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+ |
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For diagram of mevalonate biosynthesis, click here |
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. |
Links to other databases: |
BRENDA, EAWAG-BBD, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9031-72-5 |
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. Patent JORNVALL-H-1977-443, Eur. J. Biochem. (1977), 72, 443. |
3. |
Negelein, E. and Wulff, H.-J. Diphosphopyridinproteid, Alkohol, Acetaldehyd. Patent NEGELEIN-E-1937-351, Biochem. Z. (1937), 293, 351. |
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] |
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[EC 1.1.1.1 created 1961, modified 2011] |
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EC |
1.1.1.2 |
Accepted name: |
alcohol dehydrogenase (NADP+) |
Reaction: |
an alcohol + NADP+ = an aldehyde + NADPH + H+ |
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For diagram of mevalonate biosynthesis, click here |
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 target="new">EC 1.1.1.19 (L-glucuronate reductase), EC 1.1.1.33 [mevaldate reductase (NADPH)] and target="new">EC 1.1.1.55 [lactaldehyde reductase (NADPH)]. Re-specific with respect to NADPH. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9028-12-0 |
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. Patent REEVES-RE-1971-55, Int. J. Biochem. (1971), 2, 55. |
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] |
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[EC 1.1.1.2 created 1961] |
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EC |
1.1.1.3 |
Accepted name: |
homoserine dehydrogenase |
Reaction: |
L-homoserine + NAD(P)+ = L-aspartate 4-semialdehyde + NAD(P)H + H+ |
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For diagram of threonine biosynthesis, click here |
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 target="new">EC 2.7.2.4 (aspartate kinase). |
Links to other databases: |
BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9028-13-1 |
References: |
1. |
Black, S. and Wright, N.G. Homoserine dehydrogenase. Patent BLACK-S-1955-51, J. Biol. Chem. (1955), 213, 51. |
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. Patent TARNES-WL-1972-677&F=0">STARNES-WL-1972-677, Biochemistry (1972), 11, 677. |
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. Patent VERON-M-1972-520, Eur. J. Biochem. (1972), 28, 520. |
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[EC 1.1.1.3 created 1961, modified 1976] |
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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. |
Links to other databases: |
BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 37250-09-2 |
References: |
1. |
Strecker, H.J. and Harary, I. Bacterial butylene glycol dehydrogenase and diacetyl reductase. Patent TRECKER-HJ-1954-263&F=0">STRECKER-HJ-1954-263, J. Biol. Chem. (1954), 211, 263. |
2. |
Taylor, M.B. and Juni, E. Stereoisomeric specificities of 2,3-butanediol dehydrogenase. Biochim. Biophys. Acta 39 (1960) 448–457. [DOI] [PMID: 13837186] |
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[EC 1.1.1.4 created 1961 (EC 1.1.1.74 created 1972, incorporated 1976)] |
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EC
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1.1.1.5
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Transferred entry: | acetoin dehydrogenase. Now target="new">EC 1.1.1.303, diacetyl reductase [(R)-acetoin forming] and target="new">EC 1.1.1.304, diacetyl reductase [(S)-acetoin forming]
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[EC 1.1.1.5 created 1961, modified 1976, deleted 2010] |
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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. |
Links to other databases: |
BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9028-14-2 |
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. Patent TON-RM-1953-1005&F=0">BURTON-RM-1953-1005, J. Am. Chem. Soc. (1953), 75, 1005. |
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] |
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[EC 1.1.1.6 created 1961] |
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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 |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9028-15-3 |
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] |
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[EC 1.1.1.7 created 1961] |
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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). |
Links to other databases: |
BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9075-65-4 |
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. Patent BROSEMER-RW-1969-2095, Biochemistry (1969), 8, 2095. |
3. |
O'Brien, S.J. and MacIntyre, R.J. The α-glycerophosphate cycle in Drosophila melanogaster. I. Biochemical and developmental aspects. Patent OBRIEN-SJ-1972-141, Biochem. Genet. (1972), 7, 141. |
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. Patent TIN-KL-1973-97&F=0">WARKENTIN-KL-1973-97, Eur. J. Biochem. (1973), 36, 97. |
