted name: (-)-borneol dehydrogenase
Reaction: (-)-borneol + NAD+ = (-)-camphor + NADH + H+
Systematic name: (-)-borneol:NAD+ oxidoreductase
Comments: NADP+ can also act, but more slowly.
References:
1.  Dehal, S.S. and Croteau, R. Metabolism of monoterpenes: specificity of the dehydrogenases responsible for the biosynthesis of camphor, 3-thujone, and 3-isothujone. Arch. Biochem. Biophys. 258 (1987) 287–291. [PMID: 3310901]
[EC 1.1.1.227 created 1990 (EC 1.1.1.182 created 1983, part incorporated 1990)]
 
 
EC 1.1.1.228     
Accepted name: (+)-sabinol dehydrogenase
Reaction: (+)-cis-sabinol + NAD+ = (+)-sabinone + NADH + H+
Other name(s): (+)-cis-sabinol dehydrogenase
Systematic name: (+)-cis-sabinol:NAD+ oxidoreductase
Comments: NADP+ can also act, but more slowly. Involved in the biosynthesis of (+)-3-thujone and (–)-3-isothujone.
References:
1.  Dehal, S.S. and Croteau, R. Metabolism of monoterpenes: specificity of the dehydrogenases responsible for the biosynthesis of camphor, 3-thujone, and 3-isothujone. Arch. Biochem. Biophys. 258 (1987) 287–291. [PMID: 3310901]
[EC 1.1.1.228 created 1990 (EC 1.1.1.182 created 1983, part incorporated 1990)]
 
 
EC 1.1.1.229     
Accepted name: diethyl 2-methyl-3-oxosuccinate reductase
Reaction: diethyl (2R,3R)-2-methyl-3-hydroxysuccinate + NADP+ = diethyl 2-methyl-3-oxosuccinate + NADPH + H+
Systematic name: diethyl-(2R,3R)-2-methyl-3-hydroxysuccinate:NADP+ 3-oxidoreductase
Comments: Also acts on diethyl (2S,3R)-2-methyl-3-hydroxysuccinate; and on the corresponding dimethyl esters.
References:
1.  Furuichi, A., Akita, H., Matsukura, H., Oishi, T. and Horikoshi, K. Purification and properties of an asymmetric reduction of diethyl 2-methyl-3-oxosuccinate in Saccharomyces fermentati. Agric. Biol. Chem. 51 (1987) 293–299.
[EC 1.1.1.229 created 1990]
 
 
EC 1.1.1.230     
Accepted name: 3α-hydroxyglycyrrhetinate dehydrogenase
Reaction: 3α-hydroxyglycyrrhetinate + NADP+ = 3-oxoglycyrrhetinate + NADPH + H+
Systematic name: 3α-hydroxyglycyrrhetinate:NADP+ 3-oxidoreductase
Comments: Highly specific to 3α-hydroxy derivatives of glycyrrhetinate and its analogues. Not identical to EC 1.1.1.50 3α-hydroxysteroid dehydrogenase (Si-specific).
References:
1.  Akao, T., Akao, T., Hattori, M., Namba, T. and Kobashi, K. Purification and properties of 3α-hydroxyglycyrrhetinate dehydrogenase of Clostridium innocuum from human intestine. J. Biochem. (Tokyo) 103 (1988) 504–507. [PMID: 3164718]
[EC 1.1.1.230 created 1990]
 
 
EC 1.1.1.231     
Accepted name: 15-hydroxyprostaglandin-I dehydrogenase (NADP+)
Reaction: (5Z,13E)-(15S)-6,9α-epoxy-11α,15-dihydroxyprosta-5,13-dienoate + NADP+ = (5Z,13E)-6,9α-epoxy-11α-hydroxy-15-oxoprosta-5,13-dienoate + NADPH + H+
Other name(s): prostacyclin dehydrogenase; PG I2 dehydrogenase; prostacyclin dehydrogenase; NADP-linked 15-hydroxyprostaglandin (prostacyclin) dehydrogenase; NADP+-dependent PGI2-specific 15-hydroxyprostaglandin dehydrogenase; 15-hydroxyprostaglandin-I dehydrogenase (NADP)
Systematic name: (5Z,13E)-(15S)-6,9α-epoxy-11α,15-dihydroxyprosta-5,13-dienoate:NADP+ 15-oxidoreductase
Comments: Specific for prostaglandin I2.
References:
1.  Korff, J.M. and Jarabak, J. Isolation and properties of an NADP+-dependent PGI2-specific 15-hydroxyprostaglandin dehydrogenase from rabbit kidney. Methods Enzymol. 86 (1982) 152–155. [PMID: 6182444]
[EC 1.1.1.231 created 1990]
 
 
EC 1.1.1.232     
Accepted name: 15-hydroxyicosatetraenoate dehydrogenase
Reaction: (15S)-15-hydroxy-5,8,11-cis-13-trans-icosatetraenoate + NAD(P)+ = 15-oxo-5,8,11-cis-13-trans-icosatetraenoate + NAD(P)H + H+
Other name(s): 15-hydroxyeicosatetraenoate dehydrogenase
Systematic name: (15S)-15-hydroxy-5,8,11-cis-13-trans-icosatetraenoate:NAD(P)+ 15-oxidoreductase
References:
1.  Sok, D.-E., Kang, J.B. and Shin, H.D. 15-Hydroxyeicosatetraenoic acid dehydrogenase activity in microsomal fraction of mouse liver homogenate. Biochem. Biophys. Res. Commun. 156 (1988) 524–529. [PMID: 3052453]
[EC 1.1.1.232 created 1992]
 
 
EC 1.1.1.233     
Accepted name: N-acylmannosamine 1-dehydrogenase
Reaction: N-acyl-D-mannosamine + NAD+ = N-acyl-D-mannosaminolactone + NADH + H+
Other name(s): N-acylmannosamine dehydrogenase; N-acetyl-D-mannosamine dehydrogenase; N-acyl-D-mannosamine dehydrogenase; N-acylmannosamine dehydrogenase
Systematic name: N-acyl-D-mannosamine:NAD+ 1-oxidoreductase
Comments: Acts on acetyl-D-mannosamine and glycolyl-D-mannosamine. Highly specific.
References:
1.  Horiuchi, T. and Kurokawa, T. Purification and properties of N-acyl-D-mannosamine dehydrogenase from Flavobacterium sp. 141-8. J. Biochem. (Tokyo) 104 (1988) 466–471. [PMID: 3240988]
[EC 1.1.1.233 created 1992]
 
 
EC 1.1.1.234     
Accepted name: flavanone 4-reductase
Reaction: (2S)-flavan-4-ol + NADP+ = (2S)-flavanone + NADPH + H+
Systematic name: (2S)-flavan-4-ol:NADP+ 4-oxidoreductase
Comments: Involved in the biosynthesis of 3-deoxyanthocyanidins from flavanones such as naringenin or eriodictyol.
References:
1.  Stich, K. and Forkmann, G. Biosynthesis of 3-deoxyanthocyanins with flower extracts from Sinningia cardinalis. Phytochemistry 27 (1988) 785–789.
[EC 1.1.1.234 created 1992]
 
 
EC 1.1.1.235     
Accepted name: 8-oxocoformycin reductase
Reaction: coformycin + NADP+ = 8-oxocoformycin + NADPH + H+
Other name(s): 8-ketodeoxycoformycin reductase
Systematic name: coformycin:NADP+ 8-oxidoreductase
Comments: Si-specific with respect to NADPH. Also reduces 8-oxodeoxy-coformycin to the nucleoside antibiotic deoxycoformycin.
References:
1.  Hanvey, J.C., Hawkins, E.S., Baker, D.C. and Suhadolnick, R.J. 8-Ketodeoxycoformycin and 8-ketocoformycin as intermediates in the biosynthesis of 2′-deoxycoformycin and coformycin. Biochemistry 27 (1988) 5790–5795. [PMID: 3052586]
[EC 1.1.1.235 created 1992]
 
 
EC 1.1.1.236     
Accepted name: tropinone reductase II
Reaction: pseudotropine + NADP+ = tropinone + NADPH + H+
Glossary: pseudotropine = ψ-tropine = 3β-hydroxytropane = tropan-3-exo-ol
Other name(s): tropinone (ψ-tropine-forming) reductase; pseudotropine forming tropinone reductase; tropinone reductase (ambiguous); TR-II
Systematic name: pseudotropine:NADP+ 3-oxidoreductase
Comments: This enzyme along with EC 1.1.1.206, tropine dehydrogenase, represents a branch point in tropane alkaloid metabolism [3]. Tropine (the product of EC 1.1.1.206) is incorporated into hyoscyamine and scopolamine whereas pseudotropine (the product of EC 1.1.1.236) is the first specific metabolite on the pathway to the calystegines [3]. Both enzymes are always found together in any given tropane-alkaloid-producing species, have a common substrate, tropinone, and are strictly stereospecific [2].
References:
1.  Dräger, B., Hashimoto, T. and Yamada, Y. Purification and characterization of pseudotropine forming tropinone reductase from Hyoscyamus niger root cultures. Agric. Biol. Chem. 52 (1988) 2663–2667.
2.  Couladis, M.M, Friesen, J.B., Landgrebe, M.E. and Leete, E. Enzymes catalysing the reduction of tropinone to tropine and ψ-tropine isolated from the roots of Datura innoxia. Pytochemistry 30 (1991) 801–805.
3.  Nakajima, K., Hashimoto, T. and Yamada, Y. Two tropinone reductases with different stereospecificities are short-chain dehydrogenases evolved from a common ancestor. Proc. Natl. Acad. Sci. USA 90 (1993) 9591–9595. [PMID: 8415746]
4.  Dräger, B. Tropinone reductases, enzymes at the branch point of tropane alkaloid metabolism. Phytochemistry 67 (2006) 327–337. [PMID: 16426652]
[EC 1.1.1.236 created 1992, modified 2007]
 
 
EC 1.1.1.237     
Accepted name: hydroxyphenylpyruvate reductase
Reaction: (1) (R)-3-(4-hydroxyphenyl)lactate + NAD(P)+ = 3-(4-hydroxyphenyl)pyruvate + NAD(P)H + H+
(2) (R)-3-(3,4-dihydroxyphenyl)lactate + NAD(P)+ = 3-(3,4-dihydroxyphenyl)pyruvate + NAD(P)H + H+
Other name(s): HPPR
Systematic name: (R)-3-(4-hydroxyphenyl)lactate:NAD(P)+ oxidoreductase
Comments: The enzyme participates in the biosynthesis of rosmarinic acid. It belongs to the family of D-isomer-specific 2-hydroxyacid dehydrogenases, and prefers NADPH to NADH.
References:
1.  Petersen, M. and Alfermann, A.W. Two new enzymes of rosmarinic acid biosynthesis from cell cultures of Coleus blumei: hydroxyphenylpyruvate reductase and rosmarinic acid synthase. Z. Naturforsch. C: Biosci. 43 (1988) 501–504.
2.  Kim, K.H., Janiak, V. and Petersen, M. Purification, cloning and functional expression of hydroxyphenylpyruvate reductase involved in rosmarinic acid biosynthesis in cell cultures of Coleus blumei. Plant Mol. Biol. 54 (2004) 311–323. [PMID: 15284489]
3.  Kim, Y.B., Uddina, M.R., Kim, Y., Park, C.G. and Park, S.U. Molecular cloning and characterization of tyrosine aminotransferase and hydroxyphenylpyruvate reductase, and rosmarinic acid accumulation in Scutellaria baicalensis. Nat. Prod. Commun. 9 (2014) 1311–1314. [PMID: 25918800]
4.  Wang, G.Q., Chen, J.F., Yi, B., Tan, H.X., Zhang, L. and Chen, W.S. HPPR encodes the hydroxyphenylpyruvate reductase required for the biosynthesis of hydrophilic phenolic acids in Salvia miltiorrhiza. Chin J Nat Med 15 (2017) 917–927. [PMID: 29329649]
[EC 1.1.1.237 created 1992, modified 2018]
 
 
EC 1.1.1.238     
Accepted name: 12β-hydroxysteroid dehydrogenase
Reaction: 3α,7α,12β-trihydroxy-5β-cholan-24-oate + NADP+ = 3α,7α-dihydroxy-12-oxo-5β-cholan-24-oate + NADPH + H+
Other name(s): 12β-hydroxy steroid (nicotinamide adenine dinucleotide phosphate) dehydrogenase
Systematic name: 12β-hydroxysteroid:NADP+ 12-oxidoreductase
Comments: Acts on a number of bile acids, both in their free and conjugated forms.
References:
1.  Edenharder, R. and Pfützner, A. Characterization of NADP-dependent 12β-hydroxysteroid dehydrogenase from Clostridium paraputrificum. Biochim. Biophys. Acta 962 (1988) 362–370. [PMID: 3167086]
[EC 1.1.1.238 created 1992]
 
 
EC 1.1.1.239     
Accepted name: 3α(17β)-hydroxysteroid dehydrogenase (NAD+)
Reaction: testosterone + NAD+ = androstenedione + NADH + H+
Glossary: androstenedione = androst-4-ene-3,17-dione
Other name(s): 3α,17β-hydroxy steroid dehydrogenase; 3α(17β)-HSD; 17-ketoreductase (ambiguous); 17β-HSD (ambiguous); HSD17B6 (gene name); HSD17B8 (gene name)
Systematic name: 3α(or 17β)-hydroxysteroid:NAD+ oxidoreductase
Comments: Also acts on other 17β-hydroxysteroids and on the 3α-hydroxy group of pregnanes and bile acids. Different from EC 1.1.1.50 3α-hydroxysteroid dehydrogenase (Si-specific) or EC 1.1.1.213 3α-hydroxysteroid dehydrogenase (Re-specific).
References:
1.  Sweat, M.L., Samuels, L.T. and Lumry, R. Preparation and characterisation of the enzyme which converts testosterone to androstendione. J. Biol. Chem. 185 (1950) 75–84. [PMID: 15436478]
2.  Villee, C.A. and Spencer, J.M. Some properties of the pyridine nucleotide-specific 17β-hydroxy steroid dehydrogenase of guinea pig liver. J. Biol. Chem. 235 (1960) 3615–3619. [PMID: 13781425]
3.  Endahl, G.L., Kochakia, C.D. and Hamm, D. Separation of a triphosphopyridine nucleotide-specific from a diphosphopyridine-specific 17β-hydroxy (testosterone) dehydrogenase of guinea pig liver. J. Biol. Chem. 235 (1960) 2792–2796. [PMID: 13696735]
4.  Ohmura, M., Hara, A., Nakagawa, M. and Sawada, H. Demonstration of 3α(17β)-hydroxysteroid dehydrogenase distinct from 3α-hydroxysteroid dehydrogenase in hamster liver. Biochem. J. 266 (1990) 583–589. [PMID: 2317205]
[EC 1.1.1.239 created 1992, modified 2012 (EC 1.1.1.63 created 1965, incorporated 2012)]
 
 
EC 1.1.1.240     
Accepted name: N-acetylhexosamine 1-dehydrogenase
Reaction: N-acetyl-α-D-glucosamine + NAD+ = N-acetyl-D-glucosaminate + NADH + H+
Other name(s): N-acetylhexosamine dehydrogenase; N-acetyl-D-hexosamine dehydrogenase
Systematic name: N-acetyl-D-hexosamine:NAD+ 1-oxidoreductase
Comments: Also acts on N-acetylgalactosamine and, more slowly, on N-acetylmannosamine. Anomeric specificity was tested with N-acetyl-D-glucosamine, and it was shown that the enzyme is specific for the α anomer.
References:
1.  Horiuchi, T. and Kurokawa, T. Purification and characterization of N-acetyl-D-hexosamine dehydrogenase from Pseudomonas sp no 53. Agric. Biol. Chem. 53 (1989) 1919–1925.
[EC 1.1.1.240 created 1992]
 
 
EC 1.1.1.241     
Accepted name: 6-endo-hydroxycineole dehydrogenase
Reaction: 6-endo-hydroxycineole + NAD+ = 6-oxocineole + NADH + H+
Systematic name: 6-endo-hydroxycineole:NAD+ 6-oxidoreductase
References:
1.  Williams, D.R., Trudgill, P.W. and Taylor, D.G. Metabolism of 1,8-cineole by Rhodococcus species: ring cleavage reactions. J. Gen. Microbiol. 135 (1989) 1957–1967.
[EC 1.1.1.241 created 1992]
 
 
EC 1.1.1.242      
Transferred entry: zeatin reductase. Now EC 1.3.1.69, zeatin reductase
[EC 1.1.1.242 created 1992, deleted 2001]
 
 
EC 1.1.1.243     
Accepted name: carveol dehydrogenase
Reaction: (–)-trans-carveol + NADP+ = (–)-carvone + NADPH + H+
Other name(s): (–)-trans-carveol dehydrogenase
Systematic name: (–)-trans-carveol:NADP+ oxidoreductase
References:
1.  Gershenzon, J., Maffei, M. and Croteau, R. Biochemical and histochemical-localization of monoterpene biosynthesis in the glandular trichomes of spearmint (Mentha spicata). Plant Physiol. 89 (1989) 1351–1357. [PMID: 16666709]
[EC 1.1.1.243 created 1992]
 
 
EC 1.1.1.244     
Accepted name: methanol dehydrogenase
Reaction: methanol + NAD+ = formaldehyde + NADH + H+
Systematic name: methanol:NAD+ oxidoreductase
References:
1.  Arfman, N., Watling, E.M., Clement, W., van Oosterwijk, R.J., de Vries, G.E., Harder, W., Attwood, M.M. and Dijkhuizen, L. Methanol metabolism in thermotolerant methylotrophic Bacillus strains involving a novel catabolic NAD-dependent methanol dehydrogenase as a key enzyme. Arch. Microbiol. 152 (1989) 280–288. [PMID: 2673121]
[EC 1.1.1.244 created 1992]
 
 
EC 1.1.1.245     
Accepted name: cyclohexanol dehydrogenase
Reaction: cyclohexanol + NAD+ = cyclohexanone + NADH + H+
Systematic name: cyclohexanol:NAD+ oxidoreductase
Comments: Also oxidizes some other alicyclic alcohols and diols.
References:
1.  Dangel, W., Tschech, A. and Fuchs, G. Enzyme-reactions involved in anaerobic cyclohexanol metabolism by a denitrifying Pseudomonas species. Arch. Microbiol. 152 (1989) 273–279. [PMID: 2505723]
2.  Donoghue, N.A. and Trudgill, P.W. The metabolism of cyclohexanol by Acinetobacter NCIB 9871. Eur. J. Biochem. 60 (1975) 1–7. [PMID: 1261]
3.  Trower, M.K., Buckland, R.M., Higgins, R. and Griffin, M. Isolation and characterization of a cyclohexane-metabolizing Xanthobacter sp. Appl. Environ. Microbiol. 49 (1985) 1282–1289. [PMID: 16346796]
[EC 1.1.1.245 created 1992]
 
 
EC 1.1.1.246      
Transferred entry: pterocarpin synthase. This activity is now known to be catalysed by two enzymes, vestitone reductase (EC 1.1.1.348) and medicarpin synthase (EC 4.2.1.139).
[EC 1.1.1.246 created 1992, deleted 2013]
 
 
EC 1.1.1.247     
Accepted name: codeinone reductase (NADPH)
Reaction: codeine + NADP+ = codeinone + NADPH + H+
Systematic name: codeine:NADP+ oxidoreductase
Comments: Catalyses the reversible reduction of codeinone to codeine, which is a direct precursor of morphine in the opium poppy plant, Papaver somniferum.
References:
1.  Lenz, R. and Zenk, M.H. Stereoselective reduction of codeinone, the penultimate step during morphine biosynthesis in Papaver somniferum. Tetrahedron Lett. 36 (1995) 2449–2452.
2.  Lenz, R. and Zenk, M.H. Purification and properties of codeinone reductase (NADPH) from Papaver somniferum cell cultures. Eur. J. Biochem. 233 (1995) 132–139. [PMID: 7588736]
[EC 1.1.1.247 created 1999, modified 2001]
 
 
EC 1.1.1.248     
Accepted name: salutaridine reductase (NADPH)
Reaction: salutaridinol + NADP+ = salutaridine + NADPH + H+
Systematic name: salutaridinol:NADP+ 7-oxidoreductase
Comments: Catalyses the reversible reduction of salutaridine to salutaridinol, which is a direct precursor of morphinan alkaloids in the poppy plant.
References:
1.  Gerady, R. and Zenk, M.H. Purification and characterization of salutaridine:NADPH 7-oxidoreductase from Papaver somniferum. Phytochemistry 34 (1993) 125–132.
[EC 1.1.1.248 created 1999, modified 2001]
 
 
EC 1.1.1.249      
Deleted entry: Provisional entry deleted. Revised and reinstated as EC 2.5.1.46 deoxyhypusine synthase
[EC 1.1.1.249 provisional version created 1999, deleted 1999 (reinstated 2001 as EC 2.5.1.46)]
 
 
EC 1.1.1.250     
Accepted name: D-arabinitol 2-dehydrogenase
Reaction: D-arabinitol + NAD+ = D-ribulose + NADH + H+
Other name(s): D-arabinitol 2-dehydrogenase (ribulose-forming)
Systematic name: D-arabinitol:NAD+ 2-oxidoreductase (D-ribulose-forming)
References:
1.  Wong, B., Murray, J.S., Castellanos, M. and Croen, K.D. D-Arabitol metabolism in Candida albicans: studies of the biosynthetic pathway and the gene that encodes NAD-dependent D-arabitol dehydrogenase. J. Bacteriol. 175 (1993) 6314–6320. [PMID: 8407803]
2.  Quong, M.W., Miyada, C.G., Switchenko, A.C. and Goodman, T.C. Identification, purification, and characterization of a D-arabinitol-specific dehydrogenase from Candida tropicalis. Biochem. Biophys. Res. Commun. 196 (1993) 1323–1329. [PMID: 8250887]
[EC 1.1.1.250 created 1999]
 
 
EC 1.1.1.251     
Accepted name: galactitol-1-phosphate 5-dehydrogenase
Reaction: galactitol 1-phosphate + NAD+ = D-tagatose 6-phosphate + NADH + H+
Other name(s): gatD (gene name)
Systematic name: galactitol-1-phosphate:NAD+ oxidoreductase
Comments: The enzyme from the bacterium Escherichia coli is involved in a galactitol degradation pathway. It contains two zinc atoms per subunit.
References:
1.  Wolff, J.B., Kaplan, N.O. Hexitol metabolism in Escherichia coli. J. Bacteriol. 71 (1956) 557–564. [PMID: 13331868]
2.  Nobelmann, B. and Lengeler, J.W. Sequence of the gat operon for galactitol utilization from a wild-type strain EC3132 of Escherichia coli. Biochim. Biophys. Acta 1262 (1995) 69–72. [PMID: 7772602]
3.  Benavente, R., Esteban-Torres, M., Kohring, G.W., Cortes-Cabrera, A., Sanchez-Murcia, P.A., Gago, F., Acebron, I., de las Rivas, B., Munoz, R. and Mancheno, J.M. Enantioselective oxidation of galactitol 1-phosphate by galactitol-1-phosphate 5-dehydrogenase from Escherichia coli. Acta Crystallogr. D Biol. Crystallogr. 71 (2015) 1540–1554. [PMID: 26143925]
[EC 1.1.1.251 created 1999]
 
 
EC 1.1.1.252     
Accepted name: tetrahydroxynaphthalene reductase
Reaction: scytalone + NADP+ = 1,3,6,8-tetrahydroxynaphthalene + NADPH + H+
Systematic name: scytalone:NADP+ Δ5-oxidoreductase
Comments: Reduces 1,3,6,8-tetrahydroxynaphthalene to scytalone and also reduces 1,3,8-trihydroxynaphthalene to vermelone. Involved with EC 4.2.1.94 scytalone dehydratase in the biosynthesis of melanin in pathogenic fungi.
References:
1.  Wheeler, M.H. and Greenblatt, G.A. The inhibition of melanin biosynthetic reactions in Pyricularia oryzae by compounds that prevent rice blast disease. Exp. Mycol. 12 (1988) 151–160.
2.  Vidal-Cros, A., Viviani, F., Labesse, G., Boccara, M. and Gaudry, M. Polyhydroxynaphthalene reductase involved in melanin biosynthesis in Magnaporthe grisea. Purification, cDNA cloning and sequencing. Eur. J. Biochem. 219 (1994) 985–992. [PMID: 8112349]
3.  Thompson, J.E., Basarab, G.S., Andersson, A., Lindqvist, Y. and Jordan, D.B. Trihydroxynaphthalene reductase from Magnaporthe grisea: realization of an active center inhibitor and elucidation of the kinetic mechanism. Biochemistry 36 (1997) 1852–1860. [PMID: 9048570]
[EC 1.1.1.252 created 1992 as EC 1.3.1.50, transferred 1999 to EC 1.1.1.252]
 
 
EC 1.1.1.253      
Transferred entry: pteridine reductase. Now EC 1.5.1.33, pteridine reductase
[EC 1.1.1.253 created 1999, deleted 2003]
 
 
EC 1.1.1.254     
Accepted name: (S)-carnitine 3-dehydrogenase
Reaction: (S)-carnitine + NAD+ = 3-dehydrocarnitine + NADH + H+
Systematic name: (S)-carnitine:NAD+ oxidoreductase
Comments: Specific for the (S)-enantiomer of carnitine, i.e., the enantiomer of the substrate of EC 1.1.1.108 carnitine 3-dehydrogenase
References:
1.  Setyahadi, S., Ueyama, T., Arimoto, T., Mori, N. and Kitamoto, Y. Purification and properties of a new enzyme, D-carnitine dehydrogenase, from Agrobacterium sp. 525a. Biosci. Biotechnol. Biochem. 61 (1997) 1055–1058. [PMID: 9214773]
[EC 1.1.1.254 created 1999]
 
 
EC 1.1.1.255     
Accepted name: mannitol dehydrogenase
Reaction: D-mannitol + NAD+ = D-mannose + NADH + H+
Other name(s): MTD; NAD-dependent mannitol dehydrogenase
Systematic name: mannitol:NAD+ 1-oxidoreductase
Comments: The enzyme from Apium graveolens (celery) oxidizes alditols with a minimum requirement of 2R chirality at the carbon adjacent to the primary carbon undergoing the oxidation. The enzyme is specific for NAD+ and does not use NADP+.
References:
1.  Stoop, J.M.H. and Pharr, D.M. Partial purification and characterization of mannitol: mannose 1-oxidoreductase from celeriac (Apium graveolens var. rapaceum) roots. Arch. Biochem. Biophys. 298 (1992) 612–619. [PMID: 1416989]
2.  Stoop, J.M.H., Williamson, J.D., Conkling, M.A. and Pharr, D.M. Purification of NAD-dependent mannitol dehydrogenase from celery suspension cultures. Plant Physiol. (1995) 108 (1995) 1219–1225. [PMID: 7630943]
3.  Williamson, J.D., Stoop, J.M.H., Massel, M.O., Conkling, M.A. and Pharr, D.M. Sequence analysis of a mannitol dehydrogenase cDNA from plants reveals a function for the pathogenesis-related protein ELI3. Proc. Natl. Acad. Sci. USA 92 (1995) 7148–7152. [PMID: 7638158]
4.  Stoop, J.M.H., Chilton, W.S. and Pharr, D.M. Substrate specificity of the NAD-dependent mannitol dehydrogenase from celery. Phytochemistry 43 (1996) 1145–1150.
[EC 1.1.1.255 created 2000]
 
 
EC 1.1.1.256     
Accepted name: fluoren-9-ol dehydrogenase
Reaction: fluoren-9-ol + NAD(P)+ = fluoren-9-one + NAD(P)H + H+
Systematic name: fluoren-9-ol:NAD(P)+ oxidoreductase
Comments: Involved in the pathway for fluorene metabolism in Arthrobacter sp.
References:
1.  Casellas, M., Grifoll, M., Bayona, J.M. and Solanas, A.M. New metabolites in the degradation of fluorene by Arthrobacter sp. strain F101. Appl. Environ. Microbiol. 63 (1997) 819–826. [PMID: 9055403]
2.  Grifoll, M., Casellas, M., Bayona, J.M. and Solanas, A.M. Isolation and characterization of a fluorene-degrading bacterium: identification of ring oxidation and ring fission products. Appl. Environ. Microbiol. 58 (1992) 2910–2917. [PMID: 1444405]
[EC 1.1.1.256 created 2000]
 
 
EC 1.1.1.257     
Accepted name: 4-(hydroxymethyl)benzenesulfonate dehydrogenase
Reaction: 4-(hydroxymethyl)benzenesulfonate + NAD+ = 4-formylbenzenesulfonate + NADH + H+
Systematic name: 4-(hydroxymethyl)benzenesulfonate:NAD+ oxidoreductase
Comments: Involved in the toluene-4-sulfonate degradation pathway in Comamonas testosteroni.
References:
1.  Junker, F., Saller, E., Schläfli Oppenberg, H.R., Kroneck, P.M., Leisinger, T. and Cook, A.M. Degradative pathways for p-toluenecarboxylate and p-toluenesulfonate and their multicomponent oxygenases in Comamonas testosteroni strains PSB-4 and T-2. Microbiology 142 (1996) 2419–2427. [PMID: 8828208]
[EC 1.1.1.257 created 2000]
 
 
EC 1.1.1.258     
Accepted name: 6-hydroxyhexanoate dehydrogenase
Reaction: 6-hydroxyhexanoate + NAD+ = 6-oxohexanoate + NADH + H+
Systematic name: 6-hydroxyhexanoate:NAD+ oxidoreductase
Comments: Involved in the cyclohexanol degradation pathway in Acinetobacter NCIB 9871.
References:
1.  Donoghue, N.A. and Trudgill, P.W. The metabolism of cyclohexanol by Acinetobacter NCIB 9871. Eur. J. Biochem. 60 (1975) 1–7. [PMID: 1261]
2.  Hecker, L.I., Tondeur, Y. and Farrelly, J.G. Formation of ε-hydroxycaproate and ε-aminocaproate from N-nitrosohexamethyleneimine: evidence that microsomal α-hydroxylation of cyclic nitrosamines may not always involve the insertion of molecular oxygen into the substrate. Chem. Biol. Interact. 49 (1984) 235–248. [PMID: 6722936]
[EC 1.1.1.258 created 2000]
 
 
EC 1.1.1.259     
Accepted name: 3-hydroxypimeloyl-CoA dehydrogenase
Reaction: 3-hydroxypimeloyl-CoA + NAD+ = 3-oxopimeloyl-CoA + NADH + H+
Glossary: pimelic acid = heptanedioic acid
Systematic name: 3-hydroxypimeloyl-CoA:NAD+ oxidoreductase
Comments: Involved in the anaerobic pathway of benzoate degradation in bacteria.
References:
1.  Harwood, C.S. and Gibson, J. Shedding light on anaerobic benzene ring degradation: a process unique to prokaryotes? J. Bacteriol. 179 (1997) 301–309. [PMID: 8990279]
[EC 1.1.1.259 created 2000]
 
 
EC 1.1.1.260     
Accepted name: sulcatone reductase
Reaction: sulcatol + NAD+ = sulcatone + NADH + H+
Glossary: sulcatone = 6-methylhept-5-en-2-one
sulcatol = 6-methylhept-5-en-2-ol
Systematic name: sulcatol:NAD+ oxidoreductase
Comments: Studies on the effects of growth-stage and nutrient supply on the stereochemistry of sulcatone reduction in Clostridia pasteurianum, C. tyrobutyricum and Lactobacillus brevis suggest that there may be at least two sulcatone reductases with different stereospecificities.
References:
1.  Belan, A., Botle, J., Fauve, A., Gourcy, J.G. and Veschambre, H. Use of biological systems for the preparation of chiral molecules. 3. An application in pheromone synthesis: Preparation of sulcatol enantiomers. J. Org. Chem. 52 (1987) 256–260.
2.  Tidswell, E.C., Salter, G.J., Kell, D.B. and Morris, J.G. Enantioselectivity of sulcatone reduction by some anaerobic bacteria. Enzyme Microb. Technol. 21 (1997) 143–147.
3.  Tidswell, E.C., Thompson, A.N. and Morris, J.G. Selection in chemostat culture of a mutant strain of Clostridium tryobutyricum improved in its reduction of ketones. J. Appl. Microbiol. Biotechnol. 35 (1991) 317–322.
[EC 1.1.1.260 created 2000, modified 2001]
 
