The Enzyme Database

Displaying entries 51-100 of 2450.

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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.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, UM-BBD, CAS registry number: 9015-81-0
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+
For diagram of cholesterol catabolism (rings A, B and C), click here
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+).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9028-57-3
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. [DOI] [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.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9028-42-6
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.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9028-58-4
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+).
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, CAS registry number: 9028-43-7
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
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, CAS registry number: 9014-23-7
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.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9028-44-8
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
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9028-45-9
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
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, CAS registry number: 9028-59-5
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
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, CAS registry number: 9028-68-6
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+
For diagram of the 3-hydroxypropanoate/4-hydroxybutanoate cycle and dicarboxylate/4-hydroxybutanoate cycle in archaea, click here
Other name(s): γ-hydroxybutyrate dehydrogenase
Systematic name: 4-hydroxybutanoate:NAD+ oxidoreductase
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, CAS registry number: 9028-60-8
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)+.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9028-61-9
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. [DOI] [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.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9028-63-1
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.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, UM-BBD, CAS registry number: 9028-64-2
References:
1.  Holzer, H. and Schneider, S. Reinigung und charakterisierung einer TPN-abhängigen Pyridoxol-dehydrogenase aus bierhefe. Biochim. Biophys. Acta 48 (1961) 71–76. [DOI] [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.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9028-65-3
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. [DOI] [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
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, CAS registry number: 9001-65-4
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
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, CAS registry number: 9028-70-0
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+
For diagram of retinal and derivatives biosynthesis, click here
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.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, UM-BBD, CAS registry number: 37250-10-5
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
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, CAS registry number: 37250-11-6
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. [DOI] [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.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9031-31-6
References:
1.  Roche, B. and Azoulay, E. Régulation des alcool-déshydrogénases chez Saccharomyces cerevisiae. Eur. J. Biochem. 8 (1969) 426–434. [DOI] [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+.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37250-13-8
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. [DOI] [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.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Taylor, M.B. and Juni, E. Stereoisomeric specificities of 2,3-butanediol dehydrogenase. Biochim. Biophys. Acta 39 (1960) 448–457. [DOI] [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. [DOI] [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. [DOI] [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
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37250-15-0
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.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37250-16-1
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. [DOI] [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. [DOI] [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+.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 37250-17-2
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.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37250-18-3
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
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9059-44-3
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.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37250-19-4
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. [DOI] [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)
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37250-20-7
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
For diagram of pantothenate catabolism, click here
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.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37250-21-8
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)
For diagram of leucine biosynthesis, click here
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.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9030-97-1
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. [DOI] [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+
For diagram of isoleucine and valine biosynthesis, click here
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)+]).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9075-02-9
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. [DOI] [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+
For diagram of l-lysine synthesis, click here
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].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9067-90-7
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. [DOI] [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+
For diagram of mevalonate biosynthesis, click here
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)
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37250-24-1
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.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, UM-BBD, CAS registry number: 37250-26-3
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. [DOI] [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.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37250-27-4
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. [DOI] [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.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37250-28-5
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.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37250-29-6
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.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37250-30-9
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+
For diagram of serine biosynthesis, click here
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].
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9075-29-0
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. [DOI] [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. [DOI] [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.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, CAS registry number: 37250-31-0
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
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9075-73-4
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
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37250-32-1
References:
1.  Levis, G.M. 2-Hydroxy fatty acid oxidases of rat kidney. Biochem. Biophys. Res. Commun. 38 (1970) 470–477. [DOI] [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
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37250-33-2
References:
1.  Levis, G.M. 2-Hydroxy fatty acid oxidases of rat kidney. Biochem. Biophys. Res. Commun. 38 (1970) 470–477. [DOI] [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.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 37250-34-3
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. [DOI] [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. [DOI] [PMID: 4381013]
[EC 1.1.1.100 created 1972, modified 1976]
 
 


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