5. |
Albertyn, J., van Tonder, A. and Prior, B.A. Purification and characterization of glycerol-3-phosphate dehydrogenase of Saccharomyces cerevisiae. Patent TYN-J-1992-130&F=0">ALBERTYN-J-1992-130, FEBS Lett. (1992), 308, 130. |
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. [DOI] [PMID: 7671141] |
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[EC 1.1.1.8 created 1961, modified 2005] |
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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. |
Links to other databases: |
BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9028-16-4 |
References: |
1. |
Chiang, C. and Knight, S.G. A new pathway of pentose metabolism. Patent CHIANG-C-1960-554, Biochem. Biophys. Res. Commun. (1960), 3, 554. |
2. |
Hickman, J. and Ashwell, G. A sensitive and stereospecific enzymatic assay for xylulose. Patent HICKMAN-J-1959-758, J. Biol. Chem. (1959), 234, 758. |
3. |
Jakoby, W.B. and Fredericks, J. Erythritol dehydrogenase from Aerobacter aerogenes. Patent JAKOBY-WB-1961-26, Biochim. Biophys. Acta (1961), 48, 26. |
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[EC 1.1.1.9 created 1961] |
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EC |
1.1.1.10 |
Accepted name: |
L-xylulose reductase |
Reaction: |
xylitol + NADP+ = L-xylulose + NADPH + H+ |
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For diagram of L-arabinose catabolism, click here |
Other name(s): |
xylitol dehydrogenase (ambiguous) |
Systematic name: |
xylitol:NADP+ 4-oxidoreductase (L-xylulose-forming) |
Links to other databases: |
BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9028-17-5 |
References: |
1. |
Doten, R.C. and Mortlock, R.P. Characterization of xylitol-utilizing mutants of Erwinia uredovora. Patent TEN-RC-1985-529&F=0">DOTEN-RC-1985-529, J. Bacteriol. (1985), 161, 529. |
2. |
Hickman, J. and Ashwell, G. A sensitive and stereospecific enzymatic assay for xylulose. Patent HICKMAN-J-1959-758, J. Biol. Chem. (1959), 234, 758. |
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] |
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[EC 1.1.1.10 created 1961] |
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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 |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9028-18-6 |
References: |
1. |
Lin, E.C.C. An inducible D-arabitol dehydrogenase from Aerobacter aerogenes. Patent LIN-ECC-1961-31, J. Biol. Chem. (1961), 236, 31. |
2. |
Wood, W.A., McDonough, M.J. and Jacobs, L.B. Ribitol and D-arabitol utilization by Aerobacter aerogenes. Patent WOOD-WA-1961-2190, J. Biol. Chem. (1961), 236, 2190. |
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[EC 1.1.1.11 created 1961] |
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EC |
1.1.1.12 |
Accepted name: |
L-arabinitol 4-dehydrogenase |
Reaction: |
L-arabinitol + NAD+ = L-xylulose + NADH + H+ |
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For diagram of L-arabinose catabolism, click here |
Other name(s): |
pentitol-DPN dehydrogenase (ambiguous); L-arabitol dehydrogenase |
Systematic name: |
L-arabinitol:NAD+ 4-oxidoreductase (L-xylulose-forming) |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9028-19-7 |
References: |
1. |
Chiang, C. and Knight, S.G. A new pathway of pentose metabolism. Patent CHIANG-C-1960-554, Biochem. Biophys. Res. Commun. (1960), 3, 554. |
2. |
Chiang, C. and Knight, S.G. L-Arabinose metabolism by cell-free extracts of Penicillium chrysogenum. Patent CHIANG-C-1961-271, Biochim. Biophys. Acta (1961), 46, 271. |
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[EC 1.1.1.12 created 1961] |
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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) |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9028-20-0 |
References: |
1. |
Chiang, C. and Knight, S.G. L-Arabinose metabolism by cell-free extracts of Penicillium chrysogenum. Patent CHIANG-C-1961-271, Biochim. Biophys. Acta (1961), 46, 271. |
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[EC 1.1.1.13 created 1961] |
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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+. |
Links to other databases: |
BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9028-21-1 |
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. Patent BURNELL-JN-1983-507, Int. J. Biochem. (1983), 15, 507. |
3. |
Leissing, N. and McGuinness, E.T. Rapid affinity purification and properties of rat liver sorbitol dehydrogenase. Biochim. Biophys. Acta 524 (1978) 254–261. [DOI] [PMID: 667078] |
4. |
Negm, F.B. and Loescher, W.H. Detection and characterization of sorbitol dehydrogenase from apple callus tissue. Patent NEGM-FB-1979-69, Plant Physiol. (1979), 64, 69. |
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. Patent OBRIEN-MM-1983-81, Biochem. J. (1983), 211, 81. |
6. |
Ng, K., Ye, R., Wu, X.C. and Wong, S.L. Sorbitol dehydrogenase from Bacillus subtilis. Purification, characterization, and gene cloning. Patent NG-K-1992-24989, J. Biol. Chem. (1992), 267, 24989. |
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[EC 1.1.1.14 created 1961, modified 2011] |