 
EC 1.1.1.261     
Accepted name: sn-glycerol-1-phosphate dehydrogenase
Reaction: sn-glycerol 1-phosphate + NAD(P)+ = glycerone phosphate + NAD(P)H + H+
Glossary: glycerone phosphate = dihydroxyacetone phosphate = 3-hydroxy-2-oxopropyl phosphate
Other name(s): glycerol-1-phosphate dehydrogenase [NAD(P)+]; sn-glycerol-1-phosphate:NAD+ oxidoreductase; G-1-P dehydrogenase; Gro1PDH; AraM
Systematic name: sn-glycerol-1-phosphate:NAD(P)+ 2-oxidoreductase
Comments: This enzyme is found primarily as a Zn2+-dependent form in archaea but a Ni2+-dependent form has been found in Gram-positive bacteria [6]. The Zn2+-dependent metalloenzyme is responsible for the formation of archaea-specific sn-glycerol-1-phosphate, the first step in the biosynthesis of polar lipids in archaea. It is the enantiomer of sn-glycerol 3-phosphate, the form of glycerophosphate found in bacteria and eukaryotes. The other enzymes involved in the biosynthesis of polar lipids in archaea are EC 2.5.1.41 (phosphoglycerol geranylgeranyltransferase) and EC 2.5.1.42 (geranylgeranylglycerol-phosphate geranylgeranyltransferase), which together alkylate the hydroxy groups of glycerol 1-phosphate to give unsaturated archaetidic acid, which is acted upon by EC 2.7.7.67 (CDP-archaeol synthase) to form CDP-unsaturated archaeol. The final step in the pathway involves the addition of L-serine, with concomitant removal of CMP, leading to the production of unsaturated archaetidylserine [4]. Activity of the enzyme is stimulated by K+ [2].
References:
1.  Nishihara, M. and Koga, Y. sn-Glycerol-1-phosphate dehydrogenase in Methanobacterium thermoautotrophicum: key enzyme in biosynthesis of the enantiomeric glycerophosphate backbone of ether phospholipids of archaebacteria. J. Biochem. 117 (1995) 933–935. [PMID: 8586635]
2.  Nishihara, M. and Koga, Y. Purification and properties of sn-glycerol-1-phosphate dehydrogenase from Methanobacterium thermoautotrophicum: characterization of the biosynthetic enzyme for the enantiomeric glycerophosphate backbone of ether polar lipids of Archaea. J. Biochem. 122 (1997) 572–576. [PMID: 9348086]
3.  Koga, Y., Kyuragi, T., Nishihara, M. and Sone, N. Did archaeal and bacterial cells arise independently from noncellular precursors? A hypothesis stating that the advent of membrane phospholipid with enantiomeric glycerophosphate backbones caused the separation of the two lines of descent. J. Mol. Evol. 46 (1998) 54–63. [PMID: 9419225]
4.  Morii, H., Nishihara, M. and Koga, Y. CTP:2,3-di-O-geranylgeranyl-sn-glycero-1-phosphate cytidyltransferase in the methanogenic archaeon Methanothermobacter thermoautotrophicus. J. Biol. Chem. 275 (2000) 36568–36574. [PMID: 10960477]
5.  Han, J.S. and Ishikawa, K. Active site of Zn2+-dependent sn-glycerol-1-phosphate dehydrogenase from Aeropyrum pernix K1. Archaea 1 (2005) 311–317. [PMID: 15876564]
6.  Guldan, H., Sterner, R. and Babinger, P. Identification and characterization of a bacterial glycerol-1-phosphate dehydrogenase: Ni(2+)-dependent AraM from Bacillus subtilis. Biochemistry 47 (2008) 7376–7384. [PMID: 18558723]
[EC 1.1.1.261 created 2000, modified 2009]
 
 
EC 1.1.1.262     
Accepted name: 4-hydroxythreonine-4-phosphate dehydrogenase
Reaction: 4-phosphooxy-L-threonine + NAD+ = 3-amino-2-oxopropyl phosphate + CO2 + NADH + H+
Other name(s): NAD+-dependent threonine 4-phosphate dehydrogenase; L-threonine 4-phosphate dehydrogenase; 4-(phosphohydroxy)-L-threonine dehydrogenase; PdxA; 4-(phosphonooxy)-L-threonine:NAD+ oxidoreductase; 4-phosphooxy-L-threonine:NAD+ oxidoreductase
Systematic name: 4-phosphooxy-L-threonine:NAD+ 3-oxidoreductase (decarboxylating)
Comments: The enzyme is part of the biosynthesis pathway of the coenzyme pyridoxal 5′-phosphate found in anaerobic bacteria.
References:
1.  Cane, D.E., Hsiung, Y., Cornish, J.A., Robinson, J.K and Spenser, I.D. Biosynthesis of vitamine B6: The oxidation of L-threonine 4-phosphate by PdxA. J. Am. Chem. Soc. 120 (1998) 1936–1937.
2.  Laber, B., Maurer, W., Scharf, S., Stepusin, K. and Schmidt, F.S. Vitamin B6 biosynthesis: formation of pyridoxine 5′-phosphate from 4-(phosphohydroxy)-L-threonine and 1-deoxy-D-xylulose-5-phosphate by PdxA and PdxJ protein. FEBS Lett. 449 (1999) 45–48. [PMID: 10225425]
3.  Sivaraman, J., Li, Y., Banks, J., Cane, D.E., Matte, A. and Cygler, M. Crystal structure of Escherichia coli PdxA, an enzyme involved in the pyridoxal phosphate biosynthesis pathway. J. Biol. Chem. 278 (2003) 43682–43690. [PMID: 12896974]
4.  Banks, J. and Cane, D.E. Biosynthesis of vitamin B6: direct identification of the product of the PdxA-catalyzed oxidation of 4-hydroxy-l-threonine-4-phosphate using electrospray ionization mass spectrometry. Bioorg. Med. Chem. Lett. 14 (2004) 1633–1636. [PMID: 15026039]
[EC 1.1.1.262 created 2000, modified 2006]
 
 
EC 1.1.1.263     
Accepted name: 1,5-anhydro-D-fructose reductase
Reaction: 1,5-anhydro-D-glucitol + NADP+ = 1,5-anhydro-D-fructose + NADPH + H+
Systematic name: 1,5-anhydro-D-glucitol:NADP+ oxidoreductase
Comments: Also reduces pyridine-3-aldehyde and 2,3-butanedione. Acetaldehyde, 2-dehydroglucose (glucosone) and glucuronate are poor substrates, but there is no detectable action on glucose, mannose and fructose.
References:
1.  Sakuma, M., Kametani, S. and Akanuma, H. Purification and some properties of a hepatic NADPH-dependent reductase that specifically acts on 1,5-anhydro-D-fructose. J. Biochem. (Tokyo) 123 (1998) 189–193. [PMID: 9504428]
[EC 1.1.1.263 created 2000]
 
 
EC 1.1.1.264     
Accepted name: L-idonate 5-dehydrogenase
Reaction: L-idonate + NAD(P)+ = 5-dehydro-D-gluconate + NAD(P)H + H+
Systematic name: L-idonate:NAD(P)+ oxidoreductase
Comments: The enzyme from the bacterium Escherichia coli is specific for 5-dehydro-D-gluconate. cf. EC 1.1.1.366, L-idonate 5-dehydrogenase (NAD+).
References:
1.  Bausch, C., Peekhaus, N., Utz, C., Blais, T., Murray, E., Lowary, T. and Conway, T. Sequence analysis of the GntII (subsidiary) system for gluconate metabolism reveals a novel pathway for L-idonic acid catabolism in Escherichia coli. J. Bacteriol. 180 (1998) 3704–3710. [PMID: 9658018]
[EC 1.1.1.264 created 2000, modified 2013]
 
 
EC 1.1.1.265     
Accepted name: 3-methylbutanal reductase
Reaction: 3-methylbutanol + NAD(P)+ = 3-methylbutanal + NAD(P)H + H+
Systematic name: 3-methylbutanol:NAD(P)+ oxidoreductase
Comments: The enzyme purified from Saccharomyces cerevisiae catalyses the reduction of a number of straight-chain and branched aldehydes, as well as some aromatic aldehydes.
References:
1.  van Iersel, M.F.M., Eppink, M.H.M., van Berkel, W.J.H., Rombouts, F.M. and Abee, T. Purification and characterization of a novel NADP-dependent branched-chain alcohol dehydrogenase from Saccharomyces cerevisiae. Appl. Environ. Microbiol. 63 (1997) 4079–4082. [PMID: 9327572]
2.  Ven Nedervelde, L., Verlinden, V., Philipp, D. and Debourg, A. Purification and characterization of yeast 3-methyl butanal reductases involved in the removal of wort carbonyls during fermentation. Proc. 26th Congr.-Eur. Brew. Conv. (1997) 447–454.
[EC 1.1.1.265 created 2000]
 
 
EC 1.1.1.266     
Accepted name: dTDP-4-dehydro-6-deoxyglucose reductase
Reaction: dTDP-α-D-fucopyranose + NAD(P)+ = dTDP-4-dehydro-6-deoxy-α-D-glucose + NAD(P)H + H+
Glossary: dTDP-4-dehydro-6-deoxy-α-D-glucose = dTDP-6-deoxy-α-D-xylo-hexopyranos-4-ulose = thymidine 5′-[3-(6-deoxy--D-xylo-hexopyranosyl-4-ulose) diphosphate]
Other name(s): dTDP-4-keto-6-deoxyglucose reductase; dTDP-D-fucose:NADP+ oxidoreductase; Fcf1; dTDP-6-deoxy-D-xylo-hex-4-ulopyranose reductase
Systematic name: dTDP-α-D-fucopyranose:NAD(P)+ oxidoreductase
Comments: The enzymes from the Gram-negative bacteria Aggregatibacter actinomycetemcomitans and Escherichia coli O52 are involved in activation of fucose for incorporation into capsular polysaccharide O-antigens [1,3]. The enzyme from the Gram-positive bacterium Anoxybacillus tepidamans (Geobacillus tepidamans) is involved in activation of fucose for incorporation into the organism’s S-layer [2]. The enzyme from Escherichia coli O52 has a higher catalytic efficiency with NADH than with NADPH [3].
References:
1.  Yoshida, Y., Nakano, Y., Nezu, T., Yamashita, Y. and Koga, T. A novel NDP-6-deoxyhexosyl-4-ulose reductase in the pathway for the synthesis of thymidine diphosphate-D-fucose. J. Biol. Chem. 274 (1999) 16933–16939. [PMID: 10358040]
2.  Zayni, S., Steiner, K., Pfostl, A., Hofinger, A., Kosma, P., Schaffer, C. and Messner, P. The dTDP-4-dehydro-6-deoxyglucose reductase encoding fcd gene is part of the surface layer glycoprotein glycosylation gene cluster of Geobacillus tepidamans GS5-97T. Glycobiology 17 (2007) 433–443. [PMID: 17202151]
3.  Wang, Q., Ding, P., Perepelov, A.V., Xu, Y., Wang, Y., Knirel, Y.A., Wang, L. and Feng, L. Characterization of the dTDP-D-fucofuranose biosynthetic pathway in Escherichia coli O52. Mol. Microbiol. 70 (2008) 1358–1367. [PMID: 19019146]
[EC 1.1.1.266 created 2001, modified 2013]
 
 
EC 1.1.1.267     
Accepted name: 1-deoxy-D-xylulose-5-phosphate reductoisomerase
Reaction: 2-C-methyl-D-erythritol 4-phosphate + NADP+ = 1-deoxy-D-xylulose 5-phosphate + NADPH + H+
Other name(s): DXP-reductoisomerase; 1-deoxy-D-xylulose-5-phosphate isomeroreductase; 2-C-methyl-D-erythritol 4-phosphate (MEP) synthase
Systematic name: 2-C-methyl-D-erythritol-4-phosphate:NADP+ oxidoreductase (isomerizing)
Comments: The enzyme requires Mn2+, Co2+ or Mg2+ for activity, with the first being most effective. The enzyme from several eubacteria, including Escherichia coli, forms part of an alternative nonmevalonate pathway for terpenoid biosynthesis (for diagram, click here). The mechanism has been shown to be a retroaldol/aldol reaction [2].
References:
1.  Takahashi, S., Kuzuyama, T., Watanabe, H. and Seto, H.   A 1-deoxy-D-xylulose 5-phosphate reductoisomerase catalyzing the formation of 2-C-methyl-D-erythritol 4-phosphate in an alternative nonmevalonate pathway for terpenoid biosynthesis. Proc. Natl. Acad. Sci. USA 95 (1998) 9879–9884. [PMID: 9707569]
2.  Munos, J.W., Pu, X., Mansoorabadi, S.O., Kim, H.J. and Liu, H.W. A secondary kinetic isotope effect study of the 1-deoxy-D-xylulose-5-phosphate reductoisomerase-catalyzed reaction: evidence for a retroaldol-aldol rearrangement. J. Am. Chem. Soc. 131 (2009) 2048–2049. [PMID: 19159292]
[EC 1.1.1.267 created 2001]
 
 
EC 1.1.1.268     
Accepted name: 2-(R)-hydroxypropyl-CoM dehydrogenase
Reaction: 2-(R)-hydroxypropyl-CoM + NAD+ = 2-oxopropyl-CoM + NADH + H+
Glossary: coenzyme M (CoM) = 2-sulfanylethane-1-sulfonate = 2-mercaptoethanesulfonate (deprecated)
Other name(s): 2-(2-(R)-hydroxypropylthio)ethanesulfonate dehydrogenase; 2-[2-(R)-hydroxypropylthio]ethanesulfonate:NAD+ oxidoreductase
Systematic name: 2-{[(2R)-2-hydroxypropyl]sulfanyl}ethane-1-sulfonate:NAD+ oxidoreductase
Comments: The enzyme is highly specific for (R)-2-hydroxyalkyl thioethers of CoM, in contrast to EC 1.1.1.269, 2-(S)-hydroxypropyl-CoM dehydrogenase, which is highly specific for the (S)-enantiomer. This enzyme forms component III of a four-component enzyme system (comprising EC 4.4.1.23 [2-hydroxypropyl-CoM lyase; component I], EC 1.8.1.5 [2-oxopropyl-CoM reductase (carboxylating); component II], EC 1.1.1.268 [2-(R)-hydroxypropyl-CoM dehydrogenase; component III] and EC 1.1.1.269 [2-(S)-hydroxypropyl-CoM dehydrogenase; component IV]) that is involved in epoxyalkane carboxylation in Xanthobacter sp. strain Py2.
References:
1.  Allen, J.R., Clark, D.D., Krum, J.G. and Ensign, S.A. A role for coenzyme M (2-mercaptoethanesulfonic acid) in a bacterial pathway of aliphatic epoxide carboxylation. Proc. Natl. Acad. Sci. USA 96 (1999) 8432–8437. [PMID: 10411892]
[EC 1.1.1.268 created 2001]
 
 
EC 1.1.1.269     
Accepted name: 2-(S)-hydroxypropyl-CoM dehydrogenase
Reaction: (2S)-2-hydroxypropyl-CoM + NAD+ = 2-oxopropyl-CoM + NADH + H+
Glossary: coenzyme M (CoM) = 2-sulfanylethane-1-sulfonate = 2-mercaptoethanesulfonate (deprecated)
Other name(s): 2-(2-(S)-hydroxypropylthio)ethanesulfonate dehydrogenase; 2-[2-(S)-hydroxypropylthio]ethanesulfonate:NAD+ oxidoreductase
Systematic name: 2-{[(2S)-2-hydroxypropyl]sulfanyl}ethanesulfonate:NAD+ oxidoreductase
Comments: The enzyme is highly specific for (2S)-2-hydroxyalkyl thioethers of CoM, in contrast to EC 1.1.1.268, 2-(R)-hydroxypropyl-CoM dehydrogenase, which is highly specific for the (R)-enantiomer. This enzyme forms component IV of a four-component enzyme system click here that is involved in epoxyalkane carboxylation in Xanthobacter sp. strain Py2.
References:
1.  Allen, J.R., Clark, D.D., Krum, J.G. and Ensign, S.A. A role for coenzyme M (2-mercaptoethanesulfonic acid) in a bacterial pathway of aliphatic epoxide carboxylation. Proc. Natl. Acad. Sci. USA 96 (1999) 8432–8437. [PMID: 10411892]
[EC 1.1.1.269 created 2001]
 
 
EC 1.1.1.270     
Accepted name: 3β-hydroxysteroid 3-dehydrogenase
Reaction: a 3β-hydroxysteroid + NADP+ = a 3-oxosteroid + NADPH + H+
Other name(s): 3-keto-steroid reductase; 3-KSR; HSD17B7 (gene name); ERG27 (gene name)
Systematic name: 3β-hydroxysteroid:NADP+ 3-oxidoreductase
Comments: The enzyme acts on multiple 3β-hydroxysteroids. Participates in the biosynthesis of zemosterol and cholesterol, where it catalyses the reaction in the opposite direction to that shown. The mammalian enzyme is bifunctional and also catalyses EC 1.1.1.62, 17β-estradiol 17-dehydrogenase [4].
References:
1.  Swindell, A.C. and Gaylor, J.L. Investigation of the component reactions of oxidative sterol demethylation. Formation and metabolism of 3-ketosteroid intermediates. J. Biol. Chem. 243 (1968) 5546–5555. [PMID: 4387005]
2.  Billheimer, J.T., Alcorn, M. and Gaylor, J.L. Solubilization and partial purification of a microsomal 3-ketosteroid reductase of cholesterol biosynthesis. Purification and properties of 3β-hydroxysteroid dehydrogenase and Δ5-3-ketosteroid isomerase from bovine corpora lutea. Arch. Biochem. Biophys. 211 (1981) 430–438. [PMID: 6946726]
3.  Gachotte, D., Sen, S.E., Eckstein, J., Barbuch, R., Krieger, M., Ray, B.D. and Bard, M. Characterization of the Saccharomyces cerevisiae ERG27 gene encoding the 3-keto reductase involved in C-4 sterol demethylation. Proc. Natl. Acad. Sci. USA 96 (1999) 12655–12660. [PMID: 10535978]
4.  Marijanovic, Z., Laubner, D., Moller, G., Gege, C., Husen, B., Adamski, J. and Breitling, R. Closing the gap: identification of human 3-ketosteroid reductase, the last unknown enzyme of mammalian cholesterol biosynthesis. Mol. Endocrinol. 17 (2003) 1715–1725. [PMID: 12829805]
[EC 1.1.1.270 created 2002, modified 2012]
 
 
EC 1.1.1.271     
Accepted name: GDP-L-fucose synthase
Reaction: GDP-β-L-fucose + NADP+ = GDP-4-dehydro-α-D-rhamnose + NADPH + H+
Glossary: GDP-4-dehydro-α-D-rhamnose = GDP-4-dehydro-6-deoxy-α-D-mannose
Other name(s): GDP-4-keto-6-deoxy-D-mannose-3,5-epimerase-4-reductase; GDP-L-fucose:NADP+ 4-oxidoreductase (3,5-epimerizing)
Systematic name: GDP-β-L-fucose:NADP+ 4-oxidoreductase (3,5-epimerizing)
Comments: Both human and Escherichia coli enzymes can use NADH in place of NADPH to a slight extent.
References:
1.  Chang, S., Duerr, B. and Serif, G. An epimerase-reductase in L-fucose synthesis. J. Biol. Chem. 263 (1988) 1693–1697. [PMID: 3338988]
2.  Mattila, P., Räbinä, J, Hortling, S., Jelin, J. and Renkonen, R. Functional expression of Escherichia coli enzymes synthesizing GDP-L-fucose from inherent GDP-D-mannose in Saccharomyces cerevisiae. Glycobiology 10 (2000) 1041–1047. [PMID: 11030750]
3.  Menon, S., Stahl, M., Kumar, R., Xu, G.-Y. and Sullivan, F. Stereochemical course and steady state mechanism of the reaction catalyzed by the GDP-fucose synthetase from Escherichia coli. J. Biol. Chem. 274 (1999) 26743–26750. [PMID: 10480878]
4.  Somers, W.S., Stahl, M.L. and Sullivan, F.X. GDP-fucose synthetase from Escherichia coli: Structure of a unique member of the short-chain dehydrogenase/reductase family that catalyzes two distinct reactions at the same active site. Structure 6 (1998) 1601–1612. [PMID: 9862812]
[EC 1.1.1.271 created 2002, modified 2003]
 
 
EC 1.1.1.272     
Accepted name: D-2-hydroxyacid dehydrogenase (NADP+)
Reaction: an (R)-2-hydroxycarboxylate + NADP+ = a 2-oxocarboxylate + NADPH + H+
Other name(s): ddh (gene name)
Systematic name: (R)-2-hydroxycarboxylate:NADP+ oxidoreductase
Comments: This enzyme, characterized from the halophilic archaeon Haloferax mediterranei and the mold Aspergillus oryzae, catalyses a stereospecific reduction of 2-oxocarboxylic acids into the corresponding D-2-hydroxycarboxylic acids. The enzyme prefers substrates with a main chain of 5 carbons (such as 4-methyl-2-oxopentanoate) to those with a shorter chain, and can use NADH with much lower efficiency. cf. EC 1.1.1.345, (D)-2-hydroxyacid dehydrogenase (NAD+).
References:
1.  Domenech, J. and Ferrer, J. A new D-2-hydroxyacid dehydrogenase with dual coenzyme-specificity from Haloferax mediterranei, sequence analysis and heterologous overexpression. Biochim. Biophys. Acta 1760 (2006) 1667–1674. [PMID: 17049749]
2.  Shimizu, M., Yamamoto, T., Okabe, N., Sakai, K., Koide, E., Miyachi, Y., Kurimoto, M., Mochizuki, M., Yoshino-Yasuda, S., Mitsui, S., Ito, A., Murano, H., Takaya, N. and Kato, M. Novel 4-methyl-2-oxopentanoate reductase involved in synthesis of the Japanese sake flavor, ethyl leucate. Appl. Microbiol. Biotechnol. (2015) . [PMID: 26615399]
[EC 1.1.1.272 created 2002, modified 2013]
 
 
EC 1.1.1.273     
Accepted name: vellosimine dehydrogenase
Reaction: 10-deoxysarpagine + NADP+ = vellosimine + NADPH + H+
Systematic name: 10-deoxysarpagine:NADP+ oxidoreductase
Comments: Also acts on related alkaloids with an endo-aldehyde group as vellosimine (same stereochemistry at C-16) but only slight activity with exo-aldehydes. Detected in many cell suspension cultures of plants from the family Apocynaceae.
References:
1.  Pfitzner, A., Krausch, B. and Stöckigt, J. Characteristics of vellosimine reductase, a specific enzyme involved in the biosynthesis of the Rauwolfia alkaloid sarpagine. Tetrahedron 40 (1984) 1691–1699.
[EC 1.1.1.273 created 2002]
 
 
EC 1.1.1.274     
Accepted name: 2,5-didehydrogluconate reductase (2-dehydro-D-gluconate-forming)
Reaction: 2-dehydro-D-gluconate + NADP+ = 2,5-didehydro-D-gluconate + NADPH + H+
Other name(s): 2,5-diketo-D-gluconate reductase (ambiguous)
Systematic name: 2-dehydro-D-gluconate:NADP+ 2-oxidoreductase (2-dehydro-D-gluconate-forming)
Comments: The enzyme is involved in the catabolism of 2,5-didehydrogluconate. cf. EC 1.1.1.346, 2,5-didehydrogluconate reductase (2-dehydro-L-gulonate-forming).
References:
1.  Sonoyama, T., Kageyama, B., Yagi, S. and Mitsushima, K. Biochemical aspects of 2-keto-L-gulonate accumulation from 2,5-diketo-D-gluconate by Corynebacterium sp. and its mutants. Agric. Biol. Chem. 51 (1987) 3039–3047.
[EC 1.1.1.274 created 2002, modified 2013]
 
 
EC 1.1.1.275     
Accepted name: (+)-trans-carveol dehydrogenase
Reaction: (+)-trans-carveol + NAD+ = (+)-(S)-carvone + NADH + H+
Other name(s): carveol dehydrogenase
Systematic name: (+)-trans-carveol:NAD+ oxidoreductase
Comments: NADP+ cannot replace NAD+. Forms part of the monoterpenoid biosynthesis pathway in Carum carvi (caraway) seeds.
References:
1.  Bouwmeester, H.J., Gershenzon, J., Konings, M.C.J.M. and Croteau, R. Biosynthesis of the monoterpenes limonene and carvone in the fruit of caraway. I. Demonstration of enzyme activities and their changes with development. Plant Physiol. 117 (1998) 901–912. [PMID: 9662532]
[EC 1.1.1.275 created 2003]
 
 
EC 1.1.1.276     
Accepted name: serine 3-dehydrogenase (NADP+)
Reaction: L-serine + NADP+ = 2-aminoacetaldehyde + CO2 + NADPH + H+ (overall reaction)
(1a) L-serine + NADP+ = 2-aminomalonate semialdehyde + NADPH + H+
(1b) 2-aminomalonate semialdehyde = 2-aminoacetaldehyde + CO2 (spontaneous)
Other name(s): serine 3-dehydrogenase
Systematic name: L-serine:NADP+ 3-oxidoreductase
Comments: NAD+ cannot replace NADP+ [cf. EC 1.1.1.387, serine 3-dehydrogenase (NAD+)].
References:
1.  Fujisawa, H., Nagata, S., Chowdhury, E.K., Matsumoto, M. and Misono, H. Cloning and sequencing of the serine dehydrogenase gene from Agrobacterium tumefaciens. Biosci. Biotechnol. Biochem. 66 (2002) 1137–1139. [PMID: 12092831]
2.  Chowdhury, E.K., Higuchi, K., Nagata, S. and Misono, H. A novel NADP+ dependent serine dehydrogenase from Agrobacterium tumefaciens. Biosci. Biotechnol. Biochem. 61 (1997) 152–157. [PMID: 9028042]
[EC 1.1.1.276 created 2003, modified 2015]
 
 
EC 1.1.1.277     
Accepted name: 3β-hydroxy-5β-steroid dehydrogenase
Reaction: 3β-hydroxy-5β-pregnane-20-one + NADP+ = 5β-pregnan-3,20-dione + NADPH + H+
Other name(s): 3β-hydroxysteroid 5β-oxidoreductase; 3β-hydroxysteroid 5β-progesterone oxidoreductase
Systematic name: 3β-hydroxy-5β-steroid:NADP+ 3-oxidoreductase
References:
1.  Stuhlemmer, U. and Kreis, W. Cardenolide formation and activity of pregnane-modifying enzymes in cell suspension cultures, shoot cultures and leaves of Digitalis lanata. Plant Physiol. 34 (1996) 85–91.
2.  Seitz, H.U. and Gaertner, D.E. Enzymes in cardenolide-accumulating shoot cultures of Digitalis purpurea. Plant Cell 38 (1994) 337–344.
3.  Lindemann, P. and Luckner, M. Biosynthesis of pregnane derivatives in somatic embryos of Digitalis lanata. Phytochemistry 46 (1997) 507–513.
[EC 1.1.1.277 created 2003]
 
 
EC 1.1.1.278     
Accepted name: 3β-hydroxy-5α-steroid dehydrogenase
Reaction: 3β-hydroxy-5α-pregnane-20-one + NADP+ = 5α-pregnan-3,20-dione + NADPH + H+
Systematic name: 3β-hydroxy-5α-steroid:NADP+ 3-oxidoreductase
References:
1.  Lindemann, P. and Luckner, M. Biosynthesis of pregnane derivatives in somatic embryos of Digitalis lanata. Phytochemistry 46 (1997) 507–513.
2.  Warneck, H.M. and Seitz, H.U. 3β-Hydroxysteroid oxidoreductase in suspension cultures of Digitalis lanata EHRH. Z. Naturforsch. C: Biosci. 45 (1990) 963–972. [PMID: 2291772]
[EC 1.1.1.278 created 2003]
 
 
EC 1.1.1.279     
Accepted name: (R)-3-hydroxyacid-ester dehydrogenase
Reaction: ethyl (R)-3-hydroxyhexanoate + NADP+ = ethyl 3-oxohexanoate + NADPH + H+
Other name(s): 3-oxo ester (R)-reductase
Systematic name: ethyl-(R)-3-hydroxyhexanoate:NADP+ 3-oxidoreductase
Comments: Also acts on ethyl (R)-3-oxobutanoate and some other (R)-3-hydroxy acid esters. The (R)- symbol is allotted on the assumption that no substituents change the order of priority from O-3 > C-2 > C-4. A subunit of yeast fatty acid synthase EC 2.3.1.86, fatty-acyl-CoA synthase system. cf. EC 1.1.1.280, (S)-3-hydroxyacid ester dehydrogenase.
References:
1.  Heidlas, J., Engel, K.-H. and Tressl, R. Purification and characterization of two oxidoreductases involved in the enantioselective reduction of 3-oxo, 4-oxo and 5-oxo esters in baker's yeast. Eur. J. Biochem. 172 (1988) 633–639. [PMID: 3280313]
[EC 1.1.1.279 created 1990 as EC 1.2.1.55, transferred 2003 to EC 1.1.1.279, modified 2018]
 
 
EC 1.1.1.280     
Accepted name: (S)-3-hydroxyacid-ester dehydrogenase
Reaction: ethyl (S)-3-hydroxyhexanoate + NADP+ = ethyl 3-oxohexanoate + NADPH + H+
Other name(s): 3-oxo ester (S)-reductase
Systematic name: ethyl-(S)-3-hydroxyhexanoate:NADP+ 3-oxidoreductase
Comments: Also acts on 4-oxo- and 5-oxo-fatty acids and their esters. cf. EC 1.1.1.279 (R)-3-hydroxyacid-ester dehydrogenase.
References:
1.  Heidlas, J., Engel, K.-H. and Tressl, R. Purification and characterization of two oxidoreductases involved in the enantioselective reduction of 3-oxo, 4-oxo and 5-oxo esters in baker's yeast. Eur. J. Biochem. 172 (1988) 633–639. [PMID: 3280313]
[EC 1.1.1.280 created 1990 as EC 1.2.1.56, transferred 2003 to EC 1.1.1.280]
 
 
EC 1.1.1.281     
Accepted name: GDP-4-dehydro-6-deoxy-D-mannose reductase
Reaction: GDP-α-D-rhamnose + NAD(P)+ = GDP-4-dehydro-α-D-rhamnose + NAD(P)H + H+
Glossary: GDP-α-D-rhamnose = GDP-6-deoxy-α-D-mannose
GDP-4-dehydro-α-D-rhamnose = GDP-4-dehydro-6-deoxy-α-D-mannose
Other name(s): GDP-4-keto-6-deoxy-D-mannose reductase [ambiguous]; GDP-6-deoxy-D-lyxo-4-hexulose reductase; Rmd; GDP-6-deoxy-D-mannose:NAD(P)+ 4-oxidoreductase (D-rhamnose-forming); GDP-6-deoxy-α-D-mannose:NAD(P)+ 4-oxidoreductase (D-rhamnose-forming)
Systematic name: GDP-α-D-rhamnose:NAD(P)+ 4-oxidoreductase
Comments: This enzyme differs from EC 1.1.1.187, GDP-4-dehydro-D-rhamnose reductase, in that the only product formed is GDP-α-D-rhamnose. D-Rhamnose is a constituent of lipopolysaccharides of Gram-negative plant and human pathogenic bacteria.
References:
1.  Kneidinger, B., Graninger, M., Adam, G., Puchberger, M., Kosma, P., Zayni, S. and Messner, P. Identification of two GDP-6-deoxy-D-lyxo-4-hexulose reductases synthesizing GDP-D-rhamnose in Aneurinibacillus thermoaerophilus L420-91T. J. Biol. Chem. 276 (2001) 5577–5583. [PMID: 11096116]
2.  Mäki, M., Järvinen, N., Räbinä, J., Roos, C., Maaheimo, H., Mattila, P. and Renkonen, R. Functional expression of Pseudomonas aeruginosa GDP-4-keto-6-deoxy-D-mannose reductase which synthesizes GDP-rhamnose. Eur. J. Biochem. 269 (2002) 593–601. [PMID: 11856318]
[EC 1.1.1.281 created 2004]
 
 
EC 1.1.1.282     
Accepted name: quinate/shikimate dehydrogenase [NAD(P)+]
Reaction: (1) L-quinate + NAD(P)+ = 3-dehydroquinate + NAD(P)H + H+
(2) shikimate + NAD(P)+ = 3-dehydroshikimate + NAD(P)H + H+
Glossary: quinate = (1R,3R,4R,5R)-1,3,4,5-tetrahydroxycyclohexanecarboxylic acid and is a cyclitol carboxylate
The numbering system used for the 3-dehydroquinate is that of the recommendations on cyclitols, sections I-8 and I-9: and is shown in the reaction diagram. The use of the term '5-dehydroquinate' for this compound is based on an earlier system of numbering.
Other name(s): YdiB; quinate/shikimate dehydrogenase (ambiguous)
Systematic name: L-quinate:NAD(P)+ 3-oxidoreductase
Comments: This is the second shikimate dehydrogenase enzyme found in Escherichia coli. It can use both quinate and shikimate as substrates and either NAD+ or NADP+ as acceptor. The low catalytic efficiency with both quinate and shikimate suggests that neither may be the physiological substrate. cf. EC 1.1.1.24, quinate/shikimate dehydrogenase (NAD+), EC 1.1.5.8, quinate/shikimate dehydrogenase (quinone), and EC 1.1.1.25, shikimate dehydrogenase (NADP+).
References:
1.  Michel, G., Roszak, A.W., Sauvé, V., Maclean, J., Matte, A., Coggins, J.R., Cygler, M. and Lapthorn, A.J. Structures of shikimate dehydrogenase AroE and its paralog YdiB. A common structural framework for different activities. J. Biol. Chem. 278 (2003) 19463–19472. [PMID: 12637497]
2.  Benach, J., Lee, I., Edstrom, W., Kuzin, A.P., Chiang, Y., Acton, T.B., Montelione, G.T. and Hunt, J.F. The 2.3-Å crystal structure of the shikimate 5-dehydrogenase orthologue YdiB from Escherichia coli suggests a novel catalytic environment for an NAD-dependent dehydrogenase. J. Biol. Chem. 278 (2003) 19176–19182. [PMID: 12624088]
[EC 1.1.1.282 created 2004, modified 2021]
 
