EC 1.1.1 With NAD+ or NADP+ as acceptor
EC 1.1.2 With a cytochrome as acceptor
EC 1.1.3 With oxygen as acceptor
EC 1.1.4 With a disulfide as acceptor
EC 1.1.5 With a quinone or similar compound as acceptor
EC 1.1.98 With other, known, physiological acceptors
EC 1.1.99 With unknown physiological acceptors
See separate file for EC 1.1.1.51 to EC 1.1.1.100
EC 1.1.1.101 to EC 1.1.1.150
EC 1.1.1.151 to EC 1.1.1.200
EC 1.1.1.201 to EC 1.1.1.250
EC 1.1.1.251 to EC 1.1.1.300
EC 1.1.1.301 to EC 1.1.1.350
EC 1.1.1.351 to EC 1.1.1.441
EC 1.1.1.51 to EC 1.1.1.100
EC 1.1.1.101 to EC 1.1.1.150
EC 1.1.1.151 to EC 1.1.1.200
EC 1.1.1.201 to EC 1.1.1.250
EC 1.1.1.251 to EC 1.1.1.300
EC 1.1.1.301 to EC 1.1.1.350
EC 1.1.1.351 to EC 1.1.1.441
Accepted name: alcohol dehydrogenase
Reaction: (1) a primary alcohol + NAD+ = an aldehyde + NADH + H+
(2) a secondary alcohol + NAD+ = a ketone + NADH + H+
Other name(s): aldehyde reductase; ADH; alcohol dehydrogenase (NAD); aliphatic alcohol dehydrogenase; ethanol dehydrogenase; NAD-dependent alcohol dehydrogenase; NAD-specific aromatic alcohol dehydrogenase; NADH-alcohol dehydrogenase; NADH-aldehyde dehydrogenase; primary alcohol dehydrogenase; yeast alcohol dehydrogenase
Systematic name: alcohol:NAD+ oxidoreductase
Comments: A zinc protein. Acts on primary or secondary alcohols or hemi-acetals with very broad specificity; however the enzyme oxidizes methanol much more poorly than ethanol. The animal, but not the yeast, enzyme acts also on cyclic secondary alcohols.
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 ed., vol. 11, Academic Press, New York, 1975, p. 103-190.
2. Jörnvall, H. Differences between alcohol dehydrogenases. Structural properties and evolutionary aspects. Eur. J. Biochem. 72 (1977) 443-452. [PMID: 320001]
3. Negelein, E. and Wulff, H.-J. Diphosphopyridinproteid Alkohol, acetaldehyd. Biochem. Z. 293 (1937) 351-389.
4. Sund, H. and Theorell, H. Alcohol dehydrogenase. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Eds.), The Enzymes, 2nd ed., vol. 7, Academic Press, New York, 1963, p. 25-83.
5. Theorell, H. Kinetics and equilibria in the liver alcohol dehydrogenase system. Adv. Enzymol. Relat. Subj. Biochem. 20 (1958) 31-49.
Accepted name: alcohol dehydrogenase (NADP+)
Reaction: an alcohol + NADP+ = an aldehyde + NADPH + H+
Other name(s): aldehyde reductase (NADPH2); NADP-alcohol dehydrogenase; NADP+-aldehyde reductase; NADP+-dependent aldehyde reductase; NADPH-aldehyde reductase; NADPH-dependent aldehyde reductase; nonspecific succinic semialdehyde reductase; ALR 1; low-Km aldehyde reductase; high-Km aldehyde reductase; alcohol dehydrogenase (NADP)
Systematic name: alcohol:NADP+ oxidoreductase
Comments: A zinc protein. Some members of this group oxidize only primary alcohols; others act also on secondary alcohols. May be identical with EC 1.1.1.19 (L-glucuronate reductase), EC 1.1.1.33 [mevaldate reductase (NADPH)] and EC 1.1.1.55 [lactaldehyde reductase (NADPH)]. Re-specific with respect to NADPH.
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. Int. J. Biochem. 2 (1971) 55-64.
4. Tabakoff, B. and Erwin, V.G. Purification and characterization of a reduced nicotinamide adenine dinucleotide phosphate-linked aldehyde reductase from brain. J. Biol. Chem. 245 (1970) 3263-3268. [PMID: 4393513]
Accepted name: homoserine dehydrogenase
Reaction: L-homoserine + NAD(P)+ = L-aspartate 4-semialdehyde + NAD(P)H + H+
For diagram 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 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. J. Biol. Chem. 213 (1955) 51-60.
2. Starnes, W.L., Munk, P., Maul, S.B., Cunningham, G.N., Cox, D.J. and Shive, W. Threonine-sensitive aspartokinase-homoserine dehydrogenase complex, amino acid composition, molecular weight, and subunit composition of the complex. Biochemistry 11 (1972) 677-687. [PMID: 4551091]
3. Véron, M., Falcoz-Kelly, F. and Cohen, G.N. The threonine-sensitive homoserine dehydrogenase and aspartokinase activities of Escherichia coli K12. The two catalytic activities are carried by two independent regions of the polypeptide chain. Eur. J. Biochem. 28 (1972) 520-527. [PMID: 4562990]
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. J. Biol. Chem. 211 (1954) 263-270.
2. Taylor, M.B. and Juni, E. Stereoisomeric specificities of 2,3-butanediol dehydrogenase. Biochim. Biophys. Acta 39 (1960) 448-457.
[EC 1.1.1.5 Transferred entry: acetoin dehydrogenase. Now EC 1.1.1.303, diacetyl reductase [(R)-acetoin forming] and EC 1.1.1.304, diacetyl reductase [(S)-acetoin forming] (EC 1.1.1.5 created 1961, modified 1976, deleted 2010)]
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.