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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. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9028-22-2 |
References: |
1. |
Shaw, D.R.D. Polyol dehydrogenases. 3. Galactitol dehydrogenase and D-iditol dehydrogenase. Patent SHAW-DRD-1956-394, Biochem. J. (1956), 64, 394. |
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[EC 1.1.1.15 created 1961] |
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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. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9028-23-3 |
References: |
1. |
Shaw, D.R.D. Polyol dehydrogenases. 3. Galactitol dehydrogenase and D-iditol dehydrogenase. Patent SHAW-DRD-1956-394, Biochem. J. (1956), 64, 394. |
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. Patent WICHELECKI-DJ-2015-28963, J. Biol. Chem. (2015), 290, 28963. |
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[EC 1.1.1.16 created 1961] |
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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 |
Links to other databases: |
BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9028-24-4 |
References: |
1. |
Marmur, J. and Hotchkiss, R.D. Mannitol metabolism, a transferable property of pneumococcus. Patent MARMUR-J-1955-383, J. Biol. Chem. (1955), 214, 383. |
2. |
Wolfe, J.B. and Kaplan, N.O. Hexose phosphate and hexose reductase. A. D-Mannitol-1-phosphate dehydrogenase from E. coli. Patent WOLFE-JB-1955-346, Methods Enzymol. (1955), 1, 346. |
3. |
Wolfe, J.B. and Kaplan, N.O. D-Mannitol 1-phosphate dehydrogenase from Escherichia coli. Patent WOLFE-JB-1956-849, J. Biol. Chem. (1956), 218, 849. |
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[EC 1.1.1.17 created 1961] |
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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 |
Links to other databases: |
BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9028-25-5 |
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. [DOI] [PMID: 13292912] |
3. |
Vidal-Lieria, M. and van Uden, N. Inositol dehydrogenase from the yeast Cryptococcus melibiosum. Patent VIDAL-LIERIA-M-1973-295, Biochim. Biophys. Acta (1973), 293, 295. |
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[EC 1.1.1.18 created 1961] |
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EC |
1.1.1.19 |
Accepted name: |
glucuronate reductase |
Reaction: |
L-gulonate + NADP+ = D-glucuronate + NADPH + H+ |
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For diagram of mammalian ascorbic-acid biosynthesis, click here |
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 target="new">EC 1.1.1.2 [alcohol dehydrogenase (NADP+)]. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9028-29-9 |
References: |
1. |
Sivak, A. and Hoffmann-Ostenhof, O. Enzymes of meso-inositol catabolism in the yeast Schwanniomyces occidentalis. Patent SIVAK-A-1961-426, Biochim. Biophys. Acta (1961), 53, 426. |
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. Patent YORK-JL-1961-298, Biochim. Biophys. Acta (1961), 47, 298. |
|
[EC 1.1.1.19 created 1961] |
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|
|
|
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 |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9028-30-2 |
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. Patent SUZUKI-K-1960-313, J. Biochem. (Tokyo) (1960), 48, 313. |
|
[EC 1.1.1.20 created 1961] |
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|
|
EC |
1.1.1.21 |
Accepted name: |
aldose reductase |
Reaction: |
alditol + NAD(P)+ = aldose + NAD(P)H + H+ |
|
For diagram of L-arabinose catabolism, click here |
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. |
Links to other databases: |
BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9028-31-3 |
References: |
1. |
Attwood, M.A. and Doughty, C.C. Purification and properties of calf liver aldose reductase. Patent TTWOOD-MA-1974-358&F=0">ATTWOOD-MA-1974-358, Biochim. Biophys. Acta (1974), 370, 358. |
2. |
Boghosian, R.A. and McGuinness, E.T. Affinity purification and properties of porcine brain aldose reductase. Biochim. Biophys. Acta 567 (1979) 278–286. [DOI] [PMID: 36151] |
3. |
Hers, H.G. L’Aldose-réductase. Patent HERS-HG-1960-120, Biochim. Biophys. Acta (1960), 37, 120. |
4. |
Scher, B.M. and Horecker, B.L. Pentose metabolism in Candida. 3. The triphosphopyridine nucleotide-specific polyol dehydrogenase of Candida utilis. Patent SCHER-BM-1966-117, Arch. Biochem. Biophys. (1966), 116, 117. |
|
[EC 1.1.1.21 created 1961 (EC 1.1.1.139 created 1972, incorporated 1978), modified 2019] |
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|
EC |
1.1.1.22 |
Accepted name: |
UDP-glucose 6-dehydrogenase |
Reaction: |
UDP-α-D-glucose + trong>2trong> NAD+ + H2O = UDP-α-D-glucuronate + trong>2trong> NADH + trong>2trong> H+ |
|
For diagram of the biosynthesis of UDP-α-D-glucose, UDP-α-D-galactose and UDP-α-D-glucuronate, click here |
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. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9028-26-6 |
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. [DOI] [PMID: 1091296] |
2. |