 
EC 1.1.1.283     
Accepted name: methylglyoxal reductase (NADPH)
Reaction: (S)-lactaldehyde + NADP+ = 2-oxopropanal + NADPH + H+
Glossary: 2-oxopropanal = methylglyoxal
Other name(s): lactaldehyde dehydrogenase (NADP+); GRE2 (gene name); methylglyoxal reductase (NADPH-dependent); lactaldehyde:NADP+ oxidoreductase
Systematic name: (S)-lactaldehyde:NADP+ oxidoreductase
Comments: The enzyme from the yeast Saccharomyces cerevisiae catalyses the reduction of a keto group in a number of compounds, forming enantiopure products. Among the substrates are methylglyoxal (which is reduced to (S)-lactaldehyde) [1,2], 3-methylbutanal [3], hexane-2,5-dione [4] and 3-chloro-1-phenylpropan-1-one [5]. The enzyme differs from EC 1.1.1.78, methylglyoxal reductase (NADH), which is found in mammals, by its coenzyme requirement, reaction direction, and enantiomeric preference.
References:
1.  Murata, K., Fukuda, Y., Simosaka, M., Watanabe, K., Saikusa, T. and Kimura, A. Metabolism of 2-oxoaldehyde in yeasts. Purification and characterization of NADPH-dependent methylglyoxal-reducing enzyme from Saccharomyces cerevisiae. Eur. J. Biochem. 151 (1985) 631–636. [PMID: 3896793]
2.  Chen, C.N., Porubleva, L., Shearer, G., Svrakic, M., Holden, L.G., Dover, J.L., Johnston, M., Chitnis, P.R. and Kohl, D.H. Associating protein activities with their genes: rapid identification of a gene encoding a methylglyoxal reductase in the yeast Saccharomyces cerevisiae. Yeast 20 (2003) 545–554. [PMID: 12722185]
3.  Hauser, M., Horn, P., Tournu, H., Hauser, N.C., Hoheisel, J.D., Brown, A.J. and Dickinson, J.R. A transcriptome analysis of isoamyl alcohol-induced filamentation in yeast reveals a novel role for Gre2p as isovaleraldehyde reductase. FEMS Yeast Res. 7 (2007) 84–92. [PMID: 16999827]
4.  Muller, M., Katzberg, M., Bertau, M. and Hummel, W. Highly efficient and stereoselective biosynthesis of (2S,5S)-hexanediol with a dehydrogenase from Saccharomyces cerevisiae. Org. Biomol. Chem. 8 (2010) 1540–1550. [PMID: 20237665]
5.  Choi, Y.H., Choi, H.J., Kim, D., Uhm, K.N. and Kim, H.K. Asymmetric synthesis of (S)-3-chloro-1-phenyl-1-propanol using Saccharomyces cerevisiae reductase with high enantioselectivity. Appl. Microbiol. Biotechnol. 87 (2010) 185–193. [PMID: 20111861]
6.  Breicha, K., Muller, M., Hummel, W. and Niefind, K. Crystallization and preliminary crystallographic analysis of Gre2p, an NADP+-dependent alcohol dehydrogenase from Saccharomyces cerevisiae. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 66 (2010) 838–841. [PMID: 20606287]
[EC 1.1.1.283 created 2005, modified 2013]
 
 
EC 1.1.1.284     
Accepted name: S-(hydroxymethyl)glutathione dehydrogenase
Reaction: S-(hydroxymethyl)glutathione + NAD(P)+ = S-formylglutathione + NAD(P)H + H+
Other name(s): NAD-linked formaldehyde dehydrogenase (incorrect); formaldehyde dehydrogenase (incorrect); formic dehydrogenase (incorrect); class III alcohol dehydrogenase; ADH3; χ-ADH; FDH (incorrect); formaldehyde dehydrogenase (glutathione) (incorrect); GS-FDH (incorrect); glutathione-dependent formaldehyde dehydrogenase (incorrect); GD-FALDH; NAD- and glutathione-dependent formaldehyde dehydrogenase; NAD-dependent formaldehyde dehydrogenase (incorrect)
Systematic name: S-(hydroxymethyl)glutathione:NAD+ oxidoreductase
Comments: The substrate, S-(hydroxymethyl)glutathione, forms spontaneously from glutathione and formaldehyde; its rate of formation is increased in some bacteria by the presence of EC 4.4.1.22, S-(hydroxymethyl)glutathione synthase. This enzyme forms part of the pathway that detoxifies formaldehyde, since the product is hydrolysed by EC 3.1.2.12, S-formylglutathione hydrolase. The human enzyme belongs to the family of zinc-dependent alcohol dehydrogenases. Also specifically reduces S-nitrosylglutathione.
References:
1.  Jakoby, W.B. Aldehyde dehydrogenases. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Ed.), The Enzymes, 2nd edn, vol. 7, Academic Press, New York, 1963, pp. 203–221.
2.  Rose, Z.B. and Racker, E. Formaldehyde dehydrogenase. Methods Enzymol. 9 (1966) 357–360.
3.  Liu, L., Hausladen, A., Zeng, M., Que, L., Heitman, J. and Stamler, J.S. A metabolic enzyme for S-nitrosothiol conserved from bacteria to humans. Nature 410 (2001) 490–494. [PMID: 11260719]
4.  Sanghani, P.C., Stone, C.L., Ray, B.D., Pindel, E.V., Hurley, T.D. and Bosron, W.F. Kinetic mechanism of human glutathione-dependent formaldehyde dehydrogenase. Biochemistry 39 (2000) 10720–10729. [PMID: 10978156]
5.  van Ophem, P.W. and Duine, J.A. NAD- and co-substrate (GSH or factor)-dependent formaldehyde dehydrogenases from methylotrophic microorganisms act as a class III alcohol dehydrogenase. FEMS Microbiol. Lett. 116 (1994) 87–94.
6.  Ras, J., van Ophem, P.W., Reijnders, W.N., Van Spanning, R.J., Duine, J.A., Stouthamer, A.H. and Harms, N. Isolation, sequencing, and mutagenesis of the gene encoding NAD- and glutathione-dependent formaldehyde dehydrogenase (GD-FALDH) from Paracoccus denitrificans, in which GD-FALDH is essential for methylotrophic growth. J. Bacteriol. 177 (1995) 247–251. [PMID: 7798140]
7.  Barber, R.D., Rott, M.A. and Donohue, T.J. Characterization of a glutathione-dependent formaldehyde dehydrogenase from Rhodobacter sphaeroides. J. Bacteriol. 178 (1996) 1386–1393. [PMID: 8631716]
[EC 1.1.1.284 created 2005 (EC 1.2.1.1 created 1961, modified 1982, modified 2002, part transferred 2005 to EC 1.1.1.284)]
 
 
EC 1.1.1.285     
Accepted name: 3′′-deamino-3′′-oxonicotianamine reductase
Reaction: 2′-deoxymugineic acid + NAD(P)+ = 3′′-deamino-3′′-oxonicotianamine + NAD(P)H + H+
Systematic name: 2′-deoxymugineic acid:NAD(P)+ 3′′-oxidoreductase
References:
1.  Shojima, S., Nishizawa, N.-K., Fushiya, S., Nozoe, S., Irifune, T. and Mori, S. In vitro biosynthesis of 2′-deoxymugineic acid from L-methionine and nicotianamine. Plant Physiol. 93 (1990) 1497–1503. [PMID: 16667646]
[EC 1.1.1.285 created 2005]
 
 
EC 1.1.1.286     
Accepted name: isocitrate—homoisocitrate dehydrogenase
Reaction: (1) isocitrate + NAD+ = 2-oxoglutarate + CO2 + NADH
(2) (1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate + NAD+ = 2-oxoadipate + CO2 + NADH + H+
Glossary: isocitrate = (1R,2S)-1-hydroxypropane-1,2,3-tricarboxylate (previously known as threo-Ds-isocitrate)
homoisocitrate = (-)-threo-homoisocitrate = (1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate
Other name(s): homoisocitrate—isocitrate dehydrogenase; PH1722
Systematic name: isocitrate(homoisocitrate):NAD+ oxidoreductase (decarboxylating)
Comments: Requires Mn2+ and K+ or NH4+ for activity. Unlike EC 1.1.1.41, isocitrate dehydrogenase (NAD+) and EC 1.1.1.87, homoisocitrate dehydrogenase, this enzyme, from Pyrococcus horikoshii, can use both isocitrate and homoisocitrate as substrates. The enzyme may play a role in both the lysine and glutamate biosynthesis pathways.
References:
1.  Miyazaki, K. Bifunctional isocitrate-homoisocitrate dehydrogenase: a missing link in the evolution of β-decarboxylating dehydrogenase. Biochem. Biophys. Res. Commun. 331 (2005) 341–346. [PMID: 15845397]
[EC 1.1.1.286 created 2005]
 
 
EC 1.1.1.287     
Accepted name: D-arabinitol dehydrogenase (NADP+)
Reaction: (1) D-arabinitol + NADP+ = D-xylulose + NADPH + H+
(2) D-arabinitol + NADP+ = D-ribulose + NADPH + H+
Other name(s): NADP+-dependent D-arabitol dehydrogenase; ARD1p; D-arabitol dehydrogenase 1
Systematic name: D-arabinitol:NADP+ oxidoreductase
Comments: The enzyme from the rust fungus Uromyces fabae can use D-arabinitol and D-mannitol as substrates in the forward direction and D-xylulose, D-ribulose and, to a lesser extent, D-fructose as substrates in the reverse direction. This enzyme carries out the reactions of both EC 1.1.1.11, D-arabinitol 4-dehydrogenase and EC 1.1.1.250, D-arabinitol 2-dehydrogenase, but unlike them, uses NADP+ rather than NAD+ as cofactor. D-Arabinitol is capable of quenching reactive oxygen species involved in defense reactions of the host plant.
References:
1.  Link, T., Lohaus, G., Heiser, I., Mendgen, K., Hahn, M. and Voegele, R.T. Characterization of a novel NADP+-dependent D-arabitol dehydrogenase from the plant pathogen Uromyces fabae. Biochem. J. 389 (2005) 289–295. [PMID: 15796718]
[EC 1.1.1.287 created 2005]
 
 
EC 1.1.1.288     
Accepted name: xanthoxin dehydrogenase
Reaction: xanthoxin + NAD+ = abscisic aldehyde + NADH + H+
Other name(s): xanthoxin oxidase; ABA2
Systematic name: xanthoxin:NAD+ oxidoreductase
Comments: Requires a molybdenum cofactor for activity. NADP+ cannot replace NAD+ and short-chain alcohols such as ethanol, isopropanol, butanol and cyclohexanol cannot replace xanthoxin as substrate [3]. Involved in the abscisic-acid biosynthesis pathway in plants, along with EC 1.2.3.14 (abscisic-aldehyde oxidase), EC 1.13.11.51 (9-cis-epoxycarotenoid dioxygenase) and EC 1.14.13.93 [(+)-abscisic acid 8′-hydroxylase]. Abscisic acid is a sesquiterpenoid plant hormone that is involved in the control of a wide range of essential physiological processes, including seed development, germination and responses to stress [3].
References:
1.  Sindhu, R.K. and Walton, D.C. Xanthoxin metabolism in cell-free preparations from wild type and wilty mutants of tomato. Plant Physiol. 88 (1988) 178–182. [PMID: 16666262]
2.  Schwartz, S.H., Leon-Kloosterziel, K.M., Koornneef, M. and Zeevaart, J.A. Biochemical characterization of the aba2 and aba3 mutants in Arabidopsis thaliana. Plant Physiol. 114 (1997) 161–166. [PMID: 9159947]
3.  González-Guzmán, M., Apostolova, N., Bellés, J.M., Barrero, J.M., Piqueras, P., Ponce, M.R., Micol, J.L., Serrano, R. and Rodríguez, P.L. The short-chain alcohol dehydrogenase ABA2 catalyzes the conversion of xanthoxin to abscisic aldehyde. Plant Cell 14 (2002) 1833–1846. [PMID: 12172025]
[EC 1.1.1.288 created 2005]
 
 
EC 1.1.1.289     
Accepted name: sorbose reductase
Reaction: D-glucitol + NADP+ = L-sorbose + NADPH + H+
Glossary: L-sorbose = L-xylo-hex-2-ulose
Other name(s): Sou1p
Systematic name: D-glucitol:NADP+ oxidoreductase
Comments: The reaction occurs predominantly in the reverse direction. This enzyme can also convert D-fructose into D-mannitol, but more slowly. Belongs in the short-chain dehydrogenase family.
References:
1.  Greenberg, J.R., Price, N.P., Oliver, R.P., Sherman, F. and Rustchenko, E. Candida albicans SOU1 encodes a sorbose reductase required for L-sorbose utilization. Yeast 22 (2005) 957–969. [PMID: 16134116]
2.  Greenberg, J.R., Price, N.P., Oliver, R.P., Sherman, F. and Rustchenko, E. Erratum report: Candida albicans SOU1 encodes a sorbose reductase required for L-sorbose utilization. Yeast 22 (2005) 1171.
3.  Sugisawa, T., Hoshino, T. and Fujiwara, A. Purification and properties of NADPH-linked L-sorbose reductase from Gluconobacter melanogenus N44-1. Agric. Biol. Chem. 55 (1991) 2043–2049.
4.  Shinjoh, M., Tazoe, M. and Hoshino, T. NADPH-dependent L-sorbose reductase is responsible for L-sorbose assimilation in Gluconobacter suboxydans IFO 3291. J. Bacteriol. 184 (2002) 861–863. [PMID: 11790761]
[EC 1.1.1.289 created 2006]
 
 
EC 1.1.1.290     
Accepted name: 4-phosphoerythronate dehydrogenase
Reaction: 4-phospho-D-erythronate + NAD+ = (3R)-3-hydroxy-2-oxo-4-phosphooxybutanoate + NADH + H+
Other name(s): PdxB; PdxB 4PE dehydrogenase; 4-O-phosphoerythronate dehydrogenase; 4PE dehydrogenase; erythronate-4-phosphate dehydrogenase
Systematic name: 4-phospho-D-erythronate:NAD+ 2-oxidoreductase
Comments: This enzyme catalyses a step in a bacterial pathway for the biosynthesis of pyridoxal 5′-phosphate. The enzyme contains a tightly-bound NAD(H) cofactor that is not re-oxidized by free NAD+. In order to re-oxidize the cofactor and restore enzyme activity, the enzyme catalyses the reduction of a 2-oxo acid (such as 2-oxoglutarate, oxaloacetate, or pyruvate) to the respective (R)-hydroxy acid [6]. cf. EC 1.1.1.399, 2-oxoglutarate reductase.
References:
1.  Lam, H.M. and Winkler, M.E. Metabolic relationships between pyridoxine (vitamin B6) and serine biosynthesis in Escherichia coli K-12. J. Bacteriol. 172 (1990) 6518–6528. [PMID: 2121717]
2.  Pease, A.J., Roa, B.R., Luo, W. and Winkler, M.E. Positive growth rate-dependent regulation of the pdxA, ksgA, and pdxB genes of Escherichia coli K-12. J. Bacteriol. 184 (2002) 1359–1369. [PMID: 11844765]
3.  Zhao, G. and Winkler, M.E. A novel α-ketoglutarate reductase activity of the serA-encoded 3-phosphoglycerate dehydrogenase of Escherichia coli K-12 and its possible implications for human 2-hydroxyglutaric aciduria. J. Bacteriol. 178 (1996) 232–239. [PMID: 8550422]
4.  Grant, G.A. A new family of 2-hydroxyacid dehydrogenases. Biochem. Biophys. Res. Commun. 165 (1989) 1371–1374. [PMID: 2692566]
5.  Schoenlein, P.V., Roa, B.B. and Winkler, M.E. Divergent transcription of pdxB and homology between the pdxB and serA gene products in Escherichia coli K-12. J. Bacteriol. 171 (1989) 6084–6092. [PMID: 2681152]
6.  Rudolph, J., Kim, J. and Copley, S.D. Multiple turnovers of the nicotino-enzyme PdxB require α-keto acids as cosubstrates. Biochemistry 49 (2010) 9249–9255. [PMID: 20831184]
[EC 1.1.1.290 created 2006, modified 2016]
 
 
EC 1.1.1.291     
Accepted name: 2-hydroxymethylglutarate dehydrogenase
Reaction: (S)-2-hydroxymethylglutarate + NAD+ = 2-formylglutarate + NADH + H+
Other name(s): HgD
Systematic name: (S)-2-hydroxymethylglutarate:NAD+ oxidoreductase
Comments: NADP+ cannot replace NAD+. Forms part of the nicotinate-fermentation catabolism pathway in Eubacterium barkeri. Other enzymes involved in this pathway are EC 1.17.1.5 (nicotinate dehydrogenase), EC 1.3.7.1 (6-hydroxynicotinate reductase), EC 3.5.2.18 (enamidase), EC 5.4.99.4 (2-methyleneglutarate mutase), EC 5.3.3.6 (methylitaconate Δ-isomerase), EC 4.2.1.85 (dimethylmaleate hydratase) and EC 4.1.3.32 (2,3-dimethylmalate lyase).
References:
1.  Alhapel, A., Darley, D.J., Wagener, N., Eckel, E., Elsner, N. and Pierik, A.J. Molecular and functional analysis of nicotinate catabolism in Eubacterium barkeri. Proc. Natl. Acad. Sci. USA 103 (2006) 12341–12346. [PMID: 16894175]
[EC 1.1.1.291 created 2006]
 
 
EC 1.1.1.292     
Accepted name: 1,5-anhydro-D-fructose reductase (1,5-anhydro-D-mannitol-forming)
Reaction: 1,5-anhydro-D-mannitol + NADP+ = 1,5-anhydro-D-fructose + NADPH + H+
Other name(s): 1,5-anhydro-D-fructose reductase (ambiguous); AFR (ambiguous)
Systematic name: 1,5-anhydro-D-mannitol:NADP+ oxidoreductase
Comments: This enzyme is present in some but not all Rhizobium species and belongs in the GFO/IDH/MocA protein family [2]. This enzyme differs from hepatic 1,5-anhydro-D-fructose reductase, which yields 1,5-anhydro-D-glucitol as the product (see EC 1.1.1.263). In Sinorhizobium morelense, the product of the reaction, 1,5-anhydro-D-mannitol, can be further metabolized to D-mannose [1]. The enzyme also reduces 1,5-anhydro-D-erythro-hexo-2,3-diulose and 2-ketoaldoses (called osones), such as D-glucosone (D-arabino-hexos-2-ulose) and 6-deoxy-D-glucosone. It does not reduce common aldoses and ketoses, or non-sugar aldehydes and ketones [1].
References:
1.  Kühn, A., Yu, S. and Giffhorn, F. Catabolism of 1,5-anhydro-D-fructose in Sinorhizobium morelense S-30.7.5: discovery, characterization, and overexpression of a new 1,5-anhydro-D-fructose reductase and its application in sugar analysis and rare sugar synthesis. Appl. Environ. Microbiol. 72 (2006) 1248–1257. [PMID: 16461673]
2.  Dambe, T.R., Kühn, A.M., Brossette, T., Giffhorn, F. and Scheidig, A.J. Crystal structure of NADP(H)-dependent 1,5-anhydro-D-fructose reductase from Sinorhizobium morelense at 2.2 Å resolution: construction of a NADH-accepting mutant and its application in rare sugar synthesis. Biochemistry 45 (2006) 10030–10042. [PMID: 16906761]
[EC 1.1.1.292 created 2007]
 
 
EC 1.1.1.293      
Deleted entry: tropinone reductase I. This enzyme was already in the Enzyme List as EC 1.1.1.206, tropine dehydrogenase so EC 1.1.1.293 has been withdrawn at the public-review stage
[EC 1.1.1.293 created 2007, withdrawn while undergoing public review]
 
 
EC 1.1.1.294     
Accepted name: chlorophyll(ide) b reductase
Reaction: 71-hydroxychlorophyllide a + NAD(P)+ = chlorophyllide b + NAD(P)H + H+
Other name(s): chlorophyll b reductase; Chl b reductase
Systematic name: 71-hydroxychlorophyllide-a:NAD(P)+ oxidoreductase
Comments: This enzyme carries out the first step in the conversion of chlorophyll b to chlorophyll a. It is involved in chlorophyll degradation, which occurs during leaf senescence [3] and it also forms part of the chlorophyll cycle, which interconverts chlorophyll a and b in response to changing light conditions [4,5].
References:
1.  Scheumann, V., Ito, H., Tanaka, A., Schoch, S. and Rüdiger, W. Substrate specificity of chlorophyll(ide) b reductase in etioplasts of barley (Hordeum vulgare L.). Eur. J. Biochem. 242 (1996) 163–170. [PMID: 8954166]
2.  Scheumann, V., Schoch, S. and Rüdiger, W. Chlorophyll a formation in the chlorophyll b reductase reaction requires reduced ferredoxin. J. Biol. Chem. 273 (1998) 35102–35108. [PMID: 9857045]
3.  Hörtensteiner, S. Chlorophyll degradation during senescence. Annu. Rev. Plant Biol. 57 (2006) 55–77. [PMID: 16669755]
4.  Ito, H., Ohtsuka, T. and Tanaka, A. Conversion of chlorophyll b to chlorophyll a via 7-hydroxymethyl chlorophyll. J. Biol. Chem. 271 (1996) 1475–1479. [PMID: 8576141]
5.  Rüdiger, W. Biosynthesis of chlorophyll b and the chlorophyll cycle. Photosynth. Res. 74 (2002) 187–193. [PMID: 16228557]
[EC 1.1.1.294 created 2007]
 
 
EC 1.1.1.295     
Accepted name: momilactone-A synthase
Reaction: 3β-hydroxy-9β-pimara-7,15-diene-19,6β-olide + NAD(P)+ = momilactone A + NAD(P)H + H+
Other name(s): momilactone A synthase; OsMAS
Systematic name: 3β-hydroxy-9β-pimara-7,15-diene-19,6β-olide:NAD(P)+ oxidoreductase
Comments: The rice phytoalexin momilactone A is a diterpenoid secondary metabolite that is involved in the defense mechanism of the plant. Momilactone A is produced in response to attack by a pathogen through the perception of elicitor signal molecules such as chitin oligosaccharide, or after exposure to UV irradiation. The enzyme, which catalyses the last step in the biosynthesis of momilactone A, can use both NAD+ and NADP+ but activity is higher with NAD+ [1].
References:
1.  Atawong, A., Hasegawa, M. and Kodama, O. Biosynthesis of rice phytoalexin: enzymatic conversion of 3β-hydroxy-9β-pimara-7,15-dien-19,6β-olide to momilactone A. Biosci. Biotechnol. Biochem. 66 (2002) 566–570. [PMID: 12005050]
2.  Shimura, K., Okada, A., Okada, K., Jikumaru, Y., Ko, K.W., Toyomasu, T., Sassa, T., Hasegawa, M., Kodama, O., Shibuya, N., Koga, J., Nojiri, H. and Yamane, H. Identification of a biosynthetic gene cluster in rice for momilactones. J. Biol. Chem. 282 (2007) 34013–34018. [PMID: 17872948]
[EC 1.1.1.295 created 2008]
 
 
EC 1.1.1.296     
Accepted name: dihydrocarveol dehydrogenase
Reaction: menth-8-en-2-ol + NAD+ = menth-8-en-2-one + NADH + H+
Glossary: (+)-dihydrocarveol = (1S,2S,4S)-menth-8-en-2-ol
(+)-isodihydrocarveol = (1S,2S,4R)-menth-8-en-2-ol
(+)-neoisodihydrocarveol = (1S,2R,4R)-menth-8-en-2-ol
(–)-dihydrocarvone = (1S,4S)-menth-8-en-2-one
(+)-isodihydrocarvone = (1S,4R)-menth-8-en-2-one
Other name(s): carveol dehydrogenase (ambiguous)
Systematic name: menth-8-en-2-ol:NAD+ oxidoreductase
Comments: This enzyme from the Gram-positive bacterium Rhodococcus erythropolis DCL14 forms part of the carveol and dihydrocarveol degradation pathway. The enzyme accepts all eight stereoisomers of menth-8-en-2-ol as substrate, although some isomers are converted faster than others. The preferred substrates are (+)-neoisodihydrocarveol, (+)-isodihydrocarveol, (+)-dihydrocarveol and (–)-isodihydrocarveol.
References:
1.  van der Werf, M.J. and Boot, A.M. Metabolism of carveol and dihydrocarveol in Rhodococcus erythropolis DCL14. Microbiology 146 (2000) 1129–1141. [PMID: 10832640]
[EC 1.1.1.296 created 2008]
 
 
EC 1.1.1.297     
Accepted name: limonene-1,2-diol dehydrogenase
Reaction: menth-8-ene-1,2-diol + NAD+ = 1-hydroxymenth-8-en-2-one + NADH + H+ (general reaction)
(1) (1S,2S,4R)-menth-8-ene-1,2-diol + NAD+ = (1S,4R)-1-hydroxymenth-8-en-2-one + NADH + H+
(2) (1R,2R,4S)-menth-8-ene-1,2-diol + NAD+ = (1R,4S)-1-hydroxymenth-8-en-2-one + NADH + H+
Glossary: limonene-1,2-diol = menth-8-ene-1,2-diol = 1-methyl-4-(prop-1-en-2-yl)cyclohexane-1,2-diol
Other name(s): NAD+-dependent limonene-1,2-diol dehydrogenase
Systematic name: menth-8-ene-1,2-diol:NAD+ oxidoreductase
Comments: While the enzyme from the Gram-positive bacterium Rhodococcus erythropolis DCL14 can use both (1S,2S,4R)- and (1R,2R,4S)-menth-8-ene-1,2-diol as substrate, activity is higher with (1S,2S,4R)-menth-8-ene-1,2-diol as substrate.
References:
1.  van der Werf, M.J., Swarts, H.J. and de Bont, J.A. Rhodococcus erythropolis DCL14 contains a novel degradation pathway for limonene. Appl. Environ. Microbiol. 65 (1999) 2092–2102. [PMID: 10224006]
[EC 1.1.1.297 created 2008]
 
 
EC 1.1.1.298     
Accepted name: 3-hydroxypropionate dehydrogenase (NADP+)
Reaction: 3-hydroxypropanoate + NADP+ = malonate semialdehyde + NADPH + H+
Glossary: 3-hydroxypropanoate = 3-hydroxypropionate
Other name(s): 3-hydroxypropanoate dehydrogenase (NADP+); 3-hydroxypropionate:NADP+ oxidoreductase
Systematic name: 3-hydroxypropanoate:NADP+ oxidoreductase
Comments: Catalyses the reduction of malonate semialdehyde to 3-hydroxypropanoate, a key step in the 3-hydroxypropanoate and the 3-hydroxypropanoate/4-hydroxybutanoate cycles, autotrophic CO2 fixation pathways found in some green non-sulfur phototrophic bacteria and archaea, respectively [1,2]. The enzyme from Chloroflexus aurantiacus is bifunctional, and also catalyses the upstream reaction in the pathway, EC 1.2.1.75 [3]. Different from EC 1.1.1.59 [3-hydroxypropionate dehydrogenase (NAD+)] by cofactor preference.
References:
1.  Strauss, G. and Fuchs, G. Enzymes of a novel autotrophic CO2 fixation pathway in the phototrophic bacterium Chloroflexus aurantiacus, the 3-hydroxypropionate cycle. Eur. J. Biochem. 215 (1993) 633–643. [PMID: 8354269]
2.  Berg, I.A., Kockelkorn, D., Buckel, W. and Fuchs, G. A 3-hydroxypropionate/4-hydroxybutyrate autotrophic carbon dioxide assimilation pathway in Archaea. Science 318 (2007) 1782–1786. [PMID: 18079405]
3.  Hugler, M., Menendez, C., Schagger, H. and Fuchs, G. Malonyl-coenzyme A reductase from Chloroflexus aurantiacus, a key enzyme of the 3-hydroxypropionate cycle for autotrophic CO2 fixation. J. Bacteriol. 184 (2002) 2404–2410. [PMID: 11948153]
[EC 1.1.1.298 created 2009]
 
 
EC 1.1.1.299     
Accepted name: malate dehydrogenase [NAD(P)+]
Reaction: (S)-malate + NAD(P)+ = oxaloacetate + NAD(P)H + H+
Other name(s): MdH II, NAD(P)+-dependent malate dehyrogenase
Systematic name: (S)-malate:NAD(P)+ oxidoreductase
Comments: This enzyme, which was characterized from the methanogenic archaeon Methanobacterium thermoautotrophicum, catalyses only the reduction of oxaloacetate, and can use NAD+ and NADP+ with similar specific activity [1]. Different from EC 1.1.1.37 (malate dehydrogenase (NAD+)), EC 1.1.1.82 (malate dehydrogenase (NADP+)) and EC 1.1.5.4 (malate dehydrogenase (quinone)).
References:
1.  Thompson, H., Tersteegen, A., Thauer, R.K. and Hedderich, R. Two malate dehydrogenases in Methanobacterium thermoautotrophicum. Arch. Microbiol. 170 (1998) 38–42. [PMID: 9639601]
[EC 1.1.1.299 created 2009]
 
 
EC 1.1.1.300     
Accepted name: NADP-retinol dehydrogenase
Reaction: retinol + NADP+ = retinal + NADPH + H+
Other name(s): all-trans retinal reductase (ambiguous); all-trans-retinol dehydrogenase; NADP(H)-dependent retinol dehydrogenase/reductase; RDH11; RDH12; RDH13; RDH14; retinol dehydrogenase 12; retinol dehydrogenase 14; retinol dehydrogenase [NADP+]; RalR1; PSDR1
Systematic name: retinol:NADP+ oxidoreductase
Comments: Greater catalytic efficiency in the reductive direction. This observation, and the enzyme’s localization at the entrance to the mitochondrial matrix, suggest that it may function to protect mitochondria against oxidative stress associated with the highly reactive retinal produced from dietary β-carotene by EC 1.13.11.63 (β-carotene 15,15′-dioxygenase) [2]. Km-values for NADP+ and NADPH are at least 800-fold lower than those for NAD+ and NADH [1,4]. This enzyme differs from EC 1.1.1.105, retinol dehydrogenase, which prefers NAD+ and NADH.
References:
1.  Belyaeva, O.V., Korkina, O.V., Stetsenko, A.V., Kim, T., Nelson, P.S. and Kedishvili, N.Y. Biochemical properties of purified human retinol dehydrogenase 12 (RDH12): catalytic efficiency toward retinoids and C9 aldehydes and effects of cellular retinol-binding protein type I (CRBPI) and cellular retinaldehyde-binding protein (CRALBP) on the oxidation and reduction of retinoids. Biochemistry 44 (2005) 7035–7047. [PMID: 15865448]
2.  Belyaeva, O.V., Korkina, O.V., Stetsenko, A.V. and Kedishvili, N.Y. Human retinol dehydrogenase 13 (RDH13) is a mitochondrial short-chain dehydrogenase/reductase with a retinaldehyde reductase activity. FEBS J. 275 (2008) 138–147. [PMID: 18039331]
3.  Haeseleer, F., Huang, J., Lebioda, L., Saari, J.C. and Palczewski, K. Molecular characterization of a novel short-chain dehydrogenase/reductase that reduces all-trans-retinal. J. Biol. Chem. 273 (1998) 21790–21799. [PMID: 9705317]
4.  Kedishvili, N.Y., Chumakova, O.V., Chetyrkin, S.V., Belyaeva, O.V., Lapshina, E.A., Lin, D.W., Matsumura, M. and Nelson, P.S. Evidence that the human gene for prostate short-chain dehydrogenase/reductase (PSDR1) encodes a novel retinal reductase (RalR1). J. Biol. Chem. 277 (2002) 28909–28915. [PMID: 12036956]
[EC 1.1.1.300 created 2009]
 