Maxwell, E.S., Kalckar, H.M. and Strominger, J.L. Some properties of uridine diphosphoglucose dehydrogenase. Patent MAXWELL-ES-1956-2, Arch. Biochem. Biophys. (1956), 65, 2. |
3. |
Strominger, J.L. and Mapson, L.W. Uridine diphosphoglucose dehydrogenase of pea seedlings. Patent TROMINGER-JL-1957-567&F=0">STROMINGER-JL-1957-567, Biochem. J. (1957), 66, 567. |
4. |
Strominger, J.L., Maxwell, E.S., Axelrod, J. and Kalckar, H.M. Enzymatic formation of uridine diphosphogluconic acid. Patent TROMINGER-JL-1957-79&F=0">STROMINGER-JL-1957-79, J. Biol. Chem. (1957), 224, 79. |
|
[EC 1.1.1.22 created 1961] |
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|
|
|
EC |
1.1.1.23 |
Accepted name: |
histidinol dehydrogenase |
Reaction: |
L-histidinol + trong>2trong> NAD+ + H2O = L-histidine + trong>2trong> NADH + trong>3trong> 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 target="new">EC 3.5.4.19 (phosphoribosyl-AMP cyclohydrolase) and target="new">EC 3.6.1.31 (phosphoribosyl-ATP diphosphatase). |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9028-27-7 |
References: |
1. |
Adams, E. Enzymatic synthesis of histidine from histidinol. Patent ADAMS-E-1954-829, J. Biol. Chem. (1954), 209, 829. |
2. |
Adams, E. L-Histidinal, a biosynthetic precursor of histidine. Patent ADAMS-E-1955-325, J. Biol. Chem. (1955), 217, 325. |
3. |
Loper, J.C. Histidinol dehydrogenase from Salmonella typhimurium. Crystallization and composition studies. Patent LOPER-JC-1968-3264, J. Biol. Chem. (1968), 243, 3264. |
4. |
Yourno, J. and Ino, I. Purification and crystallization of histidinol dehydrogenase from Salmonella typhimurium LT-2. Patent YOURNO-J-1968-3273, J. Biol. Chem. (1968), 243, 3273. |
|
[EC 1.1.1.23 created 1961] |
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|
EC |
1.1.1.24 |
Accepted name: |
quinate/shikimate dehydrogenase (NAD+) |
Reaction: |
L-quinate + NAD+ = 3-dehydroquinate + NADH + H+ |
|
For diagram of shikimate and chorismate biosynthesis, click here |
Glossary: |
target="new" href="glossary/quinic.html">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, target="new" href="https://www.qmul.ac.uk/sbcs/iupac/cyclitol/I6t10.html#I8">sections I-8 and I-9: and is shown in the target="new" href="reaction/misc/shikim.html">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. target="new">EC 1.1.5.8, quinate/shikimate dehydrogenase (quinone), target="new">EC 1.1.1.282, quinate/shikimate dehydrogenase [NAD(P)+], and target="new">EC 1.1.1.25, shikimate dehydrogenase (NADP+). |
Links to other databases: |
BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9028-28-8 |
References: |
1. |
Mitsuhashi, S. and Davis, B.D. Aromatic biosynthesis. XIII. Conversion of quinic acid to 5-dehydroquinic acid by quinic dehydrogenase. Patent TSUHASHI-S-1954-268&F=0">MITSUHASHI-S-1954-268, Biochim. Biophys. Acta (1954), 15, 268. |
2. |
Gamborg, O.L. Aromatic metabolism in plants. III. Quinate dehydrogenase from mung bean cell suspension cultures. Patent GAMBORG-OL-1966-483, Biochim. Biophys. Acta (1966), 128, 483. |
3. |
Hawkins, A.R., Giles, N.H. and Kinghorn, J.R. Genetical and biochemical aspects of quinate breakdown in the filamentous fungus Aspergillus nidulans. Patent HAWKINS-AR-1982-271, Biochem. Genet. (1982), 20, 271. |
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. Patent SINGH-S-2008-2221, Mol. Biol. Evol. (2008), 25, 2221. |
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. [DOI] [PMID: 19376919] |
6. |
Kubota, T., Tanaka, Y., Hiraga, K., Inui, M. and Yukawa, H. Characterization of shikimate dehydrogenase homologues of Corynebacterium glutamicum. Patent TA-T-2013-8139&F=0">KUBOTA-T-2013-8139, Appl. Microbiol. Biotechnol. (2013), 97, 8139. |
7. |
Peek, J. and Christendat, D. The shikimate dehydrogenase family: functional diversity within a conserved structural and mechanistic framework. Patent PEEK-J-2015-85, Arch. Biochem. Biophys. (2015), 566, 85. |
|
[EC 1.1.1.24 created 1961, modified 1976, modified 2004, modified 2021] |
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EC |
1.1.1.25 |
Accepted name: |
shikimate dehydrogenase (NADP+) |
Reaction: |
shikimate + NADP+ = 3-dehydroshikimate + NADPH + H+ |
|
For diagram of shikimate and chorismate biosynthesis, click here |
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 target="new">EC 4.2.1.10, 3-dehydroquinate dehydratase [4]. cf. target="new">EC 1.1.1.24, quinate/shikimate dehydrogenase (NAD+), target="new">EC 1.1.5.8, quinate/shikimate dehydrogenase (quinone), and target="new">EC 1.1.1.282, quinate/shikimate dehydrogenase [NAD(P)+]. |
Links to other databases: |
BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9026-87-3 |
References: |
1. |
Mitsuhashi, S. and Davis, B.D. Aromatic biosynthesis. XIII. Conversion of quinic acid to 5-dehydroquinic acid by quinic dehydrogenase. Patent TSUHASHI-S-1954-268&F=0">MITSUHASHI-S-1954-268, Biochim. Biophys. Acta (1954), 15, 268. |
2. |
Yaniv, H. and Gilvarg, C. Aromatic biosynthesis. XIV. 5-Dehydroshikimic reductase. Patent YANIV-H-1955-787, J. Biol. Chem. (1955), 213, 787. |
3. |
Balinsky, D. and Davies, D.D. Aromatic biosynthesis in higher plants. 1. Preparation and properties of dehydroshikimic reductase. Patent BALINSKY-D-1961-292, Biochem. J. (1961), 80, 292. |
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. Patent TON-IA-1988-319&F=0">ANTON-IA-1988-319, Biochem. J. (1988), 249, 319. |
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. Patent YE-S-2003-4144, J. Bacteriol. (2003), 185, 4144. |
|
[EC 1.1.1.25 created 1961, modified 1976, modified 2004, modified 2021] |
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EC |
1.1.1.26 |
Accepted name: |
glyoxylate reductase |
Reaction: |
glycolate + NAD+ = glyoxylate + NADH + H+ |
|
For diagram of L-arabinose catabolism, click here |
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. |
Links to other databases: |
BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9028-32-4 |
References: |
|
[EC 1.1.1.26 created 1961] |
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|
|
|
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. |
Links to other databases: |
BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9001-60-9 |
References: |
1. |
Dennis, D. and Kaplan, N.O. D and L-lactic acid dehydrogenase in Lactobacillus plantarum. Patent DENNIS-D-1960-810, J. Biol. Chem. (1960), 235, 810. |
2. |
Everse, J. and Kaplan, N.O. Lactate dehydrogenases: structure and function. Patent EVERSE-J-1973-61, Adv. Enzymol. Relat. Subj. Biochem. (1973), 37, 61. |
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. Patent SCHAR-H-P-1979-795, Hoppe-Seyler's Z. Physiol. Chem. (1979), 360, 795. |
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[EC 1.1.1.27 created 1961] |
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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 |
Links to other databases: |
BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9028-36-8 |
References: |
1. |
Dennis, D. and Kaplan, N.O. D and L-lactic acid dehydrogenase in Lactobacillus plantarum. Patent DENNIS-D-1960-810, J. Biol. Chem. (1960), 235, 810. |
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[EC 1.1.1.28 created 1961] |
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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 |
Links to other databases: |
BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9028-37-9 |
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. Patent HOLZER-H-1957-292, Biochem. Z. (1957), 329, 292. |
2. |
Stafford, H.A., Magaldi, A. and Vennesland, B. The enzymatic reduction of hydroxypyruvic acid to D-glyceric acid in higher plants. Patent TAFFORD-HA-1954-621&F=0">STAFFORD-HA-1954-621, J. Biol. Chem. (1954), 207, 621. |
|
[EC 1.1.1.29 created 1961] |
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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. |
Links to other databases: |
BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9028-38-0 |
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. Patent BERGMEYER-H-U-1967-423, Biochem. J. (1967), 102, 423. |
2. |
Delafield, F.P., Cooksey, K.E. and Doudoroff, M. β-Hydroxybutyric dehydrogenase and dimer hydrolase of Pseudomonas lemoignei. Patent DELAFIELD-FP-1965-4023, J. Biol. Chem. (1965), 240, 4023. |
3. |
Lehninger, A.L., Sudduth, H.C. and Wise, J.B. D-β-Hydroxybutyric dehydrogenase of mitochondria. Patent LEHNINGER-AL-1960-2450, J. Biol. Chem. (1960), 235, 2450. |
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[EC 1.1.1.30 created 1961] |
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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 |
Links to other databases: |
BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9028-39-1 |
References: |
1. |
Robinson, W.G. and Coon, M.J. Purification and properties of β-hydroxyisobutyric dehydrogenase. Patent ROBINSON-WG-1957-511, J. Biol. Chem. (1957), 225, 511. |
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[EC 1.1.1.31 created 1961] |
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EC
|
1.1.1.32
|
Deleted entry: | mevaldate reductase, now included with target="new">EC 1.1.1.1, alcohol dehydrogenase. |
[EC 1.1.1.32 created 1961, deleted 2022] |
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EC
|
1.1.1.33
|
Deleted entry: | mevaldate reductase (NADPH), now included with target="new">EC 1.1.1.2, alcohol dehydrogenase (NADP+). |
[EC 1.1.1.33 created 1961, deleted 2022] |
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|
EC |
1.1.1.34 |
Accepted name: |
hydroxymethylglutaryl-CoA reductase (NADPH) |
Reaction: |
(R)-mevalonate + CoA + trong>2trong> NADP+ = (S)-3-hydroxy-3-methylglutaryl-CoA + trong>2trong> NADPH + trong>2trong> H+ |
|
For diagram of mevalonate biosynthesis, click here |
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 target="new">EC 2.7.11.31 {[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase} and reactivated by target="new">EC 3.1.3.47 {[hydroxymethylglutaryl-CoA reductase (NADPH)]-phosphatase}. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9028-35-7 |
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. Patent BUCHER-NLR-1960-491, Biochim. Biophys. Acta (1960), 40, 491. |
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] |
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[EC 1.1.1.34 created 1961] |