 
EC 1.1.1.301     
Accepted name: D-arabitol-phosphate dehydrogenase
Reaction: D-arabinitol 1-phosphate + NAD+ = D-xylulose 5-phosphate + NADH + H+
Other name(s): APDH; D-arabitol 1-phosphate dehydrogenase; D-arabitol 5-phosphate dehydrogenase; D-arabinitol 1-phosphate dehydrogenase; D-arabinitol 5-phosphate dehydrogenase
Systematic name: D-arabinitol-phosphate:NAD+ oxidoreductase
Comments: This enzyme participates in arabinitol catabolism. The enzyme also converts D-arabinitol 5-phosphate to D-ribulose 5-phosphate at a lower rate [1].
References:
1.  Povelainen, M., Eneyskaya, E.V., Kulminskaya, A.A., Ivanen, D.R., Kalkkinen, N., Neustroev, K.N. and Miasnikov, A.N. Biochemical and genetic characterization of a novel enzyme of pentitol metabolism: D-arabitol-phosphate dehydrogenase. Biochem. J. 371 (2003) 191–197. [PMID: 12467497]
[EC 1.1.1.301 created 2010]
 
 
EC 1.1.1.302     
Accepted name: 2,5-diamino-6-(ribosylamino)-4(3H)-pyrimidinone 5′-phosphate reductase
Reaction: 2,5-diamino-6-(5-phospho-D-ribitylamino)pyrimidin-4(3H)-one + NAD(P)+ = 2,5-diamino-6-(5-phospho-D-ribosylamino)pyrimidin-4(3H)-one + NAD(P)H + H+
Other name(s): 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5′-phosphate reductase; MjaRED; MJ0671 (gene name)
Systematic name: 2,5-diamino-6-(5-phospho-D-ribosylamino)pyrimidin-4(3H)-one:NAD(P)+ oxidoreductase
Comments: The reaction proceeds in the opposite direction. A step in riboflavin biosynthesis, NADPH and NADH function equally well as reductant. Differs from EC 1.1.1.193 [5-amino-6-(5-phosphoribosylamino)uracil reductase] since it does not catalyse the reduction of 5-amino-6-ribosylaminopyrimidine-2,4(1H,3H)-dione 5′-phosphate [1].
References:
1.  Graupner, M., Xu, H. and White, R.H. The pyrimidine nucleotide reductase step in riboflavin and F420 biosynthesis in archaea proceeds by the eukaryotic route to riboflavin. J. Bacteriol. 184 (2002) 1952–1957. [PMID: 11889103]
2.  Chatwell, L., Krojer, T., Fidler, A., Romisch, W., Eisenreich, W., Bacher, A., Huber, R. and Fischer, M. Biosynthesis of riboflavin: structure and properties of 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5′-phosphate reductase of Methanocaldococcus jannaschii. J. Mol. Biol. 359 (2006) 1334–1351. [PMID: 16730025]
[EC 1.1.1.302 created 2010, modified 2011]
 
 
EC 1.1.1.303     
Accepted name: diacetyl reductase [(R)-acetoin forming]
Reaction: (R)-acetoin + NAD+ = diacetyl + NADH + H+
Other name(s): (R)-acetoin dehydrogenase
Systematic name: (R)-acetoin:NAD+ oxidoreductase
Comments: The reaction is catalysed in the reverse direction. This activity is usually associated with butanediol dehydrogenase activity (EC 1.1.1.4 or EC 1.1.1.76). While the butanediol dehydrogenase activity is reversible, diacetyl reductase activity is irreversible. This enzyme has been reported in the yeast Saccharomyces cerevisiae [1,2]. Different from EC 1.1.1.304, diacetyl reductase [(S)-acetoin forming].
References:
1.  Heidlas, J. and Tressl, R. Purification and characterization of a (R)-2,3-butanediol dehydrogenase from Saccharomyces cerevisiae. Arch. Microbiol. 154 (1990) 267–273. [PMID: 2222122]
2.  Gonzalez, E., Fernandez, M.R., Larroy, C., Sola, L., Pericas, M.A., Pares, X. and Biosca, J.A. Characterization of a (2R,3R)-2,3-butanediol dehydrogenase as the Saccharomyces cerevisiae YAL060W gene product. Disruption and induction of the gene. J. Biol. Chem. 275 (2000) 35876–35885. [PMID: 10938079]
[EC 1.1.1.303 created 2010 (EC 1.1.1.5 created 1961, modified 1976, part incorporated 2010)]
 
 
EC 1.1.1.304     
Accepted name: diacetyl reductase [(S)-acetoin forming]
Reaction: (S)-acetoin + NAD+ = diacetyl + NADH + H+
Other name(s): (S)-acetoin dehydrogenase
Systematic name: (S)-acetoin:NAD+ oxidoreductase
Comments: The reaction is catalysed in the reverse direction. This activity is usually associated with butanediol dehydrogenase activity (EC 1.1.1.4 or EC 1.1.1.76). While the butanediol dehydrogenase activity is reversible, diacetyl reductase activity is irreversible. This enzyme has been reported in the bacteria Geobacillus stearothermophilus, Enterobacter aerogenes and Klebsiella pneumoniae [1-3]. Different from EC 1.1.1.303, diacetyl reductase [(R)-acetoin forming].
References:
1.  Giovannini, P.P., Medici, A., Bergamini, C.M. and Rippa, M. Properties of diacetyl (acetoin) reductase from Bacillus stearothermophilus. Bioorg. Med. Chem. 4 (1996) 1197–1201. [PMID: 8879540]
2.  Carballo, J., Martin, R., Bernardo, A. and Gonzalez, J. Purification, characterization and some properties of diacetyl(acetoin) reductase from Enterobacter aerogenes. Eur. J. Biochem. 198 (1991) 327–332. [PMID: 2040298]
3.  Ui, S., Okajima, Y., Mimura, A., Kanai, H., Kobayashi, T., Kudo, T. Sequence analysis of the gene for and characterization of D-acetoin forming meso-2,3-butanediol dehydrogenase of Klebsiella pneumoniae expressed in Escherichia coli. J. Ferment. Bioeng. 83 (1997) 32–37.
[EC 1.1.1.304 created 2010 (EC 1.1.1.5 created 1961, modified 1976, part incorporated 2010)]
 
 
EC 1.1.1.305     
Accepted name: UDP-glucuronic acid dehydrogenase (UDP-4-keto-hexauronic acid decarboxylating)
Reaction: UDP-α-D-glucuronate + NAD+ = UDP-β-L-threo-pentapyranos-4-ulose + CO2 + NADH + H+
Other name(s): UDP-GlcUA decarboxylase; ArnADH; UDP-glucuronate:NAD+ oxidoreductase (decarboxylating)
Systematic name: UDP-α-D-glucuronate:NAD+ oxidoreductase (decarboxylating)
Comments: The activity is part of a bifunctional enzyme also performing the reaction of EC 2.1.2.13 (UDP-4-amino-4-deoxy-L-arabinose formyltransferase).
References:
1.  Breazeale, S.D., Ribeiro, A.A., McClerren, A.L. and Raetz, C.R.H. A formyltransferase required for polymyxin resistance in Escherichia coli and the modification of lipid A with 4-amino-4-deoxy-L-arabinose. Identification and function of UDP-4-deoxy-4-formamido-L-arabinose. J. Biol. Chem. 280 (2005) 14154–14167. [PMID: 15695810]
2.  Gatzeva-Topalova, P.Z., May, A.P. and Sousa, M.C. Crystal structure of Escherichia coli ArnA (PmrI) decarboxylase domain. A key enzyme for lipid A modification with 4-amino-4-deoxy-L-arabinose and polymyxin resistance. Biochemistry 43 (2004) 13370–13379. [PMID: 15491143]
3.  Williams, G.J., Breazeale, S.D., Raetz, C.R.H. and Naismith, J.H. Structure and function of both domains of ArnA, a dual function decarboxylase and a formyltransferase, involved in 4-amino-4-deoxy-L-arabinose biosynthesis. J. Biol. Chem. 280 (2005) 23000–23008. [PMID: 15809294]
4.  Gatzeva-Topalova, P.Z., May, A.P. and Sousa, M.C. Structure and mechanism of ArnA: conformational change implies ordered dehydrogenase mechanism in key enzyme for polymyxin resistance. Structure 13 (2005) 929–942. [PMID: 15939024]
5.  Yan, A., Guan, Z. and Raetz, C.R.H. An undecaprenyl phosphate-aminoarabinose flippase required for polymyxin resistance in Escherichia coli. J. Biol. Chem. 282 (2007) 36077–36089. [PMID: 17928292]
[EC 1.1.1.305 created 2010]
 
 
EC 1.1.1.306     
Accepted name: S-(hydroxymethyl)mycothiol dehydrogenase
Reaction: S-(hydroxymethyl)mycothiol + NAD+ = S-formylmycothiol + NADH + H+
Glossary: mycothiol = 1-O-[2-(N2-acetyl-L-cysteinamido)-2-deoxy-α-D-glucopyranosyl]-1D-myo-inositol
Other name(s): NAD/factor-dependent formaldehyde dehydrogenase; mycothiol-dependent formaldehyde dehydrogenase
Systematic name: S-(hydroxymethyl)mycothiol:NAD+ oxidoreductase
Comments: S-hydroxymethylmycothiol is believed to form spontaneously from formaldehyde and mycothiol. This enzyme oxidizes the product of this spontaneous reaction to S-formylmycothiol, in a reaction that is analogous to EC 1.1.1.284, S-(hydroxymethyl)glutathione dehydrogenase.
References:
1.  Misset-Smits, M., Van Ophem, P.W., Sakuda, S. and Duine, J.A. Mycothiol, 1-O-(2′-[N-acetyl-L-cysteinyl]amido-2′-deoxy-α-D-glucopyranosyl)-D-myo-inositol, is the factor of NAD/factor-dependent formaldehyde dehydrogenase. FEBS Lett. 409 (1997) 221–222. [PMID: 9202149]
2.  Norin, A., Van Ophem, P.W., Piersma, S.R., Person, B., Duine, J.A. and Jornvall, H. Mycothiol-dependent formaldehyde dehydrogenase, a prokaryotic medium-chain dehydrogenase/reductase, phylogenetically links different eukaryotic alcohol dehydrogenase's - primary structure, conformational modelling and functional correlations. Eur. J. Biochem. 248 (1997) 282–289. [PMID: 9346279]
3.  Vogt, R.N., Steenkamp, D.J., Zheng, R. and Blanchard, J.S. The metabolism of nitrosothiols in the Mycobacteria: identification and characterization of S-nitrosomycothiol reductase. Biochem. J. 374 (2003) 657–666. [PMID: 12809551]
4.  Rawat, M. and Av-Gay, Y. Mycothiol-dependent proteins in actinomycetes. FEMS Microbiol. Rev. 31 (2007) 278–292. [PMID: 17286835]
[EC 1.1.1.306 created 2010 as EC 1.2.1.66, transferred 2010 to EC 1.1.1.306]
 
 
EC 1.1.1.307     
Accepted name: D-xylose reductase
Reaction: xylitol + NAD(P)+ = D-xylose + NAD(P)H + H+
Other name(s): XylR; XyrA; msXR; dsXR; monospecific xylose reductase; dual specific xylose reductase; NAD(P)H-dependent xylose reductase; xylose reductase
Systematic name: xylitol:NAD(P)+ oxidoreductase
Comments: Xylose reductase catalyses the initial reaction in the xylose utilization pathway, the NAD(P)H dependent reduction of xylose to xylitol.
References:
1.  Neuhauser, W., Haltrich, D., Kulbe, K.D. and Nidetzky, B. NAD(P)H-dependent aldose reductase from the xylose-assimilating yeast Candida tenuis. Isolation, characterization and biochemical properties of the enzyme. Biochem. J. 326 (1997) 683–692. [PMID: 9307017]
2.  Nidetzky, B., Bruggler, K., Kratzer, R. and Mayr, P. Multiple forms of xylose reductase in Candida intermedia: comparison of their functional properties using quantitative structure-activity relationships, steady-state kinetic analysis, and pH studies. J. Agric. Food Chem. 51 (2003) 7930–7935. [PMID: 14690376]
3.  Iablochkova, E.N., Bolotnikova, O.I., Mikhailova, N.P., Nemova, N.N. and Ginak, A.I. The activity of xylose reductase and xylitol dehydrogenase in yeasts. Mikrobiologiia 72 (2003) 466–469. [PMID: 14526534] (in Russian)
4.  Chen, L.C., Huang, S.C., Chuankhayan, P., Chen, C.D., Huang, Y.C., Jeyakanthan, J., Pang, H.F., Men, L.C., Chen, Y.C., Wang, Y.K., Liu, M.Y., Wu, T.K. and Chen, C.J. Purification, crystallization and preliminary X-ray crystallographic analysis of xylose reductase from Candida tropicalis. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 65 (2009) 419–421. [PMID: 19342796]
5.  Verduyn, C., Van Kleef, R., Frank, J., Schreuder, H., Van Dijken, J.P. and Scheffers, W.A. Properties of the NAD(P)H-dependent xylose reductase from the xylose-fermenting yeast Pichia stipitis. Biochem. J. 226 (1985) 669–677. [PMID: 3921014]
6.  Fernandes, S., Tuohy, M.G. and Murray, P.G. Xylose reductase from the thermophilic fungus Talaromyces emersonii: cloning and heterologous expression of the native gene (Texr) and a double mutant (TexrK271R + N273D) with altered coenzyme specificity. J. Biosci. 34 (2009) 881–890. [PMID: 20093741]
7.  Lee, J.K., Koo, B.S. and Kim, S.Y. Cloning and characterization of the xyl1 gene, encoding an NADH-preferring xylose reductase from Candida parapsilosis, and its functional expression in Candida tropicalis. Appl. Environ. Microbiol. 69 (2003) 6179–6188. [PMID: 14532079]
8.  Woodyer, R., Simurdiak, M., van der Donk, W.A. and Zhao, H. Heterologous expression, purification, and characterization of a highly active xylose reductase from Neurospora crassa. Appl. Environ. Microbiol. 71 (2005) 1642–1647. [PMID: 15746370]
[EC 1.1.1.307 created 2010]
 
 
EC 1.1.1.308     
Accepted name: sulfopropanediol 3-dehydrogenase
Reaction: (R)-2,3-dihydroxypropane-1-sulfonate + 2 NAD+ + H2O = (R)-3-sulfolactate + 2 NADH + 2 H+
Other name(s): DHPS 3-dehydrogenase (sulfolactate forming); 2,3-dihydroxypropane-1-sulfonate 3-dehydrogenase (sulfolactate forming); dihydroxypropanesulfonate 3-dehydrogenase; hpsN (gene name)
Systematic name: (R)-2,3-dihydroxypropane-1-sulfonate:NAD+ 3-oxidoreductase
Comments: The enzyme is involved in degradation of (R)-2,3-dihydroxypropanesulfonate.
References:
1.  Mayer, J., Huhn, T., Habeck, M., Denger, K., Hollemeyer, K. and Cook, A.M. 2,3-Dihydroxypropane-1-sulfonate degraded by Cupriavidus pinatubonensis JMP134: purification of dihydroxypropanesulfonate 3-dehydrogenase. Microbiology 156 (2010) 1556–1564. [PMID: 20150239]
[EC 1.1.1.308 created 2011]
 
 
EC 1.1.1.309     
Accepted name: phosphonoacetaldehyde reductase (NADH)
Reaction: 2-hydroxyethylphosphonate + NAD+ = phosphonoacetaldehyde + NADH + H+
Other name(s): PhpC
Systematic name: 2-hydroxyethylphosphonate:NAD+ oxidoreductase
Comments: The enzyme from Streptomyces viridochromogenes catalyses a step in the biosynthesis of phosphinothricin tripeptide, the reduction of phosphonoacetaldehyde to 2-hydroxyethylphosphonate. The preferred cofactor is NADH, lower activity with NADPH [1].
References:
1.  Blodgett, J.A., Thomas, P.M., Li, G., Velasquez, J.E., van der Donk, W.A., Kelleher, N.L. and Metcalf, W.W. Unusual transformations in the biosynthesis of the antibiotic phosphinothricin tripeptide. Nat. Chem. Biol. 3 (2007) 480–485. [PMID: 17632514]
[EC 1.1.1.309 created 2011]
 
 
EC 1.1.1.310     
Accepted name: (S)-sulfolactate dehydrogenase
Reaction: (2S)-3-sulfolactate + NAD+ = 3-sulfopyruvate + NADH + H+
Other name(s): (2S)-3-sulfolactate dehydrogenase; SlcC
Systematic name: (2S)-sulfolactate:NAD+ oxidoreductase
Comments: This enzyme, isolated from the bacterium Chromohalobacter salexigens DSM 3043, acts only on the (S)-enantiomer of 3-sulfolactate. Combined with EC 1.1.1.338, (2R)-3-sulfolactate dehydrogenase (NADP+), it provides a racemase system that converts (2S)-3-sulfolactate to (2R)-3-sulfolactate, which is degraded further by EC 4.4.1.24, (2R)-sulfolactate sulfo-lyase. The enzyme is specific for NAD+.
References:
1.  Denger, K. and Cook, A.M. Racemase activity effected by two dehydrogenases in sulfolactate degradation by Chromohalobacter salexigens: purification of (S)-sulfolactate dehydrogenase. Microbiology 156 (2010) 967–974. [PMID: 20007648]
[EC 1.1.1.310 created 2011, modified 2013]
 
 
EC 1.1.1.311     
Accepted name: (S)-1-phenylethanol dehydrogenase
Reaction: (S)-1-phenylethanol + NAD+ = acetophenone + NADH + H+
Other name(s): PED
Systematic name: (S)-1-phenylethanol:NAD+ oxidoreductase
Comments: The enzyme is involved in degradation of ethylbenzene.
References:
1.  Kniemeyer, O. and Heider, J. (S)-1-phenylethanol dehydrogenase of Azoarcus sp. strain EbN1, an enzyme of anaerobic ethylbenzene catabolism. Arch. Microbiol. 176 (2001) 129–135. [PMID: 11479712]
2.  Hoffken, H.W., Duong, M., Friedrich, T., Breuer, M., Hauer, B., Reinhardt, R., Rabus, R. and Heider, J. Crystal structure and enzyme kinetics of the (S)-specific 1-phenylethanol dehydrogenase of the denitrifying bacterium strain EbN1. Biochemistry 45 (2006) 82–93. [PMID: 16388583]
[EC 1.1.1.311 created 2011]
 
 
EC 1.1.1.312     
Accepted name: 2-hydroxy-4-carboxymuconate semialdehyde hemiacetal dehydrogenase
Reaction: 4-carboxy-2-hydroxymuconate semialdehyde hemiacetal + NADP+ = 2-oxo-2H-pyran-4,6-dicarboxylate + NADPH + H+
Other name(s): 2-hydroxy-4-carboxymuconate 6-semialdehyde dehydrogenase; 4-carboxy-2-hydroxy-cis,cis-muconate-6-semialdehyde:NADP+ oxidoreductase; α-hydroxy-γ-carboxymuconic ε-semialdehyde dehydrogenase; 4-carboxy-2-hydroxymuconate-6-semialdehyde dehydrogenase; LigC; ProD
Systematic name: 4-carboxy-2-hydroxymuconate semialdehyde hemiacetal:NADP+ 2-oxidoreductase
Comments: The enzyme does not act on unsubstituted aliphatic or aromatic aldehydes or glucose; NAD+ can replace NADP+, but with lower affinity. The enzyme was initially believed to act on 4-carboxy-2-hydroxy-cis,cis-muconate 6-semialdehyde and produce 4-carboxy-2-hydroxy-cis,cis-muconate [1]. However, later studies showed that the substrate is the hemiacetal form [3], and the product is 2-oxo-2H-pyran-4,6-dicarboxylate [2,4].
References:
1.  Maruyama, K., Ariga, N., Tsuda, M. and Deguchi, K. Purification and properties of α-hydroxy-γ-carboxymuconic ε-semialdehyde dehydrogenase. J. Biochem. (Tokyo) 83 (1978) 1125–1134. [PMID: 26671]
2.  Maruyama, K. Isolation and identification of the reaction product of α-hydroxy-γ-carboxymuconic ε-semialdehyde dehydrogenase. J. Biochem. 86 (1979) 1671–1677. [PMID: 528534]
3.  Maruyama, K. Purification and properties of 2-pyrone-4,6-dicarboxylate hydrolase. J. Biochem. (Tokyo) 93 (1983) 557–565. [PMID: 6841353]
4.  Masai, E., Momose, K., Hara, H., Nishikawa, S., Katayama, Y. and Fukuda, M. Genetic and biochemical characterization of 4-carboxy-2-hydroxymuconate-6-semialdehyde dehydrogenase and its role in the protocatechuate 4,5-cleavage pathway in Sphingomonas paucimobilis SYK-6. J. Bacteriol. 182 (2000) 6651–6658. [PMID: 11073908]
[EC 1.1.1.312 created 1978 as EC 1.2.1.45, transferred 2011 to EC 1.1.1.312]
 
 
EC 1.1.1.313     
Accepted name: sulfoacetaldehyde reductase
Reaction: isethionate + NADP+ = 2-sulfoacetaldehyde + NADPH + H+
Glossary: isethionate = 2-hydroxyethanesulfonate
2-sulfoacetaldehyde = 2-oxoethanesulfonate
Other name(s): isfD (gene name)
Systematic name: isethionate:NADP+ oxidoreductase
Comments: Catalyses the reaction only in the opposite direction. Involved in taurine degradation. The bacterium Chromohalobacter salexigens strain DSM 3043 possesses two enzymes that catalyse this reaction, a constitutive enzyme (encoded by isfD2) and an inducible enzyme (encoded by isfD). The latter is induced by taurine, and is responsible for most of the activity observed in taurine-grown cells.
References:
1.  Krejcik, Z., Hollemeyer, K., Smits, T.H. and Cook, A.M. Isethionate formation from taurine in Chromohalobacter salexigens: purification of sulfoacetaldehyde reductase. Microbiology 156 (2010) 1547–1555. [PMID: 20133363]
[EC 1.1.1.313 created 2011]
 
 
EC 1.1.1.314      
Deleted entry: germacrene A alcohol dehydrogenase. Now known to be catalyzed by EC 1.14.14.95, germacrene A hydroxylase
[EC 1.1.1.314 created 2011, deleted 2018]
 
 
EC 1.1.1.315     
Accepted name: 11-cis-retinol dehydrogenase
Reaction: 11-cis-retinol—[retinal-binding-protein] + NAD+ = 11-cis-retinal—[retinol-binding-protein] + NADH + H+
Glossary: 11-cis-retinal = 11-cis-retinaldehyde
Other name(s): RDH5 (gene name)
Systematic name: 11-cis-retinol:NAD+ oxidoreductase
Comments: This enzyme, abundant in the retinal pigment epithelium, catalyses the reduction of 11-cis-retinol to 11-cis-retinal [1] while the substrate is bound to the retinal-binding protein [4]. This is a crucial step in the regeneration of 11-cis-retinal, the chromophore of rhodopsin. The enzyme can also accept other cis forms of retinol [2].
References:
1.  Simon, A., Hellman, U., Wernstedt, C. and Eriksson, U. The retinal pigment epithelial-specific 11-cis retinol dehydrogenase belongs to the family of short chain alcohol dehydrogenases. J. Biol. Chem. 270 (1995) 1107–1112. [PMID: 7836368]
2.  Wang, J., Chai, X., Eriksson, U. and Napoli, J.L. Activity of human 11-cis-retinol dehydrogenase (Rdh5) with steroids and retinoids and expression of its mRNA in extra-ocular human tissue. Biochem. J. 338 (1999) 23–27. [PMID: 9931293]
3.  Liden, M., Romert, A., Tryggvason, K., Persson, B. and Eriksson, U. Biochemical defects in 11-cis-retinol dehydrogenase mutants associated with fundus albipunctatus. J. Biol. Chem. 276 (2001) 49251–49257. [PMID: 11675386]
4.  Wu, Z., Yang, Y., Shaw, N., Bhattacharya, S., Yan, L., West, K., Roth, K., Noy, N., Qin, J. and Crabb, J.W. Mapping the ligand binding pocket in the cellular retinaldehyde binding protein. J. Biol. Chem. 278 (2003) 12390–12396. [PMID: 12536149]
[EC 1.1.1.315 created 2011]
 
 
EC 1.1.1.316     
Accepted name: L-galactose 1-dehydrogenase
Reaction: L-galactose + NAD+ = L-galactono-1,4-lactone + NADH + H+
Other name(s): L-GalDH; L-galactose dehydrogenase
Systematic name: L-galactose:NAD+ 1-oxidoreductase
Comments: The enzyme catalyses a step in the ascorbate biosynthesis in higher plants (Smirnoff-Wheeler pathway). The activity with NADP+ is less than 10% of the activity with NAD+.
References:
1.  Mieda, T., Yabuta, Y., Rapolu, M., Motoki, T., Takeda, T., Yoshimura, K., Ishikawa, T. and Shigeoka, S. Feedback inhibition of spinach L-galactose dehydrogenase by L-ascorbate. Plant Cell Physiol. 45 (2004) 1271–1279. [PMID: 15509850]
2.  Gatzek, S., Wheeler, G.L. and Smirnoff, N. Antisense suppression of L-galactose dehydrogenase in Arabidopsis thaliana provides evidence for its role in ascorbate synthesis and reveals light modulated L-galactose synthesis. Plant J. 30 (2002) 541–553. [PMID: 12047629]
3.  Wheeler, G.L., Jones, M.A. and Smirnoff, N. The biosynthetic pathway of vitamin C in higher plants. Nature 393 (1998) 365–369. [PMID: 9620799]
4.  Oh, M.M., Carey, E.E. and Rajashekar, C.B. Environmental stresses induce health-promoting phytochemicals in lettuce. Plant Physiol. Biochem. 47 (2009) 578–583. [PMID: 19297184]
[EC 1.1.1.316 created 2011]
 
 
EC 1.1.1.317     
Accepted name: perakine reductase
Reaction: raucaffrinoline + NADP+ = perakine + NADPH + H+
Glossary: raucaffrinoline = (17R,20α,21β)-1,2-didehydro-1-demethyl-19-hydroxy-21-methyl-18-norajmalan-17-yl acetate
perakine = raucaffrine = (17R,20α,21β)-1,2-didehydro-1-demethyl-17-(acetyloxy)-21-methyl-18-norajmalan-19-al
Systematic name: raucaffrinoline:NADP+ oxidoreductase
Comments: The biosynthesis of raucaffrinoline from perakine is a side route of the ajmaline biosynthesis pathway. The enzyme is a member of the aldo-keto reductase enzyme superfamily from higher plants.
References:
1.  Sun, L., Ruppert, M., Sheludko, Y., Warzecha, H., Zhao, Y. and Stockigt, J. Purification, cloning, functional expression and characterization of perakine reductase: the first example from the AKR enzyme family, extending the alkaloidal network of the plant Rauvolfia. Plant Mol. Biol. 67 (2008) 455–467. [PMID: 18409028]
2.  Rosenthal, C., Mueller, U., Panjikar, S., Sun, L., Ruppert, M., Zhao, Y. and Stockigt, J. Expression, purification, crystallization and preliminary X-ray analysis of perakine reductase, a new member of the aldo-keto reductase enzyme superfamily from higher plants. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 62 (2006) 1286–1289. [PMID: 17142919]
[EC 1.1.1.317 created 2011]
 
 
EC 1.1.1.318     
Accepted name: eugenol synthase
Reaction: eugenol + a carboxylate + NADP+ = a coniferyl ester + NADPH + H+
Other name(s): LtCES1; EGS1; EGS2
Systematic name: eugenol:NADP+ oxidoreductase (coniferyl ester reducing)
Comments: The enzyme acts in the opposite direction. The enzymes from the plants Ocimum basilicum (sweet basil) [1,3], Clarkia breweri and Petunia hybrida [4] only accept coniferyl acetate and form eugenol. The enzyme from Pimpinella anisum (anise) forms anol (from 4-coumaryl acetate) in vivo, although the recombinant enzyme can form eugenol from coniferyl acetate [5]. The enzyme from Larrea tridentata (creosote bush) also forms chavicol from a coumaryl ester and can use NADH [2].
References:
1.  Koeduka, T., Fridman, E., Gang, D.R., Vassão, D.G., Jackson, B.L., Kish, C.M., Orlova, I., Spassova, S.M., Lewis, N.G., Noel, J.P., Baiga, T.J., Dudareva, N. and Pichersky, E. Eugenol and isoeugenol, characteristic aromatic constituents of spices, are biosynthesized via reduction of a coniferyl alcohol ester. Proc. Natl. Acad. Sci. USA 103 (2006) 10128–10133. [PMID: 16782809]
2.  Vassão, D.G., Kim, S.J., Milhollan, J.K., Eichinger, D., Davin, L.B. and Lewis, N.G. A pinoresinol-lariciresinol reductase homologue from the creosote bush (Larrea tridentata) catalyzes the efficient in vitro conversion of p-coumaryl/coniferyl alcohol esters into the allylphenols chavicol/eugenol, but not the propenylphenols p-anol/isoeugenol. Arch. Biochem. Biophys. 465 (2007) 209–218. [PMID: 17624297]
3.  Louie, G.V., Baiga, T.J., Bowman, M.E., Koeduka, T., Taylor, J.H., Spassova, S.M., Pichersky, E. and Noel, J.P. Structure and reaction mechanism of basil eugenol synthase. PLoS One 2 (2007) e993. [PMID: 17912370]
4.  Koeduka, T., Louie, G.V., Orlova, I., Kish, C.M., Ibdah, M., Wilkerson, C.G., Bowman, M.E., Baiga, T.J., Noel, J.P., Dudareva, N. and Pichersky, E. The multiple phenylpropene synthases in both Clarkia breweri and Petunia hybrida represent two distinct protein lineages. Plant J. 54 (2008) 362–374. [PMID: 18208524]
5.  Koeduka, T., Baiga, T.J., Noel, J.P. and Pichersky, E. Biosynthesis of t-anethole in anise: characterization of t-anol/isoeugenol synthase and an O-methyltransferase specific for a C7-C8 propenyl side chain. Plant Physiol. 149 (2009) 384–394. [PMID: 18987218]
[EC 1.1.1.318 created 2012]
 
 
EC 1.1.1.319     
Accepted name: isoeugenol synthase
Reaction: isoeugenol + acetate + NADP+ = coniferyl acetate + NADPH + H+
Other name(s): IGS1; t-anol/isoeugenol synthase 1
Systematic name: eugenol:NADP+ oxidoreductase (coniferyl acetate reducing)
Comments: The enzyme acts in the opposite direction. In Ocimum basilicum (sweet basil), Clarkia breweri and Petunia hybrida only isoeugenol is formed [1,2]. However in Pimpinella anisum (anise) only anol is formed in vivo, although the cloned enzyme does produce isoeugenol [3].
References:
1.  Koeduka, T., Fridman, E., Gang, D.R., Vassão, D.G., Jackson, B.L., Kish, C.M., Orlova, I., Spassova, S.M., Lewis, N.G., Noel, J.P., Baiga, T.J., Dudareva, N. and Pichersky, E. Eugenol and isoeugenol, characteristic aromatic constituents of spices, are biosynthesized via reduction of a coniferyl alcohol ester. Proc. Natl. Acad. Sci. USA 103 (2006) 10128–10133. [PMID: 16782809]
2.  Koeduka, T., Louie, G.V., Orlova, I., Kish, C.M., Ibdah, M., Wilkerson, C.G., Bowman, M.E., Baiga, T.J., Noel, J.P., Dudareva, N. and Pichersky, E. The multiple phenylpropene synthases in both Clarkia breweri and Petunia hybrida represent two distinct protein lineages. Plant J. 54 (2008) 362–374. [PMID: 18208524]
3.  Koeduka, T., Baiga, T.J., Noel, J.P. and Pichersky, E. Biosynthesis of t-anethole in anise: characterization of t-anol/isoeugenol synthase and an O-methyltransferase specific for a C7-C8 propenyl side chain. Plant Physiol. 149 (2009) 384–394. [PMID: 18987218]
[EC 1.1.1.319 created 2012]
 
 
EC 1.1.1.320     
Accepted name: benzil reductase [(S)-benzoin forming]
Reaction: (S)-benzoin + NADP+ = benzil + NADPH + H+
Glossary: (S)-benzoin = (2S)-2-hydroxy-1,2-diphenylethanone
benzil = 1,2-diphenylethane-1,2-dione
Other name(s): YueD
Systematic name: (S)-benzoin:NADP+ oxidoreductase
Comments: The enzyme also reduces 1-phenylpropane-1,2-dione. The enzyme from Bacillus cereus in addition reduces 1,4-naphthoquinone and 1-(4-methylphenyl)-2-phenylethane-1,2-dione with high efficiency [2].
References:
1.  Maruyama, R., Nishizawa, M., Itoi, Y., Ito, S. and Inoue, M. Isolation and expression of a Bacillus cereus gene encoding benzil reductase. Biotechnol. Bioeng. 75 (2001) 630–633. [PMID: 11745140]
2.  Maruyama, R., Nishizawa, M., Itoi, Y., Ito, S. and Inoue, M. The enzymes with benzil reductase activity conserved from bacteria to mammals. J. Biotechnol. 94 (2002) 157–169. [PMID: 11796169]
[EC 1.1.1.320 created 2012]
 
 
EC 1.1.1.321     
Accepted name: benzil reductase [(R)-benzoin forming]
Reaction: (R)-benzoin + NADP+ = benzil + NADPH + H+
Glossary: (R)-benzoin = (2R)-2-hydroxy-1,2-diphenylethanone
benzil = 1,2-diphenylethane-1,2-dione
Systematic name: (R)-benzoin:NADP+ oxidoreductase
Comments: The enzyme from the bacterium Xanthomonas oryzae is able to reduce enantioselectively only one of the two carbonyl groups of benzil to give optically active (R)-benzoin.
References:
1.  Konishi, J., Ohta, H. and Tuchihashi, G. Asymmetric reduction of benzil to benzoin catalyzed by the enzyme system of a microorganism. Chem. Lett. 14 (1985) 1111–1112.
[EC 1.1.1.321 created 2012]
 
 
EC 1.1.1.322     
Accepted name: (–)-endo-fenchol dehydrogenase
Reaction: (–)-endo-fenchol + NAD(P)+ = (+)-fenchone + NAD(P)H + H+
Other name(s): l-endo-fenchol dehydrogenase; FDH
Systematic name: (–)-endo-fenchol:NAD(P)+ oxidoreductase
Comments: Isolated from the plant Foeniculum vulgare (fennel). NADH is slightly preferred to NADPH.
References:
1.  Croteau, R. and Felton, N.M. Substrate specificity of monoterpenol dehydrogenases from Foeniculum vulgare and Tanacetum vulgare. Phytochemistry 19 (1980) 1343–1347.
[EC 1.1.1.322 created 2012]
 
 
EC 1.1.1.323     
Accepted name: (+)-thujan-3-ol dehydrogenase
Reaction: (+)-thujan-3-ol + NAD(P)+ = (+)-thujan-3-one + NAD(P)H + H+
Other name(s): d-3-thujanol dehydrogenase; TDH
Systematic name: (+)-thujan-3-ol:NAD(P)+ oxidoreductase
Comments: Isolated from the plant Tanacetum vulgare (tansy). NADH is preferred to NADPH.
References:
1.  Croteau, R. and Felton, N.M. Substrate specificity of monoterpenol dehydrogenases from Foeniculum vulgare and Tanacetum vulgare. Phytochemistry 19 (1980) 1343–1347.
[EC 1.1.1.323 created 2012]
 
 
EC 1.1.1.324     
Accepted name: 8-hydroxygeraniol dehydrogenase
Reaction: (6E)-8-hydroxygeraniol + 2 NADP+ = (6E)-8-oxogeranial + 2 NADPH + 2 H+ (overall reaction)
(1a) (6E)-8-hydroxygeraniol + NADP+ = (6E)-8-hydroxygeranial + NADPH + H+
(1b) (6E)-8-hydroxygeraniol + NADP+ = (6E)-8-oxogeraniol + NADPH + H+
(1c) (6E)-8-hydroxygeranial + NADP+ = (6E)-8-oxogeranial + NADPH + H+
(1d) (6E)-8-oxogeraniol + NADP+ = (6E)-8-oxogeranial + NADPH + H+
Other name(s): 8-hydroxygeraniol oxidoreductase; CYP76B10; G10H; CrG10H; SmG10H; acyclic monoterpene primary alcohol:NADP+ oxidoreductase
Systematic name: (6E)-8-hydroxygeraniol:NADP+ oxidoreductase
Comments: Contains Zn2+. The enzyme catalyses the oxidation of (6E)-8-hydroxygeraniol to (6E)-8-oxogeranial via either (6E)-8-hydroxygeranial or (6E)-8-oxogeraniol. Also acts on geraniol, nerol and citronellol. May be identical to EC 1.1.1.183 geraniol dehydrogenase. The recommended numbering of geraniol gives 8-hydroxygeraniol as the substrate rather than 10-hydroxygeraniol as used by references 1 and 2. See prenol nomenclature Pr-1.
References:
1.  Ikeda, H., Esaki, N., Nakai, S., Hashimoto, K., Uesato, S., Soda, K. and Fujita, T. Acyclic monoterpene primary alcohol:NADP+ oxidoreductase of Rauwolfia serpentina cells: the key enzyme in biosynthesis of monoterpene alcohols. J. Biochem. 109 (1991) 341–347. [PMID: 1864846]
2.  Hallahan, D.L., West, J.M., Wallsgrove, R.M., Smiley, D.W., Dawson, G.W., Pickett, J.A. and Hamilton, J.G. Purification and characterization of an acyclic monoterpene primary alcohol:NADP+ oxidoreductase from catmint (Nepeta racemosa). Arch. Biochem. Biophys. 318 (1995) 105–112. [PMID: 7726550]
[EC 1.1.1.324 created 2012]
 
 
EC 1.1.1.325     
Accepted name: sepiapterin reductase (L-threo-7,8-dihydrobiopterin forming)
Reaction: (1) L-threo-7,8-dihydrobiopterin + NADP+ = sepiapterin + NADPH + H+
(2) L-threo-tetrahydrobiopterin + 2 NADP+ = 6-pyruvoyl-5,6,7,8-tetrahydropterin + 2 NADPH + 2 H+
Glossary: sepiapterin = 2-amino-6-lactoyl-7,8-dihydropteridin-4(3H)-one
tetrahydrobiopterin = 5,6,7,8-tetrahydrobiopterin = 2-amino-6-(1,2-dihydroxypropyl)-5,6,7,8-tetrahydropteridin-4(3H)-one
Systematic name: L-threo-7,8-dihydrobiopterin:NADP+ oxidoreductase
Comments: This enzyme, isolated from the bacterium Chlorobium tepidum, catalyses the final step in the de novo synthesis of tetrahydrobiopterin from GTP. cf. EC 1.1.1.153, sepiapterin reductase (L-erythro-7,8-dihydrobiopterin forming).
References:
1.  Cho, S.H., Na, J.U., Youn, H., Hwang, C.S., Lee, C.H. and Kang, S.O. Sepiapterin reductase producing L-threo-dihydrobiopterin from Chlorobium tepidum. Biochem. J. 340 (1999) 497–503. [PMID: 10333495]
2.  Supangat, S., Choi, Y.K., Park, Y.S., Son, D., Han, C.D. and Lee, K.H. Expression, purification, crystallization and preliminary X-ray analysis of sepiapterin reductase from Chlorobium tepidum. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 61 (2005) 202–204. [PMID: 16510994]
[EC 1.1.1.325 created 2012]
 
 
EC 1.1.1.326     
Accepted name: zerumbone synthase
Reaction: 10-hydroxy-α-humulene + NAD+ = zerumbone + NADH + H+
Other name(s): ZSD1
Systematic name: 10-hydroxy-α-humulene:NAD+ oxidoreductase
Comments: The enzyme was cloned from shampoo ginger, Zingiber zerumbet.
References:
1.  Okamoto, S., Yu, F., Harada, H., Okajima, T., Hattan, J., Misawa, N. and Utsumi, R. A short-chain dehydrogenase involved in terpene metabolism from Zingiber zerumbet. FEBS J. 278 (2011) 2892–2900. [PMID: 21668645]
[EC 1.1.1.326 created 2012]
 
 
EC 1.1.1.327     
Accepted name: 5-exo-hydroxycamphor dehydrogenase
Reaction: 5-exo-hydroxycamphor + NAD+ = bornane-2,5-dione + NADH + H+
Other name(s): F-dehydrogenase; FdeH
Systematic name: 5-exo-hydroxycamphor:NAD+ oxidoreductase
Comments: Contains Zn2+. Isolated from Pseudomonas putida, and involved in degradation of (+)-camphor.
References:
1.  Rheinwald, J.G., Chakrabarty, A.M. and Gunsalus, I.C. A transmissible plasmid controlling camphor oxidation in Pseudomonas putida. Proc. Natl. Acad. Sci. USA 70 (1973) 885–889. [PMID: 4351810]
2.  Koga, H., Yamaguchi, E., Matsunaga, K., Aramaki, H. and Horiuchi, T. Cloning and nucleotide sequences of NADH-putidaredoxin reductase gene (camA) and putidaredoxin gene (camB) involved in cytochrome P-450cam hydroxylase of Pseudomonas putida. J. Biochem. 106 (1989) 831–836. [PMID: 2613690]
3.  Aramaki, H., Koga, H., Sagara, Y., Hosoi, M. and Horiuchi, T. Complete nucleotide sequence of the 5-exo-hydroxycamphor dehydrogenase gene on the CAM plasmid of Pseudomonas putida (ATCC 17453). Biochim. Biophys. Acta 1174 (1993) 91–94. [PMID: 8334169]
[EC 1.1.1.327 created 2012]
 
 
EC 1.1.1.328     
Accepted name: nicotine blue oxidoreductase
Reaction: 3,3′-bipyridine-2,2′,5,5′,6,6′-hexol + NAD(P)+ = (E)-2,2′,5,5′-tetrahydroxy-6H,6′H-[3,3′-bipyridinylidene]-6,6′-dione + NAD(P)H + H+
Glossary: 3,3′-bipyridine-2,2′,5,5′,6,6′-hexol = nicotine blue leuco form
(E)-2,2′,5,5′-tetrahydroxy-6H,6′H-[3,3′-bipyridinylidene]-6,6′-dione = nicotine blue
Other name(s): nboR (gene name)
Systematic name: 3,3′-bipyridine-2,2′,5,5′,6,6′-hexol:NADP+ 11-oxidoreductase
Comments: The enzyme, characterized from the nicotine degrading bacterium Arthrobacter nicotinovorans, catalyses the reduction of "nicotine blue" to its hydroquinone form (the opposite direction from that shown). Nicotine blue is the name given to the compound formed by the autocatalytic condensation of two molecules of 2,3,6-trihydroxypyridine, an intermediate in the nicotine degradation pathway. The main role of the enzyme may be to prevent the intracellular formation of nicotine blue semiquinone radicals, which by redox cycling would lead to the formation of toxic reactive oxygen species. The enzyme possesses a slight preference for NADH over NADPH.
References:
1.  Mihasan, M., Chiribau, C.B., Friedrich, T., Artenie, V. and Brandsch, R. An NAD(P)H-nicotine blue oxidoreductase is part of the nicotine regulon and may protect Arthrobacter nicotinovorans from oxidative stress during nicotine catabolism. Appl. Environ. Microbiol. 73 (2007) 2479–2485. [PMID: 17293530]
[EC 1.1.1.328 created 2012]
 
 
EC 1.1.1.329     
Accepted name: 2-deoxy-scyllo-inosamine dehydrogenase
Reaction: 2-deoxy-scyllo-inosamine + NAD(P)+ = 3-amino-2,3-dideoxy-scyllo-inosose + NAD(P)H + H+
Glossary: 2-deoxy-scyllo-inosamine = (1R,2S,3S,4R,5S)-5-aminocyclohexane-1,2,3,4-tetrol
Other name(s): neoA (gene name); kanK (gene name, ambiguous); kanE (gene name, ambiguous)
Systematic name: 2-deoxy-scyllo-inosamine:NAD(P)+ 1-oxidoreductase
Comments: Requires zinc. Involved in the biosynthetic pathways of several clinically important aminocyclitol antibiotics, including kanamycin, neomycin and ribostamycin. cf. EC 1.1.99.38, 2-deoxy-scyllo-inosamine dehydrogenase (AdoMet-dependent).
References:
1.  Kudo, F., Yamamoto, Y., Yokoyama, K., Eguchi, T. and Kakinuma, K. Biosynthesis of 2-deoxystreptamine by three crucial enzymes in Streptomyces fradiae NBRC 12773. J. Antibiot. (Tokyo) 58 (2005) 766–774. [PMID: 16506694]
2.  Nepal, K.K., Oh, T.J. and Sohng, J.K. Heterologous production of paromamine in Streptomyces lividans TK24 using kanamycin biosynthetic genes from Streptomyces kanamyceticus ATCC12853. Mol. Cells 27 (2009) 601–608. [PMID: 19466609]
[EC 1.1.1.329 created 2012]
 
 
EC 1.1.1.330     
Accepted name: very-long-chain 3-oxoacyl-CoA reductase
Reaction: a very-long-chain (3R)-3-hydroxyacyl-CoA + NADP+ = a very-long-chain 3-oxoacyl-CoA + NADPH + H+
Glossary: a very-long-chain acyl-CoA = an acyl-CoA thioester where the acyl chain contains 23 or more carbon atoms.
Other name(s): very-long-chain 3-ketoacyl-CoA reductase; very-long-chain β-ketoacyl-CoA reductase; KCR (gene name); IFA38 (gene name)
Systematic name: (3R)-3-hydroxyacyl-CoA:NADP+ oxidoreductase
Comments: The second component of the elongase, a microsomal protein complex responsible for extending palmitoyl-CoA and stearoyl-CoA (and modified forms thereof) to very-long-chain acyl CoAs. The enzyme is active with substrates with chain length of C16 to C34, depending on the species. cf. EC 2.3.1.199, very-long-chain 3-oxoacyl-CoA synthase, EC 4.2.1.134, very-long-chain (3R)-3-hydroxyacyl-[acyl-carrier protein] dehydratase, and EC 1.3.1.93, very-long-chain enoyl-CoA reductase.
References:
1.  Beaudoin, F., Gable, K., Sayanova, O., Dunn, T. and Napier, J.A. A Saccharomyces cerevisiae gene required for heterologous fatty acid elongase activity encodes a microsomal β-keto-reductase. J. Biol. Chem. 277 (2002) 11481–11488. [PMID: 11792704]
2.  Han, G., Gable, K., Kohlwein, S.D., Beaudoin, F., Napier, J.A. and Dunn, T.M. The Saccharomyces cerevisiae YBR159w gene encodes the 3-ketoreductase of the microsomal fatty acid elongase. J. Biol. Chem. 277 (2002) 35440–35449. [PMID: 12087109]
3.  Beaudoin, F., Wu, X., Li, F., Haslam, R.P., Markham, J.E., Zheng, H., Napier, J.A. and Kunst, L. Functional characterization of the Arabidopsis β-ketoacyl-coenzyme A reductase candidates of the fatty acid elongase. Plant Physiol. 150 (2009) 1174–1191. [PMID: 19439572]
[EC 1.1.1.330 created 2012]
 
 
EC 1.1.1.331     
Accepted name: secoisolariciresinol dehydrogenase
Reaction: (–)-secoisolariciresinol + 2 NAD+ = (–)-matairesinol + 2 NADH + 2 H+
Systematic name: (–)-secoisolariciresinol:NAD+ oxidoreductase
Comments: Isolated from the plants Forsythia intermedia [1] and Podophyllum peltatum [1-3]. An intermediate lactol is detected in vitro.
References:
1.  Xia, Z.Q., Costa, M.A., Pelissier, H.C., Davin, L.B. and Lewis, N.G. Secoisolariciresinol dehydrogenase purification, cloning, and functional expression. Implications for human health protection. J. Biol. Chem. 276 (2001) 12614–12623. [PMID: 11278426]
2.  Youn, B., Moinuddin, S.G., Davin, L.B., Lewis, N.G. and Kang, C. Crystal structures of apo-form and binary/ternary complexes of Podophyllum secoisolariciresinol dehydrogenase, an enzyme involved in formation of health-protecting and plant defense lignans. J. Biol. Chem. 280 (2005) 12917–12926. [PMID: 15653677]
3.  Moinuddin, S.G., Youn, B., Bedgar, D.L., Costa, M.A., Helms, G.L., Kang, C., Davin, L.B. and Lewis, N.G. Secoisolariciresinol dehydrogenase: mode of catalysis and stereospecificity of hydride transfer in Podophyllum peltatum. Org. Biomol. Chem. 4 (2006) 808–816. [PMID: 16493463]
[EC 1.1.1.331 created 2012]
 
 
EC 1.1.1.332     
Accepted name: chanoclavine-I dehydrogenase
Reaction: chanoclavine-I + NAD+ = chanoclavine-I aldehyde + NADH + H+
Glossary: chanoclavine-I = (1E)-2-methyl-3-[(4R,5R)-4-(methylamino)-1,3,4,5-tetrahydrobenz[cd]indol-5-yl]prop-2-en-1-ol
chanoclavine-I aldehyde = (1E)-2-methyl-3-[(4R,5R)-4-(methylamino)-1,3,4,5-tetrahydrobenz[cd]indol-5-yl]prop-2-enal
Other name(s): easD (gene name); fgaDH (gene name)
Systematic name: chanoclavine-I:NAD+ oxidoreductase
Comments: The enzyme catalyses a step in the pathway of ergot alkaloid biosynthesis in certain fungi.
References:
1.  Wallwey, C., Matuschek, M. and Li, S.M. Ergot alkaloid biosynthesis in Aspergillus fumigatus: conversion of chanoclavine-I to chanoclavine-I aldehyde catalyzed by a short-chain alcohol dehydrogenase FgaDH. Arch. Microbiol. 192 (2010) 127–134. [PMID: 20039019]
2.  Wallwey, C., Heddergott, C., Xie, X., Brakhage, A.A. and Li, S.M. Genome mining reveals the presence of a conserved gene cluster for the biosynthesis of ergot alkaloid precursors in the fungal family Arthrodermataceae. Microbiology 158 (2012) 1634–1644. [PMID: 22403186]
[EC 1.1.1.332 created 2012]
 
 
EC 1.1.1.333     
Accepted name: decaprenylphospho-β-D-erythro-pentofuranosid-2-ulose 2-reductase
Reaction: trans,octacis-decaprenylphospho-β-D-arabinofuranose + NAD+ = trans,octacis-decaprenylphospho-β-D-erythro-pentofuranosid-2-ulose + NADH + H+
Other name(s): decaprenylphospho-β-D-ribofuranose 2′-epimerase; Rv3791; DprE2
Systematic name: trans,octacis-decaprenylphospho-β-D-arabinofuranose:NAD+ 2-oxidoreductase
Comments: The reaction is catalysed in the reverse direction. The enzyme, isolated from the bacterium Mycobacterium smegmatis, is involved, along with EC 1.1.98.3, decaprenylphospho-β-D-ribofuranose 2-oxidase, in the epimerization of trans,octacis-decaprenylphospho-β-D-ribofuranose to trans,octacis-decaprenylphospho-β-D-arabinoofuranose, the arabinosyl donor for the biosynthesis of mycobacterial cell wall arabinan polymers.
References:
1.  Trefzer, C., Škovierová, H., Buroni, S., Bobovská, A., Nenci, S., Molteni, E., Pojer, F., Pasca, M.R., Makarov, V., Cole, S.T., Riccardi, G., Mikušová, K. and Johnsson, K. Benzothiazinones are suicide inhibitors of mycobacterial decaprenylphosphoryl-β-D-ribofuranose 2′-oxidase DprE1. J. Am. Chem. Soc. 134 (2012) 912–915. [PMID: 22188377]
[EC 1.1.1.333 created 2012]
 
 
EC 1.1.1.334     
Accepted name: methylecgonone reductase
Reaction: ecgonine methyl ester + NADP+ = ecgonone methyl ester + NADPH + H+
Glossary: ecgonine methyl ester = 2β-carbomethoxy-3β-tropine = methyl (1R,2R,3S,5S)-3-hydroxy-8-methyl-8-azabicyclo[3.2.1]octane-2-carboxylate
ecgonone methyl ester = 2β-carbomethoxy-3-tropinone = methyl (1R,2R,5S)-8-methyl-3-oxo-8-azabicyclo[3.2.1]octane-2-carboxylate
Other name(s): MecgoR (gene name)
Systematic name: ecgonine methyl ester:NADP+ oxidoreductase
Comments: The enzyme from the plant Erythroxylum coca catalyses the penultimate step in the biosynthesis of cocaine. In vivo the reaction proceeds in the opposite direction. With NADH instead of NADPH the reaction rate is reduced to 14%. The enzyme also reduces tropinone, nortropinone and 6-hydroxytropinone but with lower reaction rates.
References:
1.  Jirschitzka, J., Schmidt, G.W., Reichelt, M., Schneider, B., Gershenzon, J. and D'Auria, J.C. Plant tropane alkaloid biosynthesis evolved independently in the Solanaceae and Erythroxylaceae. Proc. Natl. Acad. Sci. USA 109 (2012) 10304–10309. [PMID: 22665766]
[EC 1.1.1.334 created 2012]
 
 
EC 1.1.1.335     
Accepted name: UDP-N-acetyl-2-amino-2-deoxyglucuronate dehydrogenase
Reaction: UDP-N-acetyl-2-amino-2-deoxy-α-D-glucuronate + NAD+ = UDP-2-acetamido-2-deoxy-α-D-ribo-hex-3-uluronate + NADH + H+
Other name(s): WlbA; WbpB
Systematic name: UDP-N-acetyl-2-amino-2-deoxy-α-D-glucuronate:NAD+ 3-oxidoreductase
Comments: This enzyme participates in the biosynthetic pathway for UDP-α-D-ManNAc3NAcA (UDP-2,3-diacetamido-2,3-dideoxy-α-D-mannuronic acid), an important precursor of B-band lipopolysaccharide. The enzymes from Pseudomonas aeruginosa serotype O5 and Thermus thermophilus form a complex with the the enzyme catalysing the next step the pathway (EC 2.6.1.98, UDP-2-acetamido-2-deoxy-ribo-hexuluronate aminotransferase). The enzyme also possesses an EC 1.1.99.2 (L-2-hydroxyglutarate dehydrogenase) activity, and utilizes the 2-oxoglutarate produced by EC 2.6.1.98 to regenerate the tightly bound NAD+. The enzymes from Bordetella pertussis and Chromobacterium violaceum do not bind NAD+ as tightly and do not require 2-oxoglutarate to function.
References:
1.  Westman, E.L., McNally, D.J., Charchoglyan, A., Brewer, D., Field, R.A. and Lam, J.S. Characterization of WbpB, WbpE, and WbpD and reconstitution of a pathway for the biosynthesis of UDP-2,3-diacetamido-2,3-dideoxy-D-mannuronic acid in Pseudomonas aeruginosa. J. Biol. Chem. 284 (2009) 11854–11862. [PMID: 19282284]
2.  Larkin, A. and Imperiali, B. Biosynthesis of UDP-GlcNAc(3NAc)A by WbpB, WbpE, and WbpD: enzymes in the Wbp pathway responsible for O-antigen assembly in Pseudomonas aeruginosa PAO1. Biochemistry 48 (2009) 5446–5455. [PMID: 19348502]
3.  Thoden, J.B. and Holden, H.M. Structural and functional studies of WlbA: A dehydrogenase involved in the biosynthesis of 2,3-diacetamido-2,3-dideoxy-D-mannuronic acid. Biochemistry 49 (2010) 7939–7948. [PMID: 20690587]
4.  Thoden, J.B. and Holden, H.M. Biochemical and structural characterization of WlbA from Bordetella pertussis and Chromobacterium violaceum: enzymes required for the biosynthesis of 2,3-diacetamido-2,3-dideoxy-D-mannuronic acid. Biochemistry 50 (2011) 1483–1491. [PMID: 21241053]
[EC 1.1.1.335 created 2012]
 
 
EC 1.1.1.336     
Accepted name: UDP-N-acetyl-D-mannosamine dehydrogenase
Reaction: UDP-N-acetyl-α-D-mannosamine + 2 NAD+ + H2O = UDP-N-acetyl-α-D-mannosaminuronate + 2 NADH + 2 H+
Other name(s): UDP-ManNAc 6-dehydrogenase; wecC (gene name)
Systematic name: UDP-N-acetyl-α-D-mannosamine:NAD+ 6-oxidoreductase
Comments: Part of the pathway for acetamido sugar biosynthesis in bacteria and archaea. The enzyme has no activity with NADP+.
References:
1.  Namboori, S.C. and Graham, D.E. Acetamido sugar biosynthesis in the Euryarchaea. J. Bacteriol. 190 (2008) 2987–2996. [PMID: 18263721]
[EC 1.1.1.336 created 2012]
 
 
EC 1.1.1.337     
Accepted name: L-2-hydroxycarboxylate dehydrogenase (NAD+)
Reaction: a (2S)-2-hydroxycarboxylate + NAD+ = a 2-oxocarboxylate + NADH + H+
Other name(s): (R)-sulfolactate:NAD+ oxidoreductase; L-sulfolactate dehydrogenase; (R)-sulfolactate dehydrogenase; L-2-hydroxyacid dehydrogenase (NAD+); ComC
Systematic name: (2S)-2-hydroxycarboxylate:NAD+ oxidoreductase
Comments: The enzyme from the archaeon Methanocaldococcus jannaschii acts on multiple (S)-2-hydroxycarboxylates including (2R)-3-sulfolactate, (S)-malate, (S)-lactate, and (S)-2-hydroxyglutarate [3]. Note that (2R)-3-sulfolactate has the same stereo configuration as (2S)-2-hydroxycarboxylates.
References:
1.  Graupner, M., Xu, H. and White, R.H. Identification of an archaeal 2-hydroxy acid dehydrogenase catalyzing reactions involved in coenzyme biosynthesis in methanoarchaea. J. Bacteriol. 182 (2000) 3688–3692. [PMID: 10850983]
2.  Graupner, M. and White, R.H. The first examples of (S)-2-hydroxyacid dehydrogenases catalyzing the transfer of the pro-4S hydrogen of NADH are found in the archaea. Biochim. Biophys. Acta 1548 (2001) 169–173. [PMID: 11451450]
3.  Graham, D.E. and White, R.H. Elucidation of methanogenic coenzyme biosyntheses: from spectroscopy to genomics. Nat. Prod. Rep. 19 (2002) 133–147. [PMID: 12013276]
4.  Rein, U., Gueta, R., Denger, K., Ruff, J., Hollemeyer, K. and Cook, A.M. Dissimilation of cysteate via 3-sulfolactate sulfo-lyase and a sulfate exporter in Paracoccus pantotrophus NKNCYSA. Microbiology 151 (2005) 737–747. [PMID: 15758220]
[EC 1.1.1.337 created 2012]
 
 
EC 1.1.1.338     
Accepted name: (2R)-3-sulfolactate dehydrogenase (NADP+)
Reaction: (2R)-3-sulfolactate + NADP+ = 3-sulfopyruvate + NADPH + H+
Other name(s): (R)-sulfolactate:NADP+ oxidoreductase; L-sulfolactate dehydrogenase; (R)-sulfolactate dehydrogenase; ComC
Systematic name: (2R)-3-sulfolactate:NADP+ oxidoreductase
Comments: The enzyme from the bacterium Chromohalobacter salexigens can only utilize NADP+. It functions both biosynthetically in coenzyme M biosynthesis and degradatively, in the degradation of sulfolactate. It can not use (S)-malate and (S)-lactate.
References:
1.  Denger, K. and Cook, A.M. Racemase activity effected by two dehydrogenases in sulfolactate degradation by Chromohalobacter salexigens: purification of (S)-sulfolactate dehydrogenase. Microbiology 156 (2010) 967–974. [PMID: 20007648]
[EC 1.1.1.338 created 2012]
 
 
EC 1.1.1.339     
Accepted name: dTDP-6-deoxy-L-talose 4-dehydrogenase (NAD+)
Reaction: dTDP-6-deoxy-β-L-talose + NAD+ = dTDP-4-dehydro-β-L-rhamnose + NADH + H+
Glossary: dTDP-4-dehydro-β-L-rhamnose = dTDP-4-dehydro-6-deoxy-β-L-mannose
dTDP-6-deoxy-β-L-talose = dTDP-β-L-pneumose
Other name(s): tll (gene name)
Systematic name: dTDP-6-deoxy-β-L-talose:NAD+ 4-oxidoreductase
Comments: The enzyme has been characterized from the bacterium Aggregatibacter actinomycetemcomitans, in which it participates in the biosynthesis of the serotype c-specific polysaccharide antigen. Shows no activity with NADP+.
References:
1.  Nakano, Y., Suzuki, N., Yoshida, Y., Nezu, T., Yamashita, Y. and Koga, T. Thymidine diphosphate-6-deoxy-L-lyxo-4-hexulose reductase synthesizing dTDP-6-deoxy-L-talose from Actinobacillus actinomycetemcomitans. J. Biol. Chem. 275 (2000) 6806–6812. [PMID: 10702238]
[EC 1.1.1.339 created 2012]
 
 
EC 1.1.1.340     
Accepted name: 1-deoxy-11β-hydroxypentalenate dehydrogenase
Reaction: 1-deoxy-11β-hydroxypentalenate + NAD+ = 1-deoxy-11-oxopentalenate + NADH + H+
Glossary: 1-deoxy-11β-hydroxypentalenate = (1S,2R,3aR,5aS,8aR)-2-hydroxy-1,7,7-trimethyl-1,2,3,3a,5a,6,7,8-octahydrocyclopenta[c]pentalene-4-carboxylate
1-deoxy-11-oxopentalenate = (1S,3aR,5aS)-1,7,7-trimethyl-2-oxo-1,2,3,3a,5a,6,7,8-octahydrocyclopenta[c]pentalene-4-carboxylate
Other name(s): 1-deoxy-11β-hydroxypentalenic acid dehydrogenase; ptlF (gene name); penF (gene name)
Systematic name: 1-deoxy-11β-hydroxypentalenate:NAD+ oxidoreductase
Comments: Isolated from the bacterium Streptomyces avermitilis and present in many other Streptomyces species. Part of the pathway for pentalenolactone biosynthesis.
References:
1.  You, Z., Omura, S., Ikeda, H. and Cane, D.E. Pentalenolactone biosynthesis: Molecular cloning and assignment of biochemical function to PtlF, a short-chain dehydrogenase from Streptomyces avermitilis, and identification of a new biosynthetic intermediate. Arch. Biochem. Biophys. 459 (2007) 233–240. [PMID: 17178094]
[EC 1.1.1.340 created 2012]
 
 
EC 1.1.1.341     
Accepted name: CDP-abequose synthase
Reaction: CDP-α-D-abequose + NADP+ = CDP-4-dehydro-3,6-dideoxy-α-D-glucose + NADPH + H+
Glossary: CDP-α-D-abequose = CDP-3,6-dideoxy-α-D-xylo-hexose
Other name(s): rfbJ (gene name)
Systematic name: CDP-α-D-abequose:NADP+ 4-oxidoreductase
Comments: Isolated from Yersinia pseudotuberculosis [1,3] and Salmonella enterica [1,2].
References:
1.  Kessler, A.C., Brown, P.K., Romana, L.K. and Reeves, P.R. Molecular cloning and genetic characterization of the rfb region from Yersinia pseudotuberculosis serogroup IIA, which determines the formation of the 3,6-dideoxyhexose abequose. J. Gen. Microbiol. 137 (1991) 2689–2695. [PMID: 1724263]
2.  Wyk, P. and Reeves, P. Identification and sequence of the gene for abequose synthase, which confers antigenic specificity on group B salmonellae: homology with galactose epimerase. J. Bacteriol. 171 (1989) 5687–5693. [PMID: 2793832]
3.  Thorson, J.S., Lo, S.F., Ploux, O., He, X. and Liu, H.W. Studies of the biosynthesis of 3,6-dideoxyhexoses: molecular cloning and characterization of the asc (ascarylose) region from Yersinia pseudotuberculosis serogroup VA. J. Bacteriol. 176 (1994) 5483–5493. [PMID: 8071227]
[EC 1.1.1.341 created 2012]
 
 
EC 1.1.1.342     
Accepted name: CDP-paratose synthase
Reaction: CDP-α-D-paratose + NADP+ = CDP-4-dehydro-3,6-dideoxy-α-D-glucose + NADPH + H+
Glossary: CDP-α-D-paratose = CDP-3,6-dideoxy-α-D-glucose = CDP-3,6-dideoxy-α-D-ribo-hexose
Other name(s): rfbS (gene name)
Systematic name: CDP-α-D-paratose:NADP+ 4-oxidoreductase
Comments: The enzyme is involved in synthesis of paratose and tyvelose, unusual 3,6-dideoxyhexose sugars that form part of the O-antigen in the lipopolysaccharides of several enteric bacteria. Isolated from Salmonella enterica subsp. enterica serovar Typhi (Salmonella typhi).
References:
1.  Verma, N. and Reeves, P. Identification and sequence of rfbS and rfbE, which determine antigenic specificity of group A and group D salmonellae. J. Bacteriol. 171 (1989) 5694–5701. [PMID: 2793833]
2.  Hallis, T.M., Lei, Y., Que, N.L. and Liu, H. Mechanistic studies of the biosynthesis of paratose: purification and characterization of CDP-paratose synthase. Biochemistry 37 (1998) 4935–4945. [PMID: 9538012]
[EC 1.1.1.342 created 2012]
 