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|
EC |
1.1.1.35 |
Accepted name: |
3-hydroxyacyl-CoA dehydrogenase |
Reaction: |
(S)-3-hydroxyacyl-CoA + NAD+ = 3-oxoacyl-CoA + NADH + H+ |
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|
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. target="new">EC 1.1.1.211 [long-chain-3-hydroxyacyl-CoA dehydrogenase]). |
Links to other databases: |
BRENDA, EAWAG-BBD, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9028-40-4 |
References: |
1. |
Hillmer, P. and Gottschalk, G. Solubilization and partial characterisation of particulate dehydrogenases from Clostridium kluyveri. Patent HILLMER-P-1974-12, Biochim. Biophys. Acta (1974), 334, 12. |
2. |
Lehninger, A.L. and Greville, G.D. The enzymatic oxidation of d- and l-β-hydroxybutyrate. Biochim. Biophys. Acta 12 (1953) 188–202. [DOI] [PMID: 13115428] |
3. |
Stern, J.R. Crystalline β-hydroxybutyrate dehydrogenase from pig heart. Patent TERN-JR-1957-448&F=0">STERN-JR-1957-448, Biochim. Biophys. Acta (1957), 26, 448. |
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. Patent WAKIL-SJ-1954-631, J. Biol. Chem. (1954), 207, 631. |
|
[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+ |
|
For diagram of benzoyl-CoA catabolism, click here |
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 |
Links to other databases: |
BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9028-41-5 |
References: |
1. |
Wakil, S.J. and Bressler, R. Studies on the mechanism of fatty acid synthesis. X. Reduced triphosphopyridine nucleotide-acetoacetyl coenzyme A reductase. Patent WAKIL-SJ-1962-687, J. Biol. Chem. (1962), 237, 687. |
|
[EC 1.1.1.36 created 1961] |
|
|
|
|
EC |
1.1.1.37 |
Accepted name: |
malate dehydrogenase |
Reaction: |
(S)-malate + NAD+ = oxaloacetate + NADH + H+ |
|
For diagram of the citric-acid cycle, click here and for diagram of the glyoxylate cycle, click here |
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 target="new">EC 1.1.1.38, malate dehydrogenase (oxaloacetate-decarboxylating), is unable to convert it to pyruvate. Also oxidizes some other 2-hydroxydicarboxylic acids. cf. target="new">EC 1.1.1.82, malate dehydrogenase (NADP+); target="new">EC 1.1.1.299, malate dehydrogenase [NAD(P)+]; and target="new">EC 1.1.5.4, malate dehydrogenase (quinone). |
Links to other databases: |
BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9001-64-3 |
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. Patent GUHA-A-1968-609, J. Biol. Chem. (1968), 243, 609. |
3. |
McReynolds, M.S. and Kitto, G.B. Purification and properties of Drosophila malate dehydrogenases. Patent MCREYNOLDS-MS-1970-165, Biochim. Biophys. Acta (1970), 198, 165. |
4. |
Wolfe, R.G. and Nielands, J.B. Some molecular and kinetic properties of heart malic dehydrogenase. Patent WOLFE-RG-1956-61, J. Biol. Chem. (1956), 221, 61. |
|
[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 target="new">EC 1.1.1.39, malate dehydrogenase (decarboxylating), this enzyme can also decarboxylate oxaloacetate. cf. target="new">EC 1.1.1.40, malate dehydrogenase (oxaloacetate-decarboxylating) (NADP+). |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9080-52-8 |
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. Patent KAUFMAN-S-1951-301, J. Biol. Chem. (1951), 192, 301. |
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. Patent YAMAGUCHI-M-1979-325, J. Biochem. (1979), 86, 325. |
|
[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 target="new">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. target="new">EC 1.1.1.37, malate dehydrogenase; target="new">EC 1.1.1.38, malate dehydrogenase (oxaloacetate-decarboxylating); and target="new">EC 1.1.1.83, D-malate dehydrogenase (decarboxylating). |
Links to other databases: |
BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9028-46-0 |
References: |
1. |
Macrae, A.R. Isolation and properties of a ’malic’ enzyme from cauliflower bud mitochondria. Patent MACRAE-AR-1971-495, Biochem. J. (1971), 122, 495. |
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. target="new">EC 1.1.1.38, malate dehydrogenase (oxaloacetate-decarboxylating), and target="new">EC 1.1.1.39, malate dehydrogenase (decarboxylating). |
Links to other databases: |
BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9028-47-1 |
References: |
1. |
Harary, I., Korey, S.R. and Ochoa, S. Biosynthesis of dicarboxylic acids by carbon dioxide fixation. VII. Equilibrium of "malic" enzyme reaction. Patent HARARY-I-1953-595, J. Biol. Chem. (1953), 203, 595. |
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. Patent OCHOA-S-1948-979, J. Biol. Chem. (1948), 174, 979. |
3. |
Rutter, W.J. and Lardy, H.A. Purification and properties of pigeon liver malic enzyme. Patent TTER-WJ-1958-374&F=0">RUTTER-WJ-1958-374, J. Biol. Chem. (1958), 233, 374. |
4. |
Stickland, R.G. Some properties of the malic enzyme of pigeon liver. 1. Conversion of malate into pyruvate. Patent TICKLAND-RG-1959-646&F=0">STICKLAND-RG-1959-646, Biochem. J. (1959), 73, 646. |
5. |
Stickland, R.G. Some properties of the malic enzyme of pigeon liver. 2. Synthesis of malate from pyruvate. Patent TICKLAND-RG-1959-654&F=0">STICKLAND-RG-1959-654, Biochem. J. (1959), 73, 654. |
6. |
Walker, D.A. Physiological studies on acid metabolism. 7. Malic enzyme from Kalanchoë crenata: effects of carbon dioxide concentration.. Patent WALKER-DA-1960-216, Biochem. J. (1960), 74, 216. |
|
[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 |
|
For diagram of the citric-acid cycle, click here |
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 target="new">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]. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9001-58-5 |
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. Patent THAWAY-JA-1963-2875&F=0">HATHAWAY-JA-1963-2875, J. Biol. Chem. (1963), 238, 2875. |
2. |
Kornberg, A. and Pricer, W.E. Di- and triphosphopyridine nucleotide isocitric dehydrogenase in yeast. Patent KORNBERG-A-1951-123, J. Biol. Chem. (1951), 189, 123. |
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. Patent T-GWE-1954-305&F=0">PLAUT-GWE-1954-305, J. Biol. Chem. (1954), 207, 305. |
5. |
Ramakrishnan, C.V. and Martin, S.M. Isocitric dehydrogenase in Aspergillus niger. Patent RAMAKRISHNAN-CV-1955-403, Arch. Biochem. Biophys. (1955), 55, 403. |
6. |
Vickery, H.B. A suggested new nomenclature for the isomers of isocitric acid. Patent VICKERY-HB-1962-1739, J. Biol. Chem. (1962), 237, 1739. |
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. Patent CAMACHO-ML-1995-85, FEMS Microbiol. Lett. (1995), 134, 85. |
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. [DOI] [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. [DOI] [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 |
|
For diagram of the citric-acid cycle, click here |
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 target="new">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]. |
Links to other databases: |
BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9028-48-2 |
References: |
1. |
Agosin, M.U. and Weinbach, E.C. Partial purification and characterization of the isocitric dehydrogenase from Trypanosoma cruzi. Patent AGOSIN-MU-1956-117, Biochim. Biophys. Acta (1956), 21, 117. |
2. |
Moyle, J. and Dixon, M. Purification of the isocitrate enzyme (triphosphopyridine nucleotide-linked isocitrate dehydrogenase-oxalosuccinate carboxylase). Patent MOYLE-J-1956-548, Biochem. J. (1956), 63, 548. |
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. Patent T-G-1957-965&F=0">SIEBERT-G-1957-965, J. Biol. Chem. (1957), 226, 965. |
5. |
Vickery, H.B. A suggested new nomenclature for the isomers of isocitric acid. Patent VICKERY-HB-1962-1739, J. Biol. Chem. (1962), 237, 1739. |
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. Patent CAMACHO-ML-1995-85, FEMS Microbiol. Lett. (1995), 134, 85. |
7. |
Steen, I.H., Lien, T. and Birkeland, N.-K. Biochemical and phylogenetic characterization of isocitrate dehydrogenase from a hyperthermophilic archaeon, Archaeoglobus fulgidus. Patent TEEN-IH-1997-412&F=0">STEEN-IH-1997-412, Arch. Microbiol. (1997), 168, 412. |
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. [DOI] [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. Patent CECCARELLI-C-2002-43454, J. Biol. Chem. (2002), 277, 43454. |
|
[EC 1.1.1.42 created 1961, modified 2005] |
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|
|
|
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 |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9001-82-5 |
References: |
1. |
Frampton, E.W. and Wood, W.A. Carbohydrate oxidation by Pseudomonas fluorescens. VI. Conversion of 2-keto-6-phosphogluconate to pyruvate. Patent TON-EW-1961-2571&F=0">FRAMPTON-EW-1961-2571, J. Biol. Chem. (1961), 236, 2571. |
|
[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+ |
|
For diagram of the pentose phosphate pathway (early stages), click here |
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. target="new">EC 1.1.1.343, phosphogluconate dehydrogenase (NAD+-dependent, decarboxylating). |
Links to other databases: |
BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9073-95-4 |
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. Patent DICKENS-F-1951-81, Biochem. J. (1951), 50, 81. |
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. Patent TREMOLI-S-1961-2975&F=0">PONTREMOLI-S-1961-2975, J. Biol. Chem. (1961), 236, 2975. |
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. Patent TT-DBM-1953-23&F=0">SCOTT-DBM-1953-23, Biochem. J. (1953), 55, 23. |
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. Patent TT-DBM-1957-686&F=0">SCOTT-DBM-1957-686, Biochem. J. (1957), 65, 686. |
5. |
Bridges, R.B., Palumbo, M.P. and Wittenberger, C.L. Purification and properties of an NADP-specific 6-phosphogluconate dehydrogenase from Streptococcus faecalis. Patent BRIDGES-RB-1975-6093, J. Biol. Chem. (1975), 250, 6093. |
6. |
Yoon, H., Anderson, C.D. and Anderson, B.M. Kinetic studies of Haemophilus influenzae 6-phosphogluconate dehydrogenase. Patent YOON-H-1989-75, Biochim. Biophys. Acta (1989), 994, 75. |
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. Patent ZAMBONI-N-2004-4528, J. Bacteriol. (2004), 186, 4528. |
|
[EC 1.1.1.44 created 1961, modified 2013] |
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|