 
EC 1.1.1.343     
Accepted name: phosphogluconate dehydrogenase (NAD+-dependent, decarboxylating)
Reaction: 6-phospho-D-gluconate + NAD+ = D-ribulose 5-phosphate + CO2 + NADH + H+
Other name(s): 6-PGDH (ambiguous); gntZ (gene name); GNDl
Systematic name: 6-phospho-D-gluconate:NAD+ 2-oxidoreductase (decarboxylating)
Comments: Highly specific for NAD+. The enzyme catalyses both the oxidation and decarboxylation of 6-phospho-D-gluconate. In the bacterium Methylobacillus flagellatus the enzyme participates in a formaldehyde oxidation pathway [4]. cf. EC 1.1.1.44, phosphogluconate dehydrogenase (NADP+-dependent, decarboxylating).
References:
1.  Kiriuchin, M. Y., Kletsova, L. V., Chistoserdov, A. Y. and Tsygankov, Y. D. Properties of glucose 6-phosphate and 6-phosphogluconate dehydrogenases of the obligate methylotroph Methylobacillus flagellatum KT. FEMS Microbiol. Lett. 52 (1988) 199–204.
2.  Ohara, H., Russell, R.A., Uchida, K. and Kondo, H. Purification and characterization of NAD-specific 6-phosphogluconate dehydrogenase from Leuconostoc lactis SHO-54. J. Biosci. Bioeng. 98 (2004) 126–128. [PMID: 16233677]
3.  Zamboni, N., Fischer, E., Laudert, D., Aymerich, S., Hohmann, H.P. and Sauer, U. The Bacillus subtilis yqjI gene encodes the NADP+-dependent 6-P-gluconate dehydrogenase in the pentose phosphate pathway. J. Bacteriol. 186 (2004) 4528–4534. [PMID: 15231785]
4.  Chistoserdova, L., Gomelsky, L., Vorholt, J.A., Gomelsky, M., Tsygankov, Y.D. and Lidstrom, M.E. Analysis of two formaldehyde oxidation pathways in Methylobacillus flagellatus KT, a ribulose monophosphate cycle methylotroph. Microbiology 146 (2000) 233–238. [PMID: 10658669]
[EC 1.1.1.343 created 2013]
 
 
EC 1.1.1.344     
Accepted name: dTDP-6-deoxy-L-talose 4-dehydrogenase [NAD(P)+]
Reaction: dTDP-6-deoxy-β-L-talose + NAD(P)+ = dTDP-4-dehydro-β-L-rhamnose + NAD(P)H + H+
Glossary: dTDP-4-dehydro-β-L-rhamnose = dTDP-4-dehydro-6-deoxy-β-L-mannose
dTDP-6-deoxy-β-L-talose = dTDP-β-L-pneumose
Other name(s): tal (gene name)
Systematic name: dTDP-6-deoxy-β-L-talose:NAD(P)+ 4-oxidoreductase
Comments: The enzyme works equally well with NAD+ and NADP+.
References:
1.  Karki, S., Yoo, H.G., Kwon, S.Y., Suh, J.W. and Kwon, H.J. Cloning and in vitro characterization of dTDP-6-deoxy-L-talose biosynthetic genes from Kitasatospora kifunensis featuring the dTDP-6-deoxy-L-lyxo-4-hexulose reductase that synthesizes dTDP-6-deoxy-L-talose. Carbohydr. Res. 345 (2010) 1958–1962. [PMID: 20667525]
[EC 1.1.1.344 created 2013]
 
 
EC 1.1.1.345     
Accepted name: D-2-hydroxyacid dehydrogenase (NAD+)
Reaction: an (R)-2-hydroxycarboxylate + NAD+ = a 2-oxocarboxylate + NADH + H+
Other name(s): LdhA; HdhD; D-2-hydroxyisocaproate dehydrogenase; R-HicDH; D-HicDH; (R)-2-hydroxy-4-methylpentanoate:NAD+ oxidoreductase; (R)-2-hydroxyisocaproate dehydrogenase; D-mandelate dehydrogenase (ambiguous)
Systematic name: (R)-2-hydroxycarboxylate:NAD+ oxidoreductase
Comments: The enzymes, characterized from bacteria (Peptoclostridium difficile, Enterococcus faecalis and from lactic acid bacteria) prefer substrates with a main chain of 5 carbons (such as 4-methyl-2-oxopentanoate) to those with a shorter chain. It also utilizes phenylpyruvate. The enzyme from the halophilic archaeon Haloferax mediterranei prefers substrates with a main chain of 3-4 carbons (pyruvate and 2-oxobutanoate). cf. EC 1.1.1.272, (D)-2-hydroxyacid dehydrogenase (NADP+).
References:
1.  Dengler, U., Niefind, K., Kiess, M. and Schomburg, D. Crystal structure of a ternary complex of D-2-hydroxyisocaproate dehydrogenase from Lactobacillus casei, NAD+ and 2-oxoisocaproate at 1.9 Å resolution. J. Mol. Biol. 267 (1997) 640–660. [PMID: 9126843]
2.  Bonete, M.J., Ferrer, J., Pire, C., Penades, M. and Ruiz, J.L. 2-Hydroxyacid dehydrogenase from Haloferax mediterranei, a D-isomer-specific member of the 2-hydroxyacid dehydrogenase family. Biochimie 82 (2000) 1143–1150. [PMID: 11120357]
3.  Kim, J., Darley, D., Selmer, T. and Buckel, W. Characterization of (R)-2-hydroxyisocaproate dehydrogenase and a family III coenzyme A transferase involved in reduction of L-leucine to isocaproate by Clostridium difficile. Appl. Environ. Microbiol. 72 (2006) 6062–6069. [PMID: 16957230]
4.  Wada, Y., Iwai, S., Tamura, Y., Ando, T., Shinoda, T., Arai, K. and Taguchi, H. A new family of D-2-hydroxyacid dehydrogenases that comprises D-mandelate dehydrogenases and 2-ketopantoate reductases. Biosci. Biotechnol. Biochem. 72 (2008) 1087–1094. [PMID: 18391442]
5.  Chambellon, E., Rijnen, L., Lorquet, F., Gitton, C., van Hylckama Vlieg, J.E., Wouters, J.A. and Yvon, M. The D-2-hydroxyacid dehydrogenase incorrectly annotated PanE is the sole reduction system for branched-chain 2-keto acids in Lactococcus lactis. J. Bacteriol. 191 (2009) 873–881. [PMID: 19047348]
6.  Miyanaga, A., Fujisawa, S., Furukawa, N., Arai, K., Nakajima, M. and Taguchi, H. The crystal structure of D-mandelate dehydrogenase reveals its distinct substrate and coenzyme recognition mechanisms from those of 2-ketopantoate reductase. Biochem. Biophys. Res. Commun. 439 (2013) 109–114. [PMID: 23954635]
[EC 1.1.1.345 created 2013]
 
 
EC 1.1.1.346     
Accepted name: 2,5-didehydrogluconate reductase (2-dehydro-L-gulonate-forming)
Reaction: 2-dehydro-L-gulonate + NADP+ = 2,5-didehydro-D-gluconate + NADPH + H+
Glossary: 2-dehydro-L-gulonate = 2-dehydro-L-idonate = 2-keto-L-gulonate
Other name(s): 2,5-diketo-D-gluconate-reductase (ambiguous); YqhE reductase; dkgA (gene name); dkgB (gene name)
Systematic name: 2-dehydro-D-gluconate:NADP+ 2-oxidoreductase (2-dehydro-L-gulonate-forming)
Comments: The enzyme is involved in ketogluconate metabolism, and catalyses the reaction in vivo in the reverse direction to that shown [1]. It is used in the commercial microbial production of ascorbate. cf. EC 1.1.1.274, 2,5-didehydrogluconate reductase (2-dehydro-D-gluconate-forming).
References:
1.  Sonoyama, T. and Kobayashi, K. Purification and properties of two 2,5-diketo-D-gluconate reductases from a mutant strain derived from Corynebacterium sp. J Ferment Technol. 65 (1987) 311–317.
2.  Miller, J.V., Estell, D.A. and Lazarus, R.A. Purification and characterization of 2,5-diketo-D-gluconate reductase from Corynebacterium sp. J. Biol. Chem. 262 (1987) 9016–9020. [PMID: 3597405]
3.  Yum, D.Y., Lee, B.Y. and Pan, J.G. Identification of the yqhE and yafB genes encoding two 2,5-diketo-D-gluconate reductases in Escherichia coli. Appl. Environ. Microbiol. 65 (1999) 3341–3346. [PMID: 10427017]
4.  Maremonti, M., Greco, G. and Wichmann, R. Characterisation of 2,5-diketo-D-gluconic acid reductase from Corynebacterium sp. Biotechnology Letters 18 (1996) 845–850.
5.  Khurana, S., Powers, D.B., Anderson, S. and Blaber, M. Crystal structure of 2,5-diketo-D-gluconic acid reductase A complexed with NADPH at 2.1-Å resolution. Proc. Natl. Acad. Sci. USA 95 (1998) 6768–6773. [PMID: 9618487]
[EC 1.1.1.346 created 2013]
 
 
EC 1.1.1.347     
Accepted name: geraniol dehydrogenase (NAD+)
Reaction: geraniol + NAD+ = geranial + NADH + H+
Other name(s): GeDH; geoA (gene name)
Systematic name: geraniol:NAD+ oxidoreductase
Comments: The enzyme from the bacterium Castellaniella defragrans is most active in vitro with perillyl alcohol [2]. The enzyme from the prune mite Carpoglyphus lactis also acts (more slowly) on farnesol but not on nerol [1].
References:
1.  Noge, K., Kato, M., Mori, N., Kataoka, M., Tanaka, C., Yamasue, Y., Nishida, R. and Kuwahara, Y. Geraniol dehydrogenase, the key enzyme in biosynthesis of the alarm pheromone, from the astigmatid mite Carpoglyphus lactis (Acari: Carpoglyphidae). FEBS J. 275 (2008) 2807–2817. [PMID: 18422649]
2.  Lüddeke, F., Wülfing, A., Timke, M., Germer, F., Weber, J., Dikfidan, A., Rahnfeld, T., Linder, D., Meyerdierks, A. and Harder, J. Geraniol and geranial dehydrogenases induced in anaerobic monoterpene degradation by Castellaniella defragrans. Appl. Environ. Microbiol. 78 (2012) 2128–2136. [PMID: 22286981]
[EC 1.1.1.347 created 2013]
 
 
EC 1.1.1.348     
Accepted name: (3R)-2′-hydroxyisoflavanone reductase
Reaction: a (4R)-4,2′-dihydroxyisoflavan + NADP+ = a (3R)-2′-hydroxyisoflavanone + NADPH + H+
Glossary: (3R)-vestitone = (3R)-2′,7-dihydroxy-4′-methoxyisoflavanone
Other name(s): vestitone reductase; pterocarpin synthase (incorrect); pterocarpan synthase (incorrect)
Systematic name: (3R)-2′-hydroxyisoflavanone:NADP+ 4-oxidoreductase
Comments: This plant enzyme participates in the biosynthesis of the pterocarpan phytoalexins medicarpin, maackiain, and several forms of glyceollin. The enzyme has a strict stereo specificity for the 3R-isoflavanones.
References:
1.  Bless, W. and Barz, W. Isolation of pterocarpan synthase, the terminal enzyme of pterocarpan phytoalexin biosynthesis in cell-suspension cultures of Cicer arietinum. FEBS Lett. 235 (1988) 47–50.
2.  Guo, L., Dixon, R.A. and Paiva, N.L. Conversion of vestitone to medicarpin in alfalfa (Medicago sativa L.) is catalyzed by two independent enzymes. Identification, purification, and characterization of vestitone reductase and 7,2′-dihydroxy-4′-methoxyisoflavanol dehydratase. J. Biol. Chem. 269 (1994) 22372–22378. [PMID: 8071365]
3.  Guo, L., Dixon, R.A. and Paiva, N.L. The ‘pterocarpan synthase’ of alfalfa: association and co-induction of vestitone reductase and 7,2′-dihydroxy-4′-methoxy-isoflavanol (DMI) dehydratase, the two final enzymes in medicarpin biosynthesis. FEBS Lett. 356 (1994) 221–225. [PMID: 7805842]
4.  Guo, L. and Paiva, N.L. Molecular cloning and expression of alfalfa (Medicago sativa L.) vestitone reductase, the penultimate enzyme in medicarpin biosynthesis. Arch. Biochem. Biophys. 320 (1995) 353–360. [PMID: 7625843]
5.  Shao, H., Dixon, R.A. and Wang, X. Crystal structure of vestitone reductase from alfalfa (Medicago sativa L.). J. Mol. Biol. 369 (2007) 265–276. [PMID: 17433362]
[EC 1.1.1.348 created 1992 as EC 1.1.1.246, part transferred 2013 to EC 1.1.1.348]
 
 
EC 1.1.1.349     
Accepted name: norsolorinic acid ketoreductase
Reaction: (1′S)-averantin + NADP+ = norsolorinic acid + NADPH + H+
Glossary: norsolorinic acid = 2-hexanoyl-1,3,6,8-tetrahydroxy-9,10-anthraquinone
(1′S)-averantin = 1,3,6,8-tetrahydroxy-[(1S)-2-hydroxyhexyl]-9,10-anthraquinone
Other name(s): aflD (gene name); nor-1 (gene name)
Systematic name: (1′S)-averantin:NADP+ oxidoreductase
Comments: Involved in the synthesis of aflatoxins in the fungus Aspergillus parasiticus.
References:
1.  Yabe, K., Matsuyama, Y., Ando, Y., Nakajima, H. and Hamasaki, T. Stereochemistry during aflatoxin biosynthesis: conversion of norsolorinic acid to averufin. Appl. Environ. Microbiol. 59 (1993) 2486–2492. [PMID: 8368836]
2.  Zhou, R. and Linz, J.E. Enzymatic function of the nor-1 protein in aflatoxin biosynthesis in Aspergillus parasiticus. Appl. Environ. Microbiol. 65 (1999) 5639–5641. [PMID: 10584035]
[EC 1.1.1.349 created 2013]
 
 
EC 1.1.1.350     
Accepted name: ureidoglycolate dehydrogenase (NAD+)
Reaction: (S)-ureidoglycolate + NAD+ = N-carbamoyl-2-oxoglycine + NADH + H+
Systematic name: (S)-ureidoglycolate:NAD+ oxidoreductase
Comments: Involved in catabolism of purines. The enzyme from the bacterium Escherichia coli is specific for NAD+ [2]. cf. EC 1.1.1.154, ureidoglycolate dehydrogenase [NAD(P)+].
References:
1.  Cusa, E., Obradors, N., Baldoma, L., Badia, J. and Aguilar, J. Genetic analysis of a chromosomal region containing genes required for assimilation of allantoin nitrogen and linked glyoxylate metabolism in Escherichia coli. J. Bacteriol. 181 (1999) 7479–7484. [PMID: 10601204]
2.  Kim, M.I., Shin, I., Cho, S., Lee, J. and Rhee, S. Structural and functional insights into (S)-ureidoglycolate dehydrogenase, a metabolic branch point enzyme in nitrogen utilization. PLoS One 7:e52066 (2012). [PMID: 23284870]
[EC 1.1.1.350 created 2013]
 
 
EC 1.1.1.351     
Accepted name: phosphogluconate dehydrogenase [NAD(P)+-dependent, decarboxylating]
Reaction: 6-phospho-D-gluconate + NAD(P)+ = D-ribulose 5-phosphate + CO2 + NAD(P)H + H+
Systematic name: 6-phospho-D-gluconate:NAD(P)+ 2-oxidoreductase (decarboxylating)
Comments: The enzyme participates in the oxidative branch of the pentose phosphate pathway, whose main purpose is to produce reducing power and pentose for biosynthetic reactions. Unlike EC 1.1.1.44, phosphogluconate dehydrogenase (NADP+-dependent, decarboxylating), it is not specific for NADP+ and can accept both cofactors with similar efficiency. cf. EC 1.1.1.343, phosphogluconate dehydrogenase [NAD+-dependent, decarboxylating].
References:
1.  Ben-Bassat, A. and Goldberg, I. Purification and properties of glucose-6-phosphate dehydrogenase (NADP+/NAD+) and 6-phosphogluconate dehydrogenase (NADP+/NAD+) from methanol-grown Pseudomonas C. Biochim. Biophys. Acta 611 (1980) 1–10. [PMID: 7350909]
2.  Stournaras, C., Maurer, P. and Kurz, G. 6-phospho-D-gluconate dehydrogenase from Pseudomonas fluorescens. Properties and subunit structure. Eur. J. Biochem. 130 (1983) 391–396. [PMID: 6402366]
3.  Levy, H.R., Vought, V.E., Yin, X. and Adams, M.J. Identification of an arginine residue in the dual coenzyme-specific glucose-6-phosphate dehydrogenase from Leuconostoc mesenteroides that plays a key role in binding NADP+ but not NAD+. Arch. Biochem. Biophys. 326 (1996) 145–151. [PMID: 8579362]
[EC 1.1.1.351 created 2013]
 
 
EC 1.1.1.352     
Accepted name: 5′-hydroxyaverantin dehydrogenase
Reaction: (1) (1′S,5′S)-hydroxyaverantin + NAD+ = 5′-oxoaverantin + NADH + H+
(2) (1′S,5′R)-hydroxyaverantin + NAD+ = 5′-oxoaverantin + NADH + H+
Glossary: 5′-oxoaverantin = 1,3,6,8-tetrahydroxy-2-[(1S)-1-hydroxy-5-oxohexyl]anthracene-9,10-dione
Other name(s): HAVN dehydrogenase; adhA (gene name)
Systematic name: (1′S,5′S)-hydroxyaverantin:NAD+ oxidoreductase
Comments: Isolated from the aflatoxin-producing mold Aspergillus parasiticus [2]. Involved in aflatoxin biosynthesis. 5′-Oxoaverantin will spontaneously form averufin by intramolecular ketalisation. cf. EC 4.2.1.142, 5′-oxoaverantin cyclase.
References:
1.  Chang, P.K., Yu, J., Ehrlich, K.C., Boue, S.M., Montalbano, B.G., Bhatnagar, D. and Cleveland, T.E. adhA in Aspergillus parasiticus is involved in conversion of 5′-hydroxyaverantin to averufin. Appl. Environ. Microbiol. 66 (2000) 4715–4719. [PMID: 11055914]
2.  Sakuno, E., Yabe, K. and Nakajima, H. Involvement of two cytosolic enzymes and a novel intermediate, 5′-oxoaverantin, in the pathway from 5′-hydroxyaverantin to averufin in aflatoxin biosynthesis. Appl. Environ. Microbiol. 69 (2003) 6418–6426. [PMID: 14602595]
[EC 1.1.1.352 created 2013]
 
 
EC 1.1.1.353     
Accepted name: versiconal hemiacetal acetate reductase
Reaction: (1) versicolorone + NADP+ = 1′-hydroxyversicolorone + NADPH + H+
(2) versiconol acetate + NADP+ = versiconal hemiacetal acetate + NADPH + H+
(3) versiconol + NADP+ = versiconal + NADPH + H+
Glossary: 1′-hydroxyversicolorone = (2S,3S)-2,4,6,8-tetrahydroxy-3-(3-oxobutyl)anthra[2,3-b]furan-5,10-dione
versiconal = (2S,3S)-2,4,6,8-tetrahydroxy-3-(2-hydroxyethyl)anthra[2,3-b]furan-5,10-dione
versiconal hemiacetal acetate = 2-[(2S,3S)-2,4,6,8-tetrahydroxy-5,10-dioxo-5,10-dihydroanthra[2,3-b]furan-3-yl]ethyl acetate
versiconol = 1,3,6,8-tetrahydroxy-3-[(2S)-1,4-dihydroxybutan-2-yl]anthracene-5,10-dione
versiconol acetate = (3S)-4-hydroxy-3-[1,3,6,8-tetrahydroxy-9,10-dioxo-9,10-dihydroanthracen-2-yl]butyl acetate
versicolorone = 1,3,6,8-tetrahydroxy-2-[(2S)-1-hydroxy-5-oxohexan-2-yl]anthracene-5,10-dione
Other name(s): VHA reductase; VHA reductase I; VHA reductase II; vrdA (gene name)
Systematic name: versiconol-acetate:NADP+ oxidoreductase
Comments: Isolated from the mold Aspergillus parasiticus. Involved in a metabolic grid that leads to aflatoxin biosynthesis.
References:
1.  Matsushima, K., Ando, Y., Hamasaki, T. and Yabe, K. Purification and characterization of two versiconal hemiacetal acetate reductases involved in aflatoxin biosynthesis. Appl. Environ. Microbiol. 60 (1994) 2561–2567. [PMID: 16349333]
2.  Shima, Y., Shiina, M., Shinozawa, T., Ito, Y., Nakajima, H., Adachi, Y. and Yabe, K. Participation in aflatoxin biosynthesis by a reductase enzyme encoded by vrdA gene outside the aflatoxin gene cluster. Fungal Genet. Biol. 46 (2009) 221–231. [PMID: 19211038]
[EC 1.1.1.353 created 2013]
 
 
EC 1.1.1.354     
Accepted name: farnesol dehydrogenase (NAD+)
Reaction: (2E,6E)-farnesol + NAD+ = (2E,6E)-farnesal + NADH + H+
Other name(s): NAD+-farnesol dehydrogenase
Systematic name: (2E,6E)-farnesol:NAD+ 1-oxidoreductase
Comments: The enzyme from the prune mite Carpoglyphus lactis also acts on geraniol with greater activity [cf. EC 1.1.1.347, geraniol dehydrogenase (NAD+)]. Unlike EC 1.1.1.216, farnesol dehydrogenase (NADP+), this enzyme cannot use NADP+ as cofactor.
References:
1.  Noge, K., Kato, M., Mori, N., Kataoka, M., Tanaka, C., Yamasue, Y., Nishida, R. and Kuwahara, Y. Geraniol dehydrogenase, the key enzyme in biosynthesis of the alarm pheromone, from the astigmatid mite Carpoglyphus lactis (Acari: Carpoglyphidae). FEBS J. 275 (2008) 2807–2817. [PMID: 18422649]
[EC 1.1.1.354 created 2013]
 
 
EC 1.1.1.355     
Accepted name: 2′-dehydrokanamycin reductase
Reaction: kanamycin A + NADP+ = 2′-dehydrokanamycin A + NADPH + H+
Glossary: kanamycin A = (1S,2R,3R,4S,6R)-4,6-diamino-3-(6-amino-6-deoxy-α-D-glucopyranosyloxy)-2-hydroxycyclohexyl 3-amino-3-deoxy-α-D-glucopyranoside
2′-dehydrokanamycin A = (1S,2R,3R,4S,6R)-4,6-diamino-3-[(6-amino-6-deoxy-α-D-arabino-hexopyranosyl-2-ulose)oxy]-2-hydroxycyclohexyl 3-amino-3-deoxy-α-D-glucopyranoside
Other name(s): kanK (gene name, ambiguous)
Systematic name: kanamycin A:NADP+ oxidoreductase
Comments: Found in the bacterium Streptomyces kanamyceticus where it is involved in the conversion of kanamycin B to kanamycin A.
References:
1.  Sucipto, H., Kudo, F. and Eguchi, T. The last step of kanamycin biosynthesis: unique deamination reaction catalyzed by the α-ketoglutarate-dependent nonheme iron dioxygenase KanJ and the NADPH-dependent reductase KanK. Angew. Chem. Int. Ed. Engl. 51 (2012) 3428–3431. [PMID: 22374809]
[EC 1.1.1.355 created 2013]
 
 
EC 1.1.1.356     
Accepted name: GDP-L-colitose synthase
Reaction: GDP-β-L-colitose + NAD(P)+ = GDP-4-dehydro-3,6-dideoxy-α-D-mannose + NAD(P)H + H+
Glossary: L-colitose = 3,6-dideoxy-L-xylo-hexopyranose
GDP-4-dehydro-3,6-dideoxy-α-D-mannose = GDP-3,6-dideoxy-α-D-threo-hexopyranos-4-ulose
Other name(s): ColC
Systematic name: GDP-β-L-colitose:NAD(P)+ 4-oxidoreductase (5-epimerizing)
Comments: The enzyme is involved in biosynthesis of L-colitose, a 3,6-dideoxyhexose found in the O-antigen of Gram-negative lipopolysaccharides, where it catalyses the reaction in the reverse direction. The enzyme also performs the NAD(P)H-dependent epimerisation at C-5 of the sugar. The enzyme from Yersinia pseudotuberculosis is Si-specific with respect to NAD(P)H [1].
References:
1.  Alam, J., Beyer, N. and Liu, H.W. Biosynthesis of colitose: expression, purification, and mechanistic characterization of GDP-4-keto-6-deoxy-D-mannose-3-dehydrase (ColD) and GDP-L-colitose synthase (ColC). Biochemistry 43 (2004) 16450–16460. [PMID: 15610039]
[EC 1.1.1.356 created 2013]
 
 
EC 1.1.1.357     
Accepted name: 3α-hydroxysteroid 3-dehydrogenase
Reaction: a 3α-hydroxysteroid + NAD(P)+ = a 3-oxosteroid + NAD(P)H + H+
Other name(s): 3α-hydroxysteroid dehydrogenase; AKR1C4 (gene name); AKR1C2 (gene name); hsdA (gene name)
Systematic name: 3α-hydroxysteroid:NAD(P)+ 3-oxidoreductase
Comments: The enzyme acts on multiple 3α-hydroxysteroids, such as androsterone and 5 α-dihydrotestosterone. The mammalian enzymes are involved in inactivation of steroid hormones, while the bacterial enzymes are involved in steroid degradation. This entry stands for enzymes whose stereo-specificity with respect to NAD+ or NADP+ is not known. [cf. EC 1.1.1.50, 3α-hydroxysteroid 3-dehydrogenase (Si-specific) and EC 1.1.1.213, 3α-hydroxysteroid 3-dehydrogenase (Re-specific)].
References:
1.  Deyashiki, Y., Ogasawara, A., Nakayama, T., Nakanishi, M., Miyabe, Y., Sato, K. and Hara, A. Molecular cloning of two human liver 3 α-hydroxysteroid/dihydrodiol dehydrogenase isoenzymes that are identical with chlordecone reductase and bile-acid binder. Biochem. J. 299 (1994) 545–552. [PMID: 8172617]
2.  Khanna, M., Qin, K.N., Wang, R.W. and Cheng, K.C. Substrate specificity, gene structure, and tissue-specific distribution of multiple human 3 α-hydroxysteroid dehydrogenases. J. Biol. Chem. 270 (1995) 20162–20168. [PMID: 7650035]
3.  Oppermann, U.C. and Maser, E. Characterization of a 3 α-hydroxysteroid dehydrogenase/carbonyl reductase from the gram-negative bacterium Comamonas testosteroni. Eur. J. Biochem. 241 (1996) 744–749. [PMID: 8944761]
4.  Mobus, E. and Maser, E. Molecular cloning, overexpression, and characterization of steroid-inducible 3α-hydroxysteroid dehydrogenase/carbonyl reductase from Comamonas testosteroni. A novel member of the short-chain dehydrogenase/reductase superfamily. J. Biol. Chem. 273 (1998) 30888–30896. [PMID: 9812981]
5.  Nahoum, V., Gangloff, A., Legrand, P., Zhu, D.W., Cantin, L., Zhorov, B.S., Luu-The, V., Labrie, F., Breton, R. and Lin, S.X. Structure of the human 3α-hydroxysteroid dehydrogenase type 3 in complex with testosterone and NADP at 1.25-Å resolution. J. Biol. Chem. 276 (2001) 42091–42098. [PMID: 11514561]
[EC 1.1.1.357 created 2013]
 
 
EC 1.1.1.358     
Accepted name: 2-dehydropantolactone reductase
Reaction: (R)-pantolactone + NADP+ = 2-dehydropantolactone + NADPH + H+
Other name(s): 2-oxopantoyl lactone reductase; 2-ketopantoyl lactone reductase; ketopantoyl lactone reductase; 2-dehydropantoyl-lactone reductase
Systematic name: (R)-pantolactone:NADP+ oxidoreductase
Comments: The enzyme participates in an alternative pathway for biosynthesis of (R)-pantothenate (vitamin B5). This entry covers enzymes whose stereo specificity for NADP+ is not known. cf. EC 1.1.1.168 2-dehydropantolactone reductase (Re-specific) and EC 1.1.1.214, 2-dehydropantolactone reductase (Si-specific).
References:
1.  Hata, H., Shimizu, S., Hattori, S. and Yamada, H. Ketopantoyl-lactone reductase from Candida parapsilosis: purification and characterization as a conjugated polyketone reductase. Biochim. Biophys. Acta 990 (1989) 175–181. [PMID: 2644973]
[EC 1.1.1.358 created 2013]
 
 
EC 1.1.1.359     
Accepted name: aldose 1-dehydrogenase [NAD(P)+]
Reaction: an aldopyranose + NAD(P)+ = an aldono-1,5-lactone + NAD(P)H + H+
Systematic name: an aldopyranose:NAD(P)+ 1-oxidoreductase
Comments: The enzyme from the archaeon Sulfolobus solfataricus shows broad specificity towards aldoses (D-glucose, D-galactose, D-xylose, L-arabinose, 6-deoxy-D-glucose, D-fucose) and can utilize NAD+ and NADP+ with similar catalytic efficiency. It is involved in aldose catabolism via the branched variant of the Entner-Doudoroff pathway.
References:
1.  Giardina, P., de Biasi, M.G., de Rosa, M., Gambacorta, A. and Buonocore, V. Glucose dehydrogenase from the thermoacidophilic archaebacterium Sulfolobus solfataricus. Biochem. J. 239 (1986) 517–522. [PMID: 3827812]
2.  Smith, L.D., Budgen, N., Bungard, S.J., Danson, M.J. and Hough, D.W. Purification and characterization of glucose dehydrogenase from the thermoacidophilic archaebacterium Thermoplasma acidophilum. Biochem. J. 261 (1989) 973–977. [PMID: 2803257]
3.  Lamble, H.J., Heyer, N.I., Bull, S.D., Hough, D.W. and Danson, M.J. Metabolic pathway promiscuity in the archaeon Sulfolobus solfataricus revealed by studies on glucose dehydrogenase and 2-keto-3-deoxygluconate aldolase. J. Biol. Chem. 278 (2003) 34066–34072. [PMID: 12824170]
4.  Theodossis, A., Milburn, C.C., Heyer, N.I., Lamble, H.J., Hough, D.W., Danson, M.J. and Taylor, G.L. Preliminary crystallographic studies of glucose dehydrogenase from the promiscuous Entner-Doudoroff pathway in the hyperthermophilic archaeon Sulfolobus solfataricus. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 61 (2005) 112–115. [PMID: 16508107]
5.  Milburn, C.C., Lamble, H.J., Theodossis, A., Bull, S.D., Hough, D.W., Danson, M.J. and Taylor, G.L. The structural basis of substrate promiscuity in glucose dehydrogenase from the hyperthermophilic archaeon Sulfolobus solfataricus. J. Biol. Chem. 281 (2006) 14796–14804. [PMID: 16556607]
6.  Haferkamp, P., Kutschki, S., Treichel, J., Hemeda, H., Sewczyk, K., Hoffmann, D., Zaparty, M. and Siebers, B. An additional glucose dehydrogenase from Sulfolobus solfataricus: fine-tuning of sugar degradation. Biochem. Soc. Trans. 39 (2011) 77–81. [PMID: 21265750]
[EC 1.1.1.359 created 2013]
 
 
EC 1.1.1.360     
Accepted name: glucose/galactose 1-dehydrogenase
Reaction: (1) D-glucopyranose + NADP+ = D-glucono-1,5-lactone + NADPH + H+
(2) D-galactopyranose + NADP+ = D-galactono-1,5-lactone + NADPH + H+
Other name(s): GdhA; dual-specific glucose/galactose dehydrogenase; glucose (galactose) dehydrogenase; glucose/galactose dehydrogenase
Systematic name: D-glucose/D-galactose 1-dehydrogenase (NADPH)
Comments: A zinc protein. The enzyme from the archaeon Picrophilus torridus is involved in glucose and galactose catabolism via the nonphosphorylative variant of the Entner-Doudoroff pathway. It shows 20-fold higher activity with NADP+ compared to NAD+. The oxidation of D-glucose and D-galactose is catalysed at a comparable rate (cf. EC 1.1.1.119, glucose 1-dehydrogenase (NADP+) and EC 1.1.1.120, galactose 1-dehydrogenase (NADP+)).
References:
1.  Angelov, A., Futterer, O., Valerius, O., Braus, G.H. and Liebl, W. Properties of the recombinant glucose/galactose dehydrogenase from the extreme thermoacidophile, Picrophilus torridus. FEBS J. 272 (2005) 1054–1062. [PMID: 15691337]
2.  Milburn, C.C., Lamble, H.J., Theodossis, A., Bull, S.D., Hough, D.W., Danson, M.J. and Taylor, G.L. The structural basis of substrate promiscuity in glucose dehydrogenase from the hyperthermophilic archaeon Sulfolobus solfataricus. J. Biol. Chem. 281 (2006) 14796–14804. [PMID: 16556607]
[EC 1.1.1.360 created 2013]
 
 
EC 1.1.1.361     
Accepted name: glucose-6-phosphate 3-dehydrogenase
Reaction: D-glucose 6-phosphate + NAD+ = 3-dehydro-D-glucose 6-phosphate + NADH + H+
Glossary: kanosamine = 3-amino-3-deoxy-D-glucose
Other name(s): ntdC (gene name)
Systematic name: D-glucose-6-phosphate:NAD+ oxidoreductase
Comments: The enzyme, found in the bacterium Bacillus subtilis, is involved in a kanosamine biosynthesis pathway.
References:
1.  Vetter, N.D., Langill, D.M., Anjum, S., Boisvert-Martel, J., Jagdhane, R.C., Omene, E., Zheng, H., van Straaten, K.E., Asiamah, I., Krol, E.S., Sanders, D.A. and Palmer, D.R. A previously unrecognized kanosamine biosynthesis pathway in Bacillus subtilis. J. Am. Chem. Soc. 135 (2013) 5970–5973. [PMID: 23586652]
[EC 1.1.1.361 created 2013]
 
 
EC 1.1.1.362     
Accepted name: aklaviketone reductase
Reaction: aklavinone + NADP+ = aklaviketone + NADPH + H+
Glossary: aklavinone = methyl (1R,2R,4S)-2-ethyl-2,4,5,7-tetrahydroxy-6,11-dioxo-1,2,3,4,6,11-hexahydrotetracene-1-carboxylate
aklaviketone = methyl (1R,2R)-2-ethyl-2,5,7-trihydroxy-4,6,11-trioxo-1,2,3,4,6,11-hexahydrotetracene-1-carboxylate
Other name(s): dauE (gene name); aknU (gene name)
Systematic name: aklavinone:NADP+ oxidoreductase
Comments: The enzyme is involved in the synthesis of the aklavinone aglycone, a common precursor for several anthracycline antibiotics including aclacinomycins, daunorubicin and doxorubicin. The enzyme from the Gram-negative bacterium Streptomyces sp. C5 produces daunomycin.
References:
1.  Dickens, M.L., Ye, J. and Strohl, W.R. Cloning, sequencing, and analysis of aklaviketone reductase from Streptomyces sp. strain C5. J. Bacteriol. 178 (1996) 3384–3388. [PMID: 8655529]
[EC 1.1.1.362 created 2013]
 
 
EC 1.1.1.363     
Accepted name: glucose-6-phosphate dehydrogenase [NAD(P)+]
Reaction: D-glucose 6-phosphate + NAD(P)+ = 6-phospho-D-glucono-1,5-lactone + NAD(P)H + H+
Other name(s): G6PDH; G6PD; Glc6PD
Systematic name: D-glucose-6-phosphate:NAD(P)+ 1-oxidoreductase
Comments: The enzyme catalyses a step of the pentose phosphate pathway. The enzyme from the Gram-positive bacterium Leuconostoc mesenteroides prefers NADP+ while the enzyme from the Gram-negative bacterium Gluconacetobacter xylinus prefers NAD+. cf. EC 1.1.1.49, glucose-6-phosphate dehydrogenase (NADP+) and EC 1.1.1.388, glucose-6-phosphate dehydrogenase (NAD+).
References:
1.  Olive, C., Geroch, M.E. and Levy, H.R. Glucose 6-phosphate dehydrogenase from Leuconostoc mesenteroides. Kinetic studies. J. Biol. Chem. 246 (1971) 2047–2057. [PMID: 4396688]
2.  Lee, W.T. and Levy, H.R. Lysine-21 of Leuconostoc mesenteroides glucose 6-phosphate dehydrogenase participates in substrate binding through charge-charge interaction. Protein Sci. 1 (1992) 329–334. [PMID: 1304341]
3.  Cosgrove, M.S., Naylor, C., Paludan, S., Adams, M.J. and Levy, H.R. On the mechanism of the reaction catalyzed by glucose 6-phosphate dehydrogenase. Biochemistry 37 (1998) 2759–2767. [PMID: 9485426]
4.  Ragunathan, S. and Levy, H.R. Purification and characterization of the NAD-preferring glucose 6-phosphate dehydrogenase from Acetobacter hansenii (Acetobacter xylinum). Arch. Biochem. Biophys. 310 (1994) 360–366. [PMID: 8179320]
[EC 1.1.1.363 created 2013, modified 2015]
 
 
EC 1.1.1.364     
Accepted name: dTDP-4-dehydro-6-deoxy-α-D-gulose 4-ketoreductase
Reaction: dTDP-6-deoxy-α-D-allose + NAD(P)+ = dTDP-4-dehydro-6-deoxy-α-D-gulose + NAD(P)H + H+
Glossary: dTDP-4-dehydro-6-deoxy-α-D-gulose = dTDP-4-dehydro-6-deoxy-α-D-allose
Other name(s): dTDP-4-dehydro-6-deoxygulose reductase; tylD (gene name); gerKI (gene name); chmD (gene name); mydI (gene name)
Systematic name: dTDP-6-deoxy-α-D-allose:NAD(P)+ oxidoreductase
Comments: The enzyme forms an activated deoxy-α-D-allose, which is converted to mycinose after attachment to the aglycones of several macrolide antibiotics, including tylosin, chalcomycin, dihydrochalcomycin, and mycinamicin II.
References:
1.  Bate, N. and Cundliffe, E. The mycinose-biosynthetic genes of Streptomyces fradiae, producer of tylosin. J Ind Microbiol Biotechnol 23 (1999) 118–122. [PMID: 10510490]
2.  Anzai, Y., Saito, N., Tanaka, M., Kinoshita, K., Koyama, Y. and Kato, F. Organization of the biosynthetic gene cluster for the polyketide macrolide mycinamicin in Micromonospora griseorubida. FEMS Microbiol. Lett. 218 (2003) 135–141. [PMID: 12583909]
3.  Thuy, T.T., Liou, K., Oh, T.J., Kim, D.H., Nam, D.H., Yoo, J.C. and Sohng, J.K. Biosynthesis of dTDP-6-deoxy-β-D-allose, biochemical characterization of dTDP-4-keto-6-deoxyglucose reductase (GerKI) from Streptomyces sp. KCTC 0041BP. Glycobiology 17 (2007) 119–126. [PMID: 17053005]
4.  Kubiak, R.L., Phillips, R.K., Zmudka, M.W., Ahn, M.R., Maka, E.M., Pyeatt, G.L., Roggensack, S.J. and Holden, H.M. Structural and functional studies on a 3′-epimerase involved in the biosynthesis of dTDP-6-deoxy-D-allose. Biochemistry 51 (2012) 9375–9383. [PMID: 23116432]
[EC 1.1.1.364 created 2013]
 
 
EC 1.1.1.365     
Accepted name: D-galacturonate reductase
Reaction: L-galactonate + NADP+ = D-galacturonate + NADPH + H+
Other name(s): GalUR; gar1 (gene name)
Systematic name: L-galactonate:NADP+ oxidoreductase
Comments: The enzyme from plants is involved in ascorbic acid (vitamin C) biosynthesis [1,2]. The enzyme from the fungus Trichoderma reesei (Hypocrea jecorina) is involved in a eukaryotic degradation pathway of D-galacturonate. It is also active with D-glucuronate and glyceraldehyde [3]. Neither enzyme shows any activity with NADH.
References:
1.  Isherwood, F.A. and Mapson, L.W. Biological synthesis of ascorbic acid: the conversion of derivatives of D-galacturonic acid into L-ascorbic acid by plant extracts. Biochem. J. 64 (1956) 13–22. [PMID: 13363799]
2.  Agius, F., Gonzalez-Lamothe, R., Caballero, J.L., Munoz-Blanco, J., Botella, M.A. and Valpuesta, V. Engineering increased vitamin C levels in plants by overexpression of a D-galacturonic acid reductase. Nat. Biotechnol. 21 (2003) 177–181. [PMID: 12524550]
3.  Kuorelahti, S., Kalkkinen, N., Penttila, M., Londesborough, J. and Richard, P. Identification in the mold Hypocrea jecorina of the first fungal D-galacturonic acid reductase. Biochemistry 44 (2005) 11234–11240. [PMID: 16101307]
4.  Martens-Uzunova, E.S. and Schaap, P.J. An evolutionary conserved D-galacturonic acid metabolic pathway operates across filamentous fungi capable of pectin degradation. Fungal Genet. Biol. 45 (2008) 1449–1457. [PMID: 18768163]
[EC 1.1.1.365 created 2013]
 
 
EC 1.1.1.366     
Accepted name: L-idonate 5-dehydrogenase (NAD+)
Reaction: L-idonate + NAD+ = 5-dehydro-D-gluconate + NADH + H+
Systematic name: L-idonate:NAD+ oxidoreductase
Comments: Involved in the catabolism of ascorbate (vitamin C) to tartrate. No activity is observed with NADP+ (cf. EC 1.1.1.264, L-idonate 5-dehydrogenase).
References:
1.  DeBolt, S., Cook, D.R. and Ford, C.M. L-Tartaric acid synthesis from vitamin C in higher plants. Proc. Natl. Acad. Sci. USA 103 (2006) 5608–5613. [PMID: 16567629]
[EC 1.1.1.366 created 2013]
 
 
EC 1.1.1.367     
Accepted name: UDP-2-acetamido-2,6-β-L-arabino-hexul-4-ose reductase
Reaction: UDP-2-acetamido-2,6-dideoxy-β-L-talose + NAD(P)+ = UDP-2-acetamido-2,6-β-L-arabino-hexul-4-ose + NAD(P)H + H+
Glossary: UDP-2-acetamido-2,6-dideoxy-β-L-talose = UDP-N-acetyl-β-L-pneumosamine
Other name(s): WbjC; Cap5F
Systematic name: UDP-2-acetamido-2,6-dideoxy-L-talose:NADP+ oxidoreductase
Comments: Part of the biosynthesis of UDP-N-acetyl-L-fucosamine. Isolated from the bacteria Pseudomonas aeruginosa and Staphylococcus aureus.
References:
1.  Kneidinger, B., O'Riordan, K., Li, J., Brisson, J.R., Lee, J.C. and Lam, J.S. Three highly conserved proteins catalyze the conversion of UDP-N-acetyl-D-glucosamine to precursors for the biosynthesis of O antigen in Pseudomonas aeruginosa O11 and capsule in Staphylococcus aureus type 5. Implications for the UDP-N-acetyl-L-fucosamine biosynthetic pathway. J. Biol. Chem. 278 (2003) 3615–3627. [PMID: 12464616]
2.  Mulrooney, E.F., Poon, K.K., McNally, D.J., Brisson, J.R. and Lam, J.S. Biosynthesis of UDP-N-acetyl-L-fucosamine, a precursor to the biosynthesis of lipopolysaccharide in Pseudomonas aeruginosa serotype O11. J. Biol. Chem. 280 (2005) 19535–19542. [PMID: 15778500]
3.  Miyafusa, T., Tanaka, Y., Kuroda, M., Ohta, T. and Tsumoto, K. Expression, purification, crystallization and preliminary diffraction analysis of CapF, a capsular polysaccharide-synthesis enzyme from Staphylococcus aureus. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 64 (2008) 512–515. [PMID: 18540063]
[EC 1.1.1.367 created 2014]
 
 
EC 1.1.1.368     
Accepted name: 6-hydroxycyclohex-1-ene-1-carbonyl-CoA dehydrogenase
Reaction: 6-hydroxycyclohex-1-ene-1-carbonyl-CoA + NAD+ = 6-oxocyclohex-1-ene-1-carbonyl-CoA + NADH + H+
Systematic name: 6-hydroxycyclohex-1-ene-1-carbonyl-CoA:NAD+ 6-oxidoreductase
Comments: The enzyme participates in the central benzoyl-CoA degradation pathway of some anaerobic bacteria such as Thauera aromatica.
References:
1.  Laempe, D., Jahn, M. and Fuchs, G. 6-Hydroxycyclohex-1-ene-1-carbonyl-CoA dehydrogenase and 6-oxocyclohex-1-ene-1-carbonyl-CoA hydrolase, enzymes of the benzoyl-CoA pathway of anaerobic aromatic metabolism in the denitrifying bacterium Thauera aromatica. Eur. J. Biochem. 263 (1999) 420–429. [PMID: 10406950]
[EC 1.1.1.368 created 2014]
 
 
EC 1.1.1.369     
Accepted name: D-chiro-inositol 1-dehydrogenase
Reaction: 1D-chiro-inositol + NAD+ = 2D-2,3,5/4,6-pentahydroxycyclohexanone + NADH + H+
Glossary: 1D-chiro-inositol = 1,2,4/3,5,6-cyclohexane-1,2,3,4,5,6-hexol
Other name(s): DCI 1-dehydrogenase; IolG
Systematic name: 1D-chiro-inositol:NAD+ 1-oxidoreductase
Comments: The enzyme, found in the bacterium Bacillus subtilis, also catalyses the reaction of EC 1.1.1.18, inositol 2-dehydrogenase, and can also use D-glucose and D-xylose. It shows trace activity with D-ribose and D-fructose [1]. It is part of a myo-inositol/D-chiro-inositol degradation pathway leading to acetyl-CoA.
References:
1.  Ramaley, R., Fujita, Y. and Freese, E. Purification and properties of Bacillus subtilis inositol dehydrogenase. J. Biol. Chem. 254 (1979) 7684–7690. [PMID: 112095]
2.  Yoshida, K., Yamaguchi, M., Morinaga, T., Ikeuchi, M., Kinehara, M. and Ashida, H. Genetic modification of Bacillus subtilis for production of D-chiro-inositol, an investigational drug candidate for treatment of type 2 diabetes and polycystic ovary syndrome. Appl. Environ. Microbiol. 72 (2006) 1310–1315. [PMID: 16461681]
[EC 1.1.1.369 created 2014]
 
 
EC 1.1.1.370     
Accepted name: scyllo-inositol 2-dehydrogenase (NAD+)
Reaction: scyllo-inositol + NAD+ = 2,4,6/3,5-pentahydroxycyclohexanone + NADH + H+
Glossary: 2,4,6/3,5-pentahydroxycyclohexanone = (2R,3S,4s,5R,6S)-2,3,4,5,6-pentahydroxycyclohexanone = scyllo-inosose
Other name(s): iolX (gene name)
Systematic name: scyllo-inositol:NAD+ 2-oxidoreductase
Comments: The enzyme, found in the bacterium Bacillus subtilis, has no activity with NADP+ [cf. EC 1.1.1.371, scyllo-inositol 2-dehydrogenase (NADP+)]. It is part of a scyllo-inositol degradation pathway leading to acetyl-CoA.
References:
1.  Morinaga, T., Ashida, H. and Yoshida, K. Identification of two scyllo-inositol dehydrogenases in Bacillus subtilis. Microbiology 156 (2010) 1538–1546. [PMID: 20133360]
[EC 1.1.1.370 created 2014]
 
 
EC 1.1.1.371     
Accepted name: scyllo-inositol 2-dehydrogenase (NADP+)
Reaction: scyllo-inositol + NADP+ = 2,4,6/3,5-pentahydroxycyclohexanone + NADPH + H+
Glossary: 2,4,6/3,5-pentahydroxycyclohexanone = (2R,3S,4s,5R,6S)-2,3,4,5,6-pentahydroxycyclohexanone = scyllo-inosose
Other name(s): iolW (gene name)
Systematic name: scyllo-inositol:NADP+ 2-oxidoreductase
Comments: The enzyme, found in the bacterium Bacillus subtilis, has no activity with NAD+ [cf. EC 1.1.1.370, scyllo-inositol 2-dehydrogenase (NAD+)].
References:
1.  Morinaga, T., Ashida, H. and Yoshida, K. Identification of two scyllo-inositol dehydrogenases in Bacillus subtilis. Microbiology 156 (2010) 1538–1546. [PMID: 20133360]
[EC 1.1.1.371 created 2014]
 
 
EC 1.1.1.372     
Accepted name: D/L-glyceraldehyde reductase
Reaction: (1) glycerol + NADP+ = L-glyceraldehyde + NADPH + H+
(2) glycerol + NADP+ = D-glyceraldehyde + NADPH + H+
Other name(s): gld1 (gene name); gaaD (gene name)
Systematic name: glycerol:NADP+ oxidoreductase (D/L-glyceraldehyde-forming)
Comments: The enzyme takes part in a D-galacturonate degradation pathway in the fungi Aspergillus niger and Trichoderma reesei (Hypocrea jecorina). It has equal activity with D- and L-glyceraldehyde, and can also reduce glyoxal and methylglyoxal. The reaction is only observed in the direction of glyceraldehyde reduction.
References:
1.  Liepins, J., Kuorelahti, S., Penttila, M. and Richard, P. Enzymes for the NADPH-dependent reduction of dihydroxyacetone and D-glyceraldehyde and L-glyceraldehyde in the mould Hypocrea jecorina. FEBS J. 273 (2006) 4229–4235. [PMID: 16930134]
2.  Martens-Uzunova, E.S. and Schaap, P.J. An evolutionary conserved D-galacturonic acid metabolic pathway operates across filamentous fungi capable of pectin degradation. Fungal Genet. Biol. 45 (2008) 1449–1457. [PMID: 18768163]
[EC 1.1.1.372 created 2014]
 
 
EC 1.1.1.373     
Accepted name: sulfolactaldehyde 3-reductase
Reaction: 2,3-dihydroxypropane-1-sulfonate + NAD+ = 2-hydroxy-3-oxopropane-1-sulfonate + NADH + H+
Glossary: 2-hydroxy-3-oxopropane-1-sulfonate = sulfolactaldehyde
Other name(s): yihU (gene name)
Systematic name: 2,3-dihydroxypropane-1-sulfonate:NAD+ 3-oxidoreductase
Comments: The enzyme, characterized from the bacterium Escherichia coli, is involved in the degradation pathway of sulfoquinovose, the polar headgroup of sulfolipids found in the photosynthetic membranes of all higher plants, mosses, ferns, algae, and most photosynthetic bacteria, as well as the surface layer of some archaea.
References:
1.  Denger, K., Weiss, M., Felux, A.K., Schneider, A., Mayer, C., Spiteller, D., Huhn, T., Cook, A.M. and Schleheck, D. Sulphoglycolysis in Escherichia coli K-12 closes a gap in the biogeochemical sulphur cycle. Nature 507 (2014) 114–117. [PMID: 24463506]
[EC 1.1.1.373 created 2014]
 
 
EC 1.1.1.374     
Accepted name: UDP-N-acetylglucosamine 3-dehydrogenase
Reaction: UDP-N-acetyl-α-D-glucosamine + NAD+ = UDP-2-acetamido-3-dehydro-2-deoxy-α-D-glucopyranose + NADH + H+
Systematic name: UDP-N-acetyl-α-D-glucosamine:NAD+ 3-oxidoreductase
Comments: The enzyme from the archaeon Methanococcus maripaludis is activated by KCl (200 mM).
References:
1.  Namboori, S.C. and Graham, D.E. Enzymatic analysis of uridine diphosphate N-acetyl-D-glucosamine. Anal. Biochem. 381 (2008) 94–100. [PMID: 18634748]
[EC 1.1.1.374 created 2014]
 
 
EC 1.1.1.375     
Accepted name: L-2-hydroxycarboxylate dehydrogenase [NAD(P)+]
Reaction: a (2S)-2-hydroxycarboxylate + NAD(P)+ = a 2-oxocarboxylate + NAD(P)H + H+
Other name(s): MdhII; lactate/malate dehydrogenase
Systematic name: (2S)-2-hydroxycarboxylate:NAD(P)+ oxidoreductase
Comments: The enzyme from the archaeon Methanocaldococcus jannaschii catalyses the reversible oxidation of (2R)-3-sulfolactate and (S)-malate to 3-sulfopyruvate and oxaloacetate, respectively (note that (2R)-3-sulfolactate has the same stereochemical configuration as (2S)-2-hydroxycarboxylates) [1]. The enzyme can use both NADH and NADPH, although activity is higher with NADPH [1-3]. The oxidation of (2R)-3-sulfolactate was observed only in the presence of NADP+ [1]. The same organism also possesses an NAD+-specific enzyme with similar activity, cf. EC 1.1.1.337, L-2-hydroxycarboxylate dehydrogenase (NAD+).
References:
1.  Graupner, M., Xu, H. and White, R.H. Identification of an archaeal 2-hydroxy acid dehydrogenase catalyzing reactions involved in coenzyme biosynthesis in methanoarchaea. J. Bacteriol. 182 (2000) 3688–3692. [PMID: 10850983]
2.  Lee, B.I., Chang, C., Cho, S.J., Eom, S.H., Kim, K.K., Yu, Y.G. and Suh, S.W. Crystal structure of the MJ0490 gene product of the hyperthermophilic archaebacterium Methanococcus jannaschii, a novel member of the lactate/malate family of dehydrogenases. J. Mol. Biol. 307 (2001) 1351–1362. [PMID: 11292347]
3.  Madern, D. The putative L-lactate dehydrogenase from Methanococcus jannaschii is an NADPH-dependent L-malate dehydrogenase. Mol. Microbiol. 37 (2000) 1515–1520. [PMID: 10998181]
[EC 1.1.1.375 created 2014]
 
 
EC 1.1.1.376     
Accepted name: L-arabinose 1-dehydrogenase [NAD(P)+]
Reaction: L-arabinose + NAD(P)+ = L-arabinono-1,4-lactone + NAD(P)H + H+
Other name(s): L-arabino-aldose dehydrogenase
Systematic name: L-arabinose:NAD(P)+ 1-oxidoreductase
Comments: The enzymes from the bacterium Azospirillum brasilense and the archaeon Haloferax volcanii are part of the L-arabinose degradation pathway and prefer NADP+ over NAD+. In vitro the enzyme from Azospirillum brasilense shows also high catalytic efficiency with D-galactose.
References:
1.  Novick, N.J. and Tyler, M.E. Partial purification and properties of an L-arabinose dehydrogenase from Azospirillum brasilense. Can. J. Microbiol. 29 (1983) 242–246.
2.  Watanabe, S., Kodaki, T. and Makino, K. Cloning, expression, and characterization of bacterial L-arabinose 1-dehydrogenase involved in an alternative pathway of L-arabinose metabolism. J. Biol. Chem. 281 (2006) 2612–2623. [PMID: 16326697]
3.  Johnsen, U., Sutter, J.M., Zaiss, H. and Schonheit, P. L-Arabinose degradation pathway in the haloarchaeon Haloferax volcanii involves a novel type of L-arabinose dehydrogenase. Extremophiles 17 (2013) 897–909. [PMID: 23949136]
[EC 1.1.1.376 created 2014]
 
 
EC 1.1.1.377     
Accepted name: L-rhamnose 1-dehydrogenase (NADP+)
Reaction: L-rhamnose + NADP+ = L-rhamnono-1,4-lactone + NADPH + H+
Systematic name: L-rhamnose:NADP+ 1-oxidoreductase
Comments: The enzyme from the archaeon Thermoplasma acidophilum is part of the non-phosphorylative degradation pathway for L-rhamnose. The enzyme differs in cofactor specificity from EC 1.1.1.173, L-rhamnose 1-dehydrogenase, which is specific for NAD+.
References:
1.  Kim, S.M., Paek, K.H. and Lee, S.B. Characterization of NADP+-specific L-rhamnose dehydrogenase from the thermoacidophilic Archaeon Thermoplasma acidophilum. Extremophiles 16 (2012) 447–454. [PMID: 22481639]
[EC 1.1.1.377 created 2014]
 
 
EC 1.1.1.378     
Accepted name: L-rhamnose 1-dehydrogenase [NAD(P)+]
Reaction: L-rhamnose + NAD(P)+ = L-rhamnono-1,4-lactone + NAD(P)H + H+
Systematic name: L-rhamnose:NAD(P)+ 1-oxidoreductase
Comments: The enzyme, which occurs in the bacteria Azotobacter vinelandii and Sphingomonas sp. SKA58, is part of the non-phosphorylative degradation pathway for L-rhamnose. The enzyme differs in cofactor specificity from EC 1.1.1.173, L-rhamnose 1-dehydrogenase, which is specific for NAD+ and EC 1.1.1.377, L-rhamnose 1-dehydrogenase (NADP+).
References:
1.  Watanabe, S., Saimura, M. and Makino, K. Eukaryotic and bacterial gene clusters related to an alternative pathway of nonphosphorylated L-rhamnose metabolism. J. Biol. Chem. 283 (2008) 20372–20382. [PMID: 18505728]
2.  Watanabe, S. and Makino, K. Novel modified version of nonphosphorylated sugar metabolism - an alternative L-rhamnose pathway of Sphingomonas sp. FEBS J. 276 (2009) 1554–1567. [PMID: 19187228]
[EC 1.1.1.378 created 2014]
 
 
EC 1.1.1.379     
Accepted name: (R)-mandelate dehydrogenase
Reaction: (R)-mandelate + NAD+ = phenylglyoxylate + NADH + H+
Glossary: (R)-mandelate = D-mandelate
Other name(s): ManDH2; D-ManDH2; D-mandelate dehydrogenase (ambiguous)
Systematic name: (R)-mandelate:NAD+ 2-oxidoreductase
Comments: The enzyme, found in bacteria and fungi, can also accept a number of substituted mandelate derivatives, such as 3-hydroxymandelate, 4-hydroxymandelate, 2-methoxymandelate, 4-hydroxy-3-methoxymandelate and 3-hydroxy-4-methoxymandelate. The enzyme has no activity with (S)-mandelate (cf. EC 1.1.99.31, (S)-mandelate dehydrogenase) [1,2]. The enzyme transfers the pro-R-hydrogen from NADH [2].
References:
1.  Baker, D.P. and Fewson, C.A. Purification and characterization of D(–)-mandelate dehydrogenase from Rhodotorula graminis. Microbiology 135 (1989) 2035–2044.
2.  Baker, D.P., Kleanthous, C., Keen, J.N., Weinhold, E. and Fewson, C.A. Mechanistic and active-site studies on D(–)-mandelate dehydrogenase from Rhodotorula graminis. Biochem. J. 281 (1992) 211–218. [PMID: 1731758]
[EC 1.1.1.379 created 2014]
 
 
EC 1.1.1.380     
Accepted name: L-gulonate 5-dehydrogenase
Reaction: L-gulonate + NAD+ = D-fructuronate + NADH + H+
Glossary: D-fructuronate = D-arabino-hexuronate
Systematic name: L-gulonate:NAD+ 5-oxidoreductase
Comments: The enzyme, characterized from the bacterium Halomonas elongata, participates in a pathway for L-gulonate degradation.
References:
1.  Cooper, R.A. The pathway for L-gulonate catabolism in Escherichia coli K-12 and Salmonella typhimurium LT-2. FEBS Lett. 115 (1980) 63–67. [PMID: 6993236]
2.  Wichelecki, D.J., Vendiola, J.A., Jones, A.M., Al-Obaidi, N., Almo, S.C. and Gerlt, J.A. Investigating the physiological roles of low-efficiency D-mannonate and D-gluconate dehydratases in the enolase superfamily: pathways for the catabolism of L-gulonate and L-idonate. Biochemistry 53 (2014) 5692–5699. [PMID: 25145794]
[EC 1.1.1.380 created 2014]
 
 
EC 1.1.1.381     
Accepted name: 3-hydroxy acid dehydrogenase
Reaction: L-allo-threonine + NADP+ = aminoacetone + CO2 + NADPH + H+ (overall reaction)
(1a) L-allo-threonine + NADP+ = L-2-amino-3-oxobutanoate + NADPH + H+
(1b) L-2-amino-3-oxobutanoate = aminoacetone + CO2 (spontaneous)
Glossary: L-allo-threonine = (2S,3S)-2-amino-3-hydroxybutanoic acid
aminoacetone = 1-aminopropan-2-one
L-2-amino-3-oxobutanoate = (2S)-2-amino-3-oxobutanoate
Other name(s): ydfG (gene name); YMR226c (gene name)
Systematic name: L-allo-threonine:NADP+ 3-oxidoreductase
Comments: The enzyme, purified from the bacterium Escherichia coli and the yeast Saccharomyces cerevisiae, shows activity with a range of 3- and 4-carbon 3-hydroxy acids. The highest activity is seen with L-allo-threonine and D-threonine. The enzyme from Escherichia coli also shows high activity with L-serine, D-serine, (S)-3-hydroxy-2-methylpropanoate and (R)-3-hydroxy-2-methylpropanoate. The enzyme has no activity with NAD+ or L-threonine (cf. EC 1.1.1.103, L-threonine 3-dehydrogenase).
References:
1.  Fujisawa, H., Nagata, S. and Misono, H. Characterization of short-chain dehydrogenase/reductase homologues of Escherichia coli (YdfG) and Saccharomyces cerevisiae (YMR226C). Biochim. Biophys. Acta 1645 (2003) 89–94. [PMID: 12535615]
[EC 1.1.1.381 created 2014, modified 2015]
 
 
EC 1.1.1.382     
Accepted name: ketol-acid reductoisomerase (NAD+)
Reaction: (2R)-2,3-dihydroxy-3-methylbutanoate + NAD+ = (2S)-2-hydroxy-2-methyl-3-oxobutanoate + NADH + H+
Glossary: (2S)-2-hydroxy-2-methyl-3-oxobutanoate = (2S)-2-acetolactate
Systematic name: (2R)-2,3-dihydroxy-3-methylbutanoate:NAD+ oxidoreductase (isomerizing)
Comments: The enzyme, characterized from the bacteria Thermacetogenium phaeum and Desulfococcus oleovorans and from the archaeon Archaeoglobus fulgidus, is specific for NADH [cf. EC 1.1.1.86, ketol-acid reductoisomerase (NADP+) and EC 1.1.1.383, ketol-acid reductoisomerase [NAD(P)+]].
References:
1.  Brinkmann-Chen, S., Cahn, J.K. and Arnold, F.H. Uncovering rare NADH-preferring ketol-acid reductoisomerases. Metab. Eng. 26C (2014) 17–22. [PMID: 25172159]
[EC 1.1.1.382 created 2015]
 
 
EC 1.1.1.383     
Accepted name: ketol-acid reductoisomerase [NAD(P)+]
Reaction: (2R)-2,3-dihydroxy-3-methylbutanoate + NAD(P)+ = (2S)-2-hydroxy-2-methyl-3-oxobutanoate + NAD(P)H + H+
Glossary: (2S)-2-hydroxy-2-methyl-3-oxobutanoate = (2S)-2-acetolactate
Systematic name: (2R)-2,3-dihydroxy-3-methylbutanoate:NAD(P)+ oxidoreductase (isomerizing)
Comments: The enzyme, characterized from the bacteria Hydrogenobaculum sp. and Syntrophomonas wolfei subsp. wolfei and from the archaea Metallosphaera sedula and Ignisphaera aggregans, can use both NADH and NADPH with similar efficiency [cf. EC 1.1.1.86, ketol-acid reductoisomerase (NADP+) and EC 1.1.1.382, ketol-acid reductoisomerase (NAD+)].
References:
1.  Brinkmann-Chen, S., Cahn, J.K. and Arnold, F.H. Uncovering rare NADH-preferring ketol-acid reductoisomerases. Metab. Eng. 26C (2014) 17–22. [PMID: 25172159]
[EC 1.1.1.383 created 2015]
 
 
EC 1.1.1.384     
Accepted name: dTDP-3,4-didehydro-2,6-dideoxy-α-D-glucose 3-reductase
Reaction: dTDP-4-dehydro-2,6-dideoxy-α-D-glucose + NADP+ = dTDP-3,4-didehydro-2,6-dideoxy-α-D-glucose + NADPH + H+
Glossary: dTDP-4-dehydro-2,6-dideoxy-α-D-glucose = dTDP-2,6-dideoxy-α-D-threo-hexopyranos-4-ulose
dTDP-3,4-didehydro-2,6-dideoxy-α-D-glucose = thymidine 5′-[(2R,6R)-6-methyl-4,5-dioxotetrahydro-2H-pyran-2-yl] diphosphate
Other name(s): KijD10; dTDP-4-keto-2,6-dideoxy-D-glucose 3-oxidoreductase; dTDP-4-dehydro-2,6-dideoxy-α-D-glucose 3-oxidoreductase
Systematic name: dTDP-4-dehydro-2,6-dideoxy-α-D-glucose:NADP+ 3-oxidoreductase
Comments: The enzyme is involved in the biosynthesis of several deoxysugars, including L-digitoxose, L- and D-olivose, L-oliose, D-mycarose and forosamine.
References:
1.  Aguirrezabalaga, I., Olano, C., Allende, N., Rodriguez, L., Brana, A.F., Mendez, C. and Salas, J.A. Identification and expression of genes involved in biosynthesis of L-oleandrose and its intermediate L-olivose in the oleandomycin producer Streptomyces antibioticus. Antimicrob. Agents Chemother. 44 (2000) 1266–1275. [PMID: 10770761]
2.  Wang, L., White, R.L. and Vining, L.C. Biosynthesis of the dideoxysugar component of jadomycin B: genes in the jad cluster of Streptomyces venezuelae ISP5230 for L-digitoxose assembly and transfer to the angucycline aglycone. Microbiology 148 (2002) 1091–1103. [PMID: 11932454]
3.  Hong, L., Zhao, Z., Melancon, C.E., 3rd, Zhang, H. and Liu, H.W. In vitro characterization of the enzymes involved in TDP-D-forosamine biosynthesis in the spinosyn pathway of Saccharopolyspora spinosa. J. Am. Chem. Soc. 130 (2008) 4954–4967. [PMID: 18345667]
4.  Kubiak, R.L. and Holden, H.M. Combined structural and functional investigation of a C-3′′-ketoreductase involved in the biosynthesis of dTDP-L-digitoxose. Biochemistry 50 (2011) 5905–5917. [PMID: 21598943]
[EC 1.1.1.384 created 2015]
 