|
|
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. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9028-51-7 |
References: |
1. |
Dworsky, P. and Hoffmann-Ostenhof, O. L-3-Aldonic acid dehydrogenase from Schwanniomyces occidentalis. Patent DWORSKY-P-1964-269, Acta Biochim. Pol. (1964), 11, 269. |
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. Patent SMILEY-JD-1961-357, J. Biol. Chem. (1961), 236, 357. |
|
[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 |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9028-52-8 |
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. target="new">EC 1.1.1.118, glucose 1-dehydrogenase (NAD+) and target="new">EC 1.1.1.119, glucose 1-dehydrogenase (NADP+). |
Links to other databases: |
BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9028-53-9 |
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. Patent BANAUCH-D-1975-101, Z. Klin. Chem. Klin. Biochem. (1975), 13, 101. |
2. |
Brink, N.G. Beef liver glucose dehydrogenase. 1. Purification and properties. Patent BRINK-NG-1953-1081, Acta Chem. Scand. (1953), 7, 1081. |
3. |
Pauly, H.E. and Pfleiderer, G. D-Glucose dehydrogenase from Bacillus megaterium M 1286: purification, properties and structure. Patent PAULY-HE-1975-1613, Hoppe-Seylers Z. Physiol. Chem. (1975), 356, 1613. |
4. |
Strecker, H.J. and Korkes, S. Glucose dehydrogenase. Patent TRECKER-HJ-1952-769&F=0">STRECKER-HJ-1952-769, J. Biol. Chem. (1952), 196, 769. |
5. |
Thompson, R.E. and Carper, W.R. Glucose dehydrogenase from pig liver. I. Isolation and purification. Biochim. Biophys. Acta 198 (1970) 397–406. [DOI] [PMID: 4392298] |
6. |
Fujita, Y., Ramaley, R. and Freese, E. Location and properties of glucose dehydrogenase in sporulating cells and spores of Bacillus subtilis. Patent TA-Y-1977-282&F=0">FUJITA-Y-1977-282, J. Bacteriol. (1977), 132, 282. |
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[EC 1.1.1.47 created 1961, modified 2013] |
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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. |
Links to other databases: |
BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9028-54-0 |
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. [DOI] [PMID: 14251301] |
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[EC 1.1.1.48 created 1961, modified 2011] |
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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+ |
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For diagram of the pentose phosphate pathway (early stages), click here |
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. target="new">EC 1.1.1.363, glucose-6-phosphate dehydrogenase [NAD(P)+] and target="new">EC 1.1.1.388, glucose-6-phosphate dehydrogenase (NAD+). |
Links to other databases: |
BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9001-40-5 |
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. Patent ENGEL-HJ-1969-509, Biochim. Biophys. Acta (1969), 191, 509. |
2. |
Glaser, L. and Brown, D.H. Purification and properties of D-glucose-6-phosphate dehydrogenase. Patent GLASER-L-1955-67, J. Biol. Chem. (1955), 216, 67. |
3. |
Julian, G.R., Wolfe, R.G. and Reithel, F.J. The enzymes of mammary gland. II. The preparation of glucose 6-phosphate dehydrogenase. Patent JULIAN-GR-1961-754, J. Biol. Chem. (1961), 236, 754. |
4. |
Noltmann, E.A., Gubler, C.J. and Kuby, S.A. Glucose 6-phosphate dehydrogenase (Zwischenferment). I. Isolation of the crystalline enzyme from yeast. Patent TMANN-EA-1961-1225&F=0">NOLTMANN-EA-1961-1225, J. Biol. Chem. (1961), 236, 1225. |
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. Patent T-E-2001-34840&F=0">MICLET-E-2001-34840, J. Biol. Chem. (2001), 276, 34840. |
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. [DOI] [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. [DOI] [PMID: 12435510] |
8. |
Ibraheem, O., Adewale, I.O. and Afolayan, A. Purification and properties of glucose 6-phosphate dehydrogenase from Aspergillus aculeatus. Patent IBRAHEEM-O-2005-584, J. Biochem. Mol. Biol. (2005), 38, 584. |
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. Patent IYER-RB-2002-283, Extremophiles (2002), 6, 283. |
10. |
Cho, S.W. and Joshi, J.G. Characterization of glucose-6-phosphate dehydrogenase isozymes from human and pig brain. Patent CHO-SW-1990-819, Neuroscience (1990), 38, 819. |
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[EC 1.1.1.49 created 1961, modified 2013, modified 2015] |
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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. target="new">EC 1.1.1.213, 3α-hydroxysteroid 3-dehydrogenase (Re-specific). |
Links to other databases: |
BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9028-56-2 |
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. Patent KOCHAKIAN-CD-1957-811, J. Biol. Chem. (1957), 224, 811. |
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. [DOI] [PMID: 3479982] |
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[EC 1.1.1.50 created 1961, modified 1986, modified 1990, modified 2012, modified 2013] |
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