 
EC 1.1.1.385     
Accepted name: dihydroanticapsin dehydrogenase
Reaction: L-dihydroanticapsin + NAD+ = L-anticapsin + NADH + H+
Glossary: L-dihydroanticapsin = 3-[(1R,2S,5R,6S)-5-hydroxy-7-oxabicyclo[4.1.0]hept-2-yl]-L-alanine
L-anticapsin = 3-[(1R,2S,6R)-5-oxo-7-oxabicyclo[4.1.0]hept-2-yl]-L-alanine
Other name(s): BacC; ywfD (gene name)
Systematic name: L-dihydroanticapsin:NAD+ oxidoreductase
Comments: The enzyme, characterized from the bacterium Bacillus subtilis, is involved in the biosynthesis of the nonribosomally synthesized dipeptide antibiotic bacilysin, composed of L-alanine and L-anticapsin.
References:
1.  Parker, J.B. and Walsh, C.T. Action and timing of BacC and BacD in the late stages of biosynthesis of the dipeptide antibiotic bacilysin. Biochemistry 52 (2013) 889–901. [PMID: 23317005]
[EC 1.1.1.385 created 2015]
 
 
EC 1.1.1.386     
Accepted name: ipsdienol dehydrogenase
Reaction: (R)-ipsdienol + NAD(P)+ = ipsdienone + NAD(P)H + H+
Glossary: ipsdienone = 2-methyl-6-methyleneocta-2,7-dien-4-one
(R)-ipsdienol = (4R)-2-methyl-6-methyleneocta-2,7-dien-4-ol
Other name(s): IDOLDH
Systematic name: (R)-ipsdienol:NAD(P)+ oxidoreductase
Comments: The enzyme is involved in pheromone production by the pine engraver beetle, Ips pini.
References:
1.  Figueroa-Teran, R., Welch, W.H., Blomquist, G.J. and Tittiger, C. Ipsdienol dehydrogenase (IDOLDH): a novel oxidoreductase important for Ips pini pheromone production. Insect Biochem. Mol. Biol. 42 (2012) 81–90. [PMID: 22101251]
[EC 1.1.1.386 created 2015]
 
 
EC 1.1.1.387     
Accepted name: L-serine 3-dehydrogenase (NAD+)
Reaction: L-serine + NAD+ = 2-aminoacetaldehyde + CO2 + NADH + H+ (overall reaction)
(1a) L-serine + NAD+ = 2-aminomalonate semialdehyde + NADH + H+
(1b) 2-aminomalonate semialdehyde = 2-aminoacetaldehyde + CO2 (spontaneous)
Other name(s): NAD+-dependent L-serine dehydrogenase
Systematic name: L-serine:NAD+ 3-oxidoreductase
Comments: The enzyme, purified from the bacterium Pseudomonas aeruginosa, also shows activity with L-threonine (cf. EC 1.1.1.103, L-threonine 3-dehydrogenase). The enzyme has only very low activity with NADP+ [cf. EC 1.1.1.276, serine 3-dehydrogenase (NADP+)].
References:
1.  Tchigvintsev, A., Singer, A., Brown, G., Flick, R., Evdokimova, E., Tan, K., Gonzalez, C.F., Savchenko, A. and Yakunin, A.F. Biochemical and structural studies of uncharacterized protein PA0743 from Pseudomonas aeruginosa revealed NAD+-dependent L-serine dehydrogenase. J. Biol. Chem. 287 (2012) 1874–1883. [PMID: 22128181]
[EC 1.1.1.387 created 2015]
 
 
EC 1.1.1.388     
Accepted name: glucose-6-phosphate dehydrogenase (NAD+)
Reaction: D-glucose 6-phosphate + NAD+ = 6-phospho-D-glucono-1,5-lactone + NADH + H+
Other name(s): Glc6PDH; azf (gene name); archaeal zwischenferment
Systematic name: D-glucose-6-phosphate:NAD+ 1-oxidoreductase
Comments: The enzyme catalyses a step of the pentose phosphate pathway. The enzyme from the archaeon Haloferax volcanii is specific for NAD+. cf. EC 1.1.1.363, glucose-6-phosphate dehydrogenase [NAD(P)+] and EC 1.1.1.49, glucose-6-phosphate dehydrogenase (NADP+).
References:
1.  Pickl, A. and Schonheit, P. The oxidative pentose phosphate pathway in the haloarchaeon Haloferax volcanii involves a novel type of glucose-6-phosphate dehydrogenase--The archaeal Zwischenferment. FEBS Lett. 589 (2015) 1105–1111. [PMID: 25836736]
[EC 1.1.1.388 created 2015]
 
 
EC 1.1.1.389     
Accepted name: 2-dehydro-3-deoxy-L-galactonate 5-dehydrogenase
Reaction: 2-dehydro-3-deoxy-L-galactonate + NAD+ = 3-deoxy-D-glycero-2,5-hexodiulosonate + NADH + H+
Systematic name: 2-dehydro-3-deoxy-L-galactonate:NAD+ 5-oxidoreductase
Comments: The enzyme, characterized from agarose-degrading bacteria, is involved in a degradation pathway for 3,6-anhydro-α-L-galactopyranose, a major component of the polysaccharides of red macroalgae.
References:
1.  Lee, S.B., Cho, S.J., Kim, J.A., Lee, S.Y., Kim, S.M. and Lim, H.S. Metabolic pathway of 3,6-anhydro-L-galactose in agar-degrading microorganisms. Biotechnol. Bioprocess Eng. 19 (2014) 866–878.
[EC 1.1.1.389 created 2015]
 
 
EC 1.1.1.390     
Accepted name: sulfoquinovose 1-dehydrogenase
Reaction: sulfoquinovose + NAD+ = 6-deoxy-6-sulfo-D-glucono-1,5-lactone + NADH + H+
Glossary: sulfoquinovose = 6-deoxy-6-sulfo-D-glucopyranose
Systematic name: 6-deoxy-6-sulfo-D-glucopyranose:NAD+ 1-oxidoreductase
Comments: The enzyme, characterized from the bacterium Pseudomonas putida SQ1, participates in a sulfoquinovose degradation pathway. Activity with NADP+ is only 4% of that with NAD+.
References:
1.  Felux, A.K., Spiteller, D., Klebensberger, J. and Schleheck, D. Entner-Doudoroff pathway for sulfoquinovose degradation in Pseudomonas putida SQ1. Proc. Natl. Acad. Sci. USA 112 (2015) E4298–E4305. [PMID: 26195800]
[EC 1.1.1.390 created 2015]
 
 
EC 1.1.1.391     
Accepted name: 3β-hydroxycholanate 3-dehydrogenase (NAD+)
Reaction: isolithocholate + NAD+ = 3-oxo-5β-cholan-24-oate + NADH + H+
Glossary: isolithocholate = 3β-hydroxy-5β-cholan-24-oate
Other name(s): 3β-hydroxysteroid dehydrogenase
Systematic name: isolithocholate:NAD+ 3-oxidoreductase
Comments: This bacterial enzyme is involved, along with EC 1.1.1.52, 3α-hydroxycholanate dehydrogenase (NAD+), or EC 1.1.1.392, 3α-hydroxycholanate dehydrogenase (NADP+), in the modification of secondary bile acids to form 3β-bile acids (also known as iso-bile acids). The enzyme catalyses the reaction in the reduction direction in vivo. Also acts on related 3-oxo bile acids. cf. EC 1.1.1.393, 3β-hydroxycholanate 3-dehydrogenase (NADP+).
References:
1.  Edenharder, R., Pfutzner, A. and Hammann, R. Characterization of NAD-dependent 3 α- and 3 β-hydroxysteroid dehydrogenase and of NADP-dependent 7 β-hydroxysteroid dehydrogenase from Peptostreptococcus productus. Biochim. Biophys. Acta 1004 (1989) 230–238. [PMID: 2752021]
2.  Edenharder, R. and Pfutzner, M. Partial purification and characterization of an NAD-dependent 3 β-hydroxysteroid dehydrogenase from Clostridium innocuum. Appl. Environ. Microbiol. 55 (1989) 1656–1659. [PMID: 2764572]
3.  Devlin, A.S. and Fischbach, M.A. A biosynthetic pathway for a prominent class of microbiota-derived bile acids. Nat. Chem. Biol. 11 (2015) 685–690. [PMID: 26192599]
[EC 1.1.1.391 created 2016]
 
 
EC 1.1.1.392     
Accepted name: 3α-hydroxycholanate dehydrogenase (NADP+)
Reaction: lithocholate + NADP+ = 3-oxo-5β-cholan-24-oate + NADPH + H+
Glossary: lithocholate = 3α-hydroxy-5β-cholan-24-oate
Other name(s): α-hydroxy-cholanate dehydrogenase (ambiguous)
Systematic name: lithocholate:NADP+ 3-oxidoreductase
Comments: This bacterial enzyme is involved in the modification of secondary bile acids to form 3β-bile acids (also known as iso-bile acids) via a 3-oxo intermediate. The enzyme catalyses a reversible reaction in vitro. Also acts on related bile acids. cf. EC 1.1.1.52, 3α-hydroxycholanate dehydrogenase (NAD+).
References:
1.  Devlin, A.S. and Fischbach, M.A. A biosynthetic pathway for a prominent class of microbiota-derived bile acids. Nat. Chem. Biol. 11 (2015) 685–690. [PMID: 26192599]
[EC 1.1.1.392 created 2016]
 
 
EC 1.1.1.393     
Accepted name: 3β-hydroxycholanate 3-dehydrogenase (NADP+)
Reaction: isolithocholate + NADP+ = 3-oxo-5β-cholan-24-oate + NADPH + H+
Glossary: isolithocholate = 3β-hydroxy-5β-cholan-24-oate
Other name(s): 3β-hydroxysteroid dehydrogenase (ambiguous)
Systematic name: isolithocholate:NADP+ 3-oxidoreductase
Comments: This bacterial enzyme is involved, along with EC 1.1.1.52, 3α-hydroxycholanate dehydrogenase (NAD+), or EC 1.1.1.392, 3α-hydroxycholanate dehydrogenase (NADP+), in the modification of secondary bile acids to form 3β-bile acids (also known as iso-bile acids). The enzyme catalyses the reaction in the reduction direction in vivo. Also acts on related 3-oxo bile acids. cf. EC 1.1.1.391, 3β-hydroxycholanate 3-dehydrogenase (NAD+).
References:
1.  Akao, T., Akao, T., Hattori, M., Namba, T. and Kobashi, K. 3 β-Hydroxysteroid dehydrogenase of Ruminococcus sp. from human intestinal bacteria. J. Biochem. 99 (1986) 1425–1431. [PMID: 3458705]
2.  Devlin, A.S. and Fischbach, M.A. A biosynthetic pathway for a prominent class of microbiota-derived bile acids. Nat. Chem. Biol. 11 (2015) 685–690. [PMID: 26192599]
[EC 1.1.1.393 created 2016]
 
 
EC 1.1.1.394     
Accepted name: aurachin B dehydrogenase
Reaction: aurachin B + NAD+ + H2O = 4-[(2E,6E)-farnesyl]-4-hydroxy-2-methyl-3-oxo-3,4-dihydroquinoline 1-oxide + NADH + H+ (overall reaction)
(1a) 4-[(2E,6E)-farnesyl]-3,4-dihydroxy-2-methyl-3,4-dihydroquinoline 1-oxide + NAD+ = 4-[(2E,6E)-farnesyl]-4-hydroxy-2-methyl-3-oxo-3,4-dihydroquinoline 1-oxide + NADH + H+
(1b) aurachin B + H2O = 4-[(2E,6E)-farnesyl]-3,4-dihydroxy-2-methyl-3,4-dihydroquinoline 1-oxide (spontaneous)
Glossary: aurachin B= 4-[(2E,6E,10E)-3,7-dimethyldodeca-2,6,10-trien-1-yl]-3-hydroxy-2-methylquinoline 1-oxide
Other name(s): AuaH
Systematic name: aurachin B:NAD+ 3-oxidoreductase
Comments: The enzyme from the bacterium Stigmatella aurantiaca catalyses the final step in the conversion of aurachin C to aurachin B. In vivo the enzyme catalyses the reduction of 4-[(2E,6E)-farnesyl]-4-hydroxy-2-methyl-3-oxo-3,4-dihydroquinoline-1-oxide to form 4-[(2E,6E)-farnesyl]-2-methyl-1-oxo-3,4-dihydroquinoline-3,4-diol (note that the reactions written above proceed from right to left), which then undergoes a spontaneous dehydration to form aurachin B.
References:
1.  Katsuyama, Y., Harmrolfs, K., Pistorius, D., Li, Y. and Muller, R. A semipinacol rearrangement directed by an enzymatic system featuring dual-function FAD-dependent monooxygenase. Angew. Chem. Int. Ed. Engl. 51 (2012) 9437–9440. [PMID: 22907798]
[EC 1.1.1.394 created 2016]
 
 
EC 1.1.1.395     
Accepted name: 3α-hydroxy bile acid-CoA-ester 3-dehydrogenase
Reaction: a 3α-hydroxy bile acid CoA ester + NAD+ = a 3-oxo bile acid CoA ester + NADH + H+
Other name(s): baiA1 (gene name); baiA2 (gene name); baiA3 (gene name)
Systematic name: 3α-hydroxy-bile-acid-CoA-ester:NAD+ 3-oxidoreductase
Comments: This bacterial enzyme is involved in the 7-dehydroxylation process associated with bile acid degradation. The enzyme has very little activity with unconjugated bile acid substrates. It has similar activity with choloyl-CoA, chenodeoxycholoyl-CoA, deoxycholoyl-CoA, and lithocholoyl-CoA.
References:
1.  Mallonee, D.H., Lijewski, M.A. and Hylemon, P.B. Expression in Escherichia coli and characterization of a bile acid-inducible 3α-hydroxysteroid dehydrogenase from Eubacterium sp. strain VPI 12708. Curr. Microbiol. 30 (1995) 259–263. [PMID: 7766153]
2.  Bhowmik, S., Jones, D.H., Chiu, H.P., Park, I.H., Chiu, H.J., Axelrod, H.L., Farr, C.L., Tien, H.J., Agarwalla, S. and Lesley, S.A. Structural and functional characterization of BaiA, an enzyme involved in secondary bile acid synthesis in human gut microbe. Proteins 82 (2014) 216–229. [PMID: 23836456]
[EC 1.1.1.395 created 2016]
 
 
EC 1.1.1.396     
Accepted name: bacteriochlorophyllide a dehydrogenase
Reaction: (1) 3-deacetyl-3-(1-hydroxyethyl)bacteriochlorophyllide a + NAD+ = bacteriochlorophyllide a + NADH + H+
(2) 3-devinyl-3-(1-hydroxyethyl)chlorophyllide a + NAD+ = 3-acetyl-3-devinylchlorophyllide a + NADH + H+
Other name(s): bchC (gene name)
Systematic name: 3-deacetyl-3-(1-hydroxyethyl)bacteriochlorophyllide-a:NAD+ oxidoreductase (bacteriochlorophyllide a-forming)
Comments: The enzyme, together with EC 1.3.7.15, chlorophyllide-a reductase, and EC 4.2.1.165, chlorophyllide-a 31-hydratase, is involved in the conversion of chlorophyllide a to bacteriochlorophyllide a. The enzymes can act in multiple orders, resulting in the formation of different intermediates, but the final product of the cumulative action of the three enzymes is always bacteriochlorophyllide a. The enzyme oxidizes a hydroxyl group on ring A, converting it to an oxo group.
References:
1.  Wellington, C.L. and Beatty, J.T. Promoter mapping and nucleotide sequence of the bchC bacteriochlorophyll biosynthesis gene from Rhodobacter capsulatus. Gene 83 (1989) 251–261. [PMID: 2555268]
2.  McGlynn, P. and Hunter, C.N. Genetic analysis of the bchC and bchA genes of Rhodobacter sphaeroides. Mol. Gen. Genet. 236 (1993) 227–234. [PMID: 8437569]
3.  Lange, C., Kiesel, S., Peters, S., Virus, S., Scheer, H., Jahn, D. and Moser, J. Broadened substrate specificity of 3-hydroxyethyl bacteriochlorophyllide a dehydrogenase (BchC) indicates a new route for the biosynthesis of bacteriochlorophyll a. J. Biol. Chem. 290 (2015) 19697–19709. [PMID: 26088139]
[EC 1.1.1.396 created 2016]
 
 
EC 1.1.1.397     
Accepted name: β-methylindole-3-pyruvate reductase
Reaction: (2S,3R)-2-hydroxy-3-(indol-3-yl)butanoate + NAD+ = (R)-3-(indol-3-yl)-2-oxobutanoate + NADH + H+
Glossary: (R)-3-(indol-3-yl)-2-oxobutanoate = (R)-β-methylindole-3-pyruvate
(2S,3R)-2-hydroxy-3-(indol-3-yl)butanoate = indolmycenate
Other name(s): ind2 (gene name)
Systematic name: (2S,3R)-2-hydroxy-3-(indol-3-yl)butanoate:NAD+ oxidoreductase
Comments: The enzyme, characterized from the bacterium Streptomyces griseus, participates in the biosynthesis of indolmycin, an antibacterial drug that inhibits the bacterial tryptophan—tRNA ligase (EC 6.1.1.2).
References:
1.  Du, Y.L., Alkhalaf, L.M. and Ryan, K.S. In vitro reconstitution of indolmycin biosynthesis reveals the molecular basis of oxazolinone assembly. Proc. Natl. Acad. Sci. USA 112 (2015) 2717–2722. [PMID: 25730866]
[EC 1.1.1.397 created 2016]
 
 
EC 1.1.1.398     
Accepted name: 2-glutathionyl-2-methylbut-3-en-1-ol dehydrogenase
Reaction: 2-(glutathion-S-yl)-2-methylbut-3-en-1-ol + 2 NAD+ + H2O = 2-(glutathion-S-yl)-2-methylbut-3-enoate + 2 NADH + 2 H+ (overall reaction)
(1a) 2-(glutathion-S-yl)-2-methylbut-3-en-1-ol + NAD+ = 2-(glutathion-S-yl)-2-methylbut-3-enal + NADH + H+
(1b) 2-(glutathion-S-yl)-2-methylbut-3-enal + NAD+ + H2O = 2-(glutathion-S-yl)-2-methylbut-3-enoate + NADH + H+
Other name(s): isoH (gene name); 4-hydroxy-3-glutathionyl-3-methylbut-1-ene dehydrogenase
Systematic name: 2-(glutathion-S-yl)-2-methylbut-3-en-1-ol:NAD+ oxidoreductase
Comments: The enzyme, characterized from the bacterium Rhodococcus sp. AD45, is involved in isoprene degradation.
References:
1.  van Hylckama Vlieg, J.E., Kingma, J., Kruizinga, W. and Janssen, D.B. Purification of a glutathione S-transferase and a glutathione conjugate-specific dehydrogenase involved in isoprene metabolism in Rhodococcus sp. strain AD45. J. Bacteriol. 181 (1999) 2094–2101. [PMID: 10094686]
[EC 1.1.1.398 created 2016]
 
 
EC 1.1.1.399     
Accepted name: 2-oxoglutarate reductase
Reaction: (R)-2-hydroxyglutarate + NAD+ = 2-oxoglutarate + NADH + H+
Other name(s): serA (gene name)
Systematic name: (R)-2-hydroxyglutarate:NAD+ 2-oxidireductase
Comments: The enzyme catalyses a reversible reaction. The enzyme from the bacterium Peptoniphilus asaccharolyticus is specific for (R)-2-hydroxyglutarate [1,2]. The SerA enzyme from the bacterium Escherichia coli can also accept (S)-2-hydroxyglutarate with a much higher Km, and also catalyses the activity of EC 1.1.1.95, phosphoglycerate dehydrogenase [3].
References:
1.  Lerud, R.F. and Whiteley, H.R. Purification and properties of α-ketoglutarate reductase from Micrococcus aerogenes. J. Bacteriol. 106 (1971) 571–577. [PMID: 4396793]
2.  Johnson, W.M. and Westlake, D.W. Purification and characterization of glutamic acid dehydrogenase and α-ketoglutaric acid reductase from Peptococcus aerogenes. Can. J. Microbiol. 18 (1972) 881–892. [PMID: 4338318]
3.  Zhao, G. and Winkler, M.E. A novel α-ketoglutarate reductase activity of the serA-encoded 3-phosphoglycerate dehydrogenase of Escherichia coli K-12 and its possible implications for human 2-hydroxyglutaric aciduria. J. Bacteriol. 178 (1996) 232–239. [PMID: 8550422]
[EC 1.1.1.399 created 2016]
 
 
EC 1.1.1.400     
Accepted name: 2-methyl-1,2-propanediol dehydrogenase
Reaction: 2-methylpropane-1,2-diol + NAD+ = 2-hydroxy-2-methylpropanal + NADH + H+
Other name(s): mpdB (gene name)
Systematic name: 2-methylpropane-1,2-diol:NAD+ 1-oxidoreductase
Comments: This bacterial enzyme is involved in the degradation pathways of the alkene 2-methylpropene and the fuel additive tert-butyl methyl ether (MTBE), a widely occurring groundwater contaminant.
References:
1.  Lopes Ferreira, N., Labbe, D., Monot, F., Fayolle-Guichard, F. and Greer, C.W. Genes involved in the methyl tert-butyl ether (MTBE) metabolic pathway of Mycobacterium austroafricanum IFP 2012. Microbiology 152 (2006) 1361–1374. [PMID: 16622053]
2.  Kottegoda, S., Waligora, E. and Hyman, M. Metabolism of 2-methylpropene (isobutylene) by the aerobic bacterium Mycobacterium sp. strain ELW1. Appl. Environ. Microbiol. 81 (2015) 1966–1976. [PMID: 25576605]
[EC 1.1.1.400 created 2016]
 
 
EC 1.1.1.401     
Accepted name: 2-dehydro-3-deoxy-L-rhamnonate dehydrogenase (NAD+)
Reaction: 2-dehydro-3-deoxy-L-rhamnonate + NAD+ = 2,4-didehydro-3-deoxy-L-rhamnonate + NADH + H+
Other name(s): 2-keto-3-deoxy-L-rhamnonate dehydrogenase
Systematic name: 2-dehydro-3-deoxy-L-rhamnonate:NAD+ 4-oxidoreductase
Comments: The enzyme, characterized from the bacteria Sphingomonas sp. SKA58 and Sulfobacillus thermosulfidooxidans, is involved in the non-phosphorylative degradation pathway for L-rhamnose. It does not show any detectable activity with NADP+ or with other aldoses.
References:
1.  Watanabe, S. and Makino, K. Novel modified version of nonphosphorylated sugar metabolism - an alternative L-rhamnose pathway of Sphingomonas sp. FEBS J. 276 (2009) 1554–1567. [PMID: 19187228]
2.  Bae, J., Kim, S.M. and Lee, S.B. Identification and characterization of 2-keto-3-deoxy-L-rhamnonate dehydrogenase belonging to the MDR superfamily from the thermoacidophilic bacterium Sulfobacillus thermosulfidooxidans: implications to L-rhamnose metabolism in archaea. Extremophiles 19 (2015) 469–478. [PMID: 25617114]
[EC 1.1.1.401 created 2016]
 
 
EC 1.1.1.402     
Accepted name: D-erythritol 1-phosphate dehydrogenase
Reaction: D-erythritol 1-phosphate + NADP+ = D-erythrulose 1-phosphate + NADPH + H+
Other name(s): eryB (gene name)
Systematic name: D-erythritol-1-phosphate 2-oxidoreductase
Comments: The enzyme, characterized from the pathogenic bacterium Brucella abortus, which causes brucellosis in livestock, participates in erythritol catabolism.
References:
1.  Sperry, J.F. and Robertson, D.C. Erythritol catabolism by Brucella abortus. J. Bacteriol. 121 (1975) 619–630. [PMID: 163226]
2.  Sangari, F.J., Aguero, J. and Garcia-Lobo, J.M. The genes for erythritol catabolism are organized as an inducible operon in Brucella abortus. Microbiology 146 (2000) 487–495. [PMID: 10708387]
3.  Barbier, T., Collard, F., Zuniga-Ripa, A., Moriyon, I., Godard, T., Becker, J., Wittmann, C., Van Schaftingen, E. and Letesson, J.J. Erythritol feeds the pentose phosphate pathway via three new isomerases leading to D-erythrose-4-phosphate in Brucella. Proc. Natl. Acad. Sci. USA 111 (2014) 17815–17820. [PMID: 25453104]
[EC 1.1.1.402 created 2016]
 
 
EC 1.1.1.403     
Accepted name: D-threitol dehydrogenase (NAD+)
Reaction: D-threitol + NAD+ = D-erythrulose + NADH + H+
Other name(s): dthD (gene name)
Systematic name: D-threitol:NAD+ oxidoreductase
Comments: The enzyme, characterized from the bacterium Mycobacterium smegmatis, participates in the degradation of D-threitol.
References:
1.  Huang, H., Carter, M.S., Vetting, M.W., Al-Obaidi, N., Patskovsky, Y., Almo, S.C. and Gerlt, J.A. A general strategy for the discovery of metabolic pathways: D-threitol, L-threitol, and erythritol utilization in Mycobacterium smegmatis. J. Am. Chem. Soc. 137 (2015) 14570–14573. [PMID: 26560079]
[EC 1.1.1.403 created 2016]
 
 
EC 1.1.1.404     
Accepted name: tetrachlorobenzoquinone reductase
Reaction: 2,3,5,6-tetrachlorohydroquinone + NAD+ = 2,3,5,6-tetrachloro-1,4-benzoquinone + NADH + H+
Other name(s): pcpD (gene name); TCBQ reductase
Systematic name: 2,3,5,6-tetrachlorohydroquinone:NAD+ oxidoreductase
Comments: Contains FMN. The enzyme, characterized from the bacterium Sphingobium chlorophenolicum, participates in the degradation of pentachlorophenol.
References:
1.  Chen, L. and Yang, J. Biochemical characterization of the tetrachlorobenzoquinone reductase involved in the biodegradation of pentachlorophenol. Int. J. Mol. Sci. 9 (2008) 198–212. [PMID: 19325743]
2.  Yadid, I., Rudolph, J., Hlouchova, K. and Copley, S.D. Sequestration of a highly reactive intermediate in an evolving pathway for degradation of pentachlorophenol. Proc. Natl. Acad. Sci. USA 110 (2013) E2182–E2190. [PMID: 23676275]
[EC 1.1.1.404 created 2017]
 
 
EC 1.1.1.405     
Accepted name: ribitol-5-phosphate 2-dehydrogenase (NADP+)
Reaction: D-ribitol 5-phosphate + NADP+ = D-ribulose 5-phosphate + NADPH + H+
Other name(s): acs1 (gene name); bcs1 (gene name); tarJ (gene name); ribulose-5-phosphate reductase; ribulose-5-P reductase; D-ribulose 5-phosphate reductase
Systematic name: D-ribitol-5-phosphate:NADP+ 2-oxidoreductase
Comments: Requires Zn2+. The enzyme, characterized in bacteria, is specific for NADP. It is part of the synthesis pathway of CDP-ribitol. In Haemophilus influenzae it is part of a multifunctional enzyme also catalysing EC 2.7.7.40, D-ribitol-5-phosphate cytidylyltransferase. cf. EC 1.1.1.137, ribitol-5-phosphate 2-dehydrogenase.
References:
1.  Zolli, M., Kobric, D.J. and Brown, E.D. Reduction precedes cytidylyl transfer without substrate channeling in distinct active sites of the bifunctional CDP-ribitol synthase from Haemophilus influenzae. Biochemistry 40 (2001) 5041–5048. [PMID: 11305920]
2.  Pereira, M.P. and Brown, E.D. Bifunctional catalysis by CDP-ribitol synthase: convergent recruitment of reductase and cytidylyltransferase activities in Haemophilus influenzae and Staphylococcus aureus. Biochemistry 43 (2004) 11802–11812. [PMID: 15362865]
3.  Pereira, M.P., D'Elia, M.A., Troczynska, J. and Brown, E.D. Duplication of teichoic acid biosynthetic genes in Staphylococcus aureus leads to functionally redundant poly(ribitol phosphate) polymerases. J. Bacteriol. 190 (2008) 5642–5649. [PMID: 18556787]
4.  Baur, S., Marles-Wright, J., Buckenmaier, S., Lewis, R.J. and Vollmer, W. Synthesis of CDP-activated ribitol for teichoic acid precursors in Streptococcus pneumoniae. J. Bacteriol. 191 (2009) 1200–1210. [PMID: 19074383]
[EC 1.1.1.405 created 2017]
 
 
EC 1.1.1.406     
Accepted name: galactitol 2-dehydrogenase (L-tagatose-forming)
Reaction: galactitol + NAD+ = L-tagatose + NADH + H+
Other name(s): GatDH
Systematic name: galactitol:NAD+ 2-oxidoreductase (L-tagatose-forming)
Comments: The enzyme, characterized in the bacterium Rhodobacter sphaeroides, has a wide subtrate specificity. In addition to galactitol, it primarily oxidizes D-threitol and xylitol, and in addition to L-tagatose, it primarily reduces L-erythrulose, D-ribulose and L-glyceraldehyde. It is specific for NAD+. The enzyme also shows activity with D-tagatose (cf. EC 1.1.1.16, galactitol 2-dehydrogenase).
References:
1.  Schneider, K.H., Jakel, G., Hoffmann, R. and Giffhorn, F. Enzyme evolution in Rhodobacter sphaeroides: selection of a mutant expressing a new galactitol dehydrogenase and biochemical characterization of the enzyme. Microbiology 141 (1995) 1865–1873. [PMID: 7551050]
2.  Carius, Y., Christian, H., Faust, A., Zander, U., Klink, B.U., Kornberger, P., Kohring, G.W., Giffhorn, F. and Scheidig, A.J. Structural insight into substrate differentiation of the sugar-metabolizing enzyme galactitol dehydrogenase from Rhodobacter sphaeroides D. J. Biol. Chem. 285 (2010) 20006–20014. [PMID: 20410293]
[EC 1.1.1.406 created 2017]
 
 
EC 1.1.1.407     
Accepted name: D-altritol 5-dehydrogenase
Reaction: D-altritol + NAD+ = D-tagatose + NADH + H+
Systematic name: D-altritol:NAD+ 5-oxidoreductase
Comments: The enzyme, characterized in Agrobacterium fabrum C58, also has low activity with D-mannitol and D-arabinitol. It is part of a D-altritol degradation pathway.
References:
1.  Wichelecki, D.J., Vetting, M.W., Chou, L., Al-Obaidi, N., Bouvier, J.T., Almo, S.C. and Gerlt, J.A. ATP-binding cassette (ABC) transport system solute-binding protein-guided identification of novel D-altritol and galactitol catabolic pathways in Agrobacterium tumefaciens C58. J. Biol. Chem. 290 (2015) 28963–28976. [PMID: 26472925]
[EC 1.1.1.407 created 2017]
 
 
EC 1.1.1.408     
Accepted name: 4-phospho-D-threonate 3-dehydrogenase
Reaction: 4-phospho-D-threonate + NAD+ = glycerone phosphate + CO2 + NADH + H+ (overall reaction)
(1a) 4-phospho-D-threonate + NAD+ = 3-dehydro-4-phospho-D-erythronate + NADH + H+
(1b) 3-dehydro-4-phospho-D-erythronate = glycerone phosphate + CO2 (spontaneous)
Glossary: D-threonate = (2S,3R)-2,3,4-trihydroxybutanoate
glycerone phosphate = dihydroxyacetone phosphate = 3-hydroxy-2-oxopropyl phosphate
Other name(s): pdxA2 (gene name) (ambiguous)
Systematic name: 4-phospho-D-threonate:NAD+ 3-oxidoreductase
Comments: The enzyme, characterized from bacteria, is involved in a pathway for D-threonate catabolism.
References:
1.  Zhang, X., Carter, M.S., Vetting, M.W., San Francisco, B., Zhao, S., Al-Obaidi, N.F., Solbiati, J.O., Thiaville, J.J., de Crecy-Lagard, V., Jacobson, M.P., Almo, S.C. and Gerlt, J.A. Assignment of function to a domain of unknown function: DUF1537 is a new kinase family in catabolic pathways for