2. Burton, R.M. and Kaplan, N.O. A DPN specific glycerol dehydrogenase from Aerobacter aerogenes. J. Am. Chem. Soc. 75 (1953) 1005-1007.
3. Lin, E.C.C. and Magasanik, B. The activation of glycerol dehydrogenase from Aerobacter aerogenes by monovalent cations. J. Biol. Chem. 235 (1960) 1820-1823.
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.
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; 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)
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. (Eds.), The Enzymes, 2nd ed., vol. 7, Academic Press, New York, 1963, pp. 85-96.
2. Brosemer, R.W. and Kuhn, R.W. Comparative structural properties of honeybee and rabbit α-glycerophosphate dehydrogenases. Biochemistry 8 (1969) 2095-2105. [PMID: 4307630]
3. O'Brien, S.J. and MacIntyre, R.J. The α-glycerophosphate cycle in Drosophila melanogaster. I. Biochemical and developmental aspects. Biochem. Genet. 7 (1972) 141-161. [PMID: 4340553]
4. Warkentin, K.L. and Fondy, T.P. Isolation and characterization of cytoplasmic L-glycerol-3-phosphate dehydrogenase from rabbit-renal-adipose tissue and its comparison with the skeletal-muscle enzyme. Eur. J. Biochem. 36 (1973) 97-109. [PMID: 4200180]
5. Albertyn, J., van Tonder, A. and Prior, B.A. Purification and characterization of glycerol-3-phosphate dehydrogenase of Saccharomyces cerevisiae. FEBS Lett. 308 (1992) 130-132. [PMID: 1499720]
6. Koekemoer, T.C., Litthauer, D. and Oelofsen, W. Isolation and characterization of adipose tissue glycerol-3-phosphate dehydrogenase. Int. J. Biochem. Cell. Biol. 27 (1995) 625-632. [PMID: 7671141]
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. Biochem. Biophys. Res. Commun. 3 (1960) 554-559.
2. Hickman, J. and Ashwell, G. A sensitive and stereospecific enzymatic assay for xylulose. J. Biol. Chem. 234 (1959) 758-761.
3. Jakoby, W.B. and Fredericks, J. Erythritol dehydrogenase from Aerobacter aerogenes. Biochim. Biophys. Acta 48 (1961) 26-32.
Accepted name: L-xylulose reductase
Reaction: xylitol + NADP+ = L-xylulose + NADPH + H+
For diagram of reaction 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. J. Bacteriol. 161 (1985) 529-533. [PMID: 2981816]
2. Hickman, J. and Ashwell, G. A sensitive and stereospecific enzymatic assay for xylulose. J. Biol. Chem. 234 (1959) 758-761.
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.
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.
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. J. Biol. Chem. 236 (1961) 31-36.
2. Wood, W.A., McDonough, M.J. and Jacobs, L.B. Ribitol and D-arabitol utilization by Aerobacter aerogenes. J. Biol. Chem. 236 (1961) 2190-2195.
Accepted name: L-arabinitol 4-dehydrogenase
Reaction: L-arabinitol + NAD+ = L-xylulose + NADH + H+
For diagram of reaction 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. Biochem. Biophys. Res. Commun. 3 (1960) 554-559.
2. Chiang, C. and Knight, S.G. L-Arabinose metabolism by cell-free extracts of Penicillium chrysogenum. Biochim. Biophys. Acta 46 (1961) 271-278.
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. Biochim. Biophys. Acta 46 (1961) 271-278.
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. Int. J. Biochem. 15 (1983) 507-511. [PMID: 6852349]
3. Leissing, N. and McGuinness, E.T. Rapid affinity purification and properties of rat liver sorbitol dehydrogenase. Biochim. Biophys. Acta 524 (1978) 254-261. [PMID: 667078]
4. Negm, F.B. and Loescher, W.H. Detection and characterization of sorbitol dehydrogenase from apple callus tissue. Plant Physiol. 64 (1979) 69-73. [PMID: 16660917]
5. O'Brien, M.M., Schofield, P.J. and Edwards, M.R. Polyol-pathway enzymes of human brain. Partial purification and properties of sorbitol dehydrogenase. Biochem. J. 211 (1983) 81-90. [PMID: 6870831]
6. Ng, K., Ye, R., Wu, X.C. and Wong, S.L. Sorbitol dehydrogenase from Bacillus subtilis. Purification, characterization, and gene cloning. J. Biol. Chem. 267 (1992) 24989-24994. [PMID: 1460002]
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. Biochem. J. 64 (1956) 394-405.
Accepted name: galactitol 2-dehydrogenase
Reaction: galactitol + NAD+ = D-tagatose + NADH + H+
For diagram of reaction click here.
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.
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. Biochem. J. 64 (1956) 394-405.
2. Wichelecki, D.J., Vetting, M.W., Chou, L., Al-Obaidi, N., Bouvier, J.T., Almo, S.C. and Gerlt, J.A. ATP-binding cassette (ABC) transport system solute-binding protein-guided identification of novel D-altritol and galactitol catabolic pathways in Agrobacterium tumefaciens C58. J. Biol. Chem. 290 (2015) 28963Ð28976. [PMID: 26472925]
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. J. Biol. Chem. 214 (1955) 383-396.
2. Wolfe, J.B. and Kaplan, N.O. Hexose phosphate and hexose reductase. A. D-Mannitol-1-phosphate dehydrogenase from E. coli. Methods Enzymol. 1 (1955) 346-348.
3. Wolfe, J.B. and Kaplan, N.O. D-Mannitol 1-phosphate dehydrogenase from Escherichia coli. J. Biol. Chem. 218 (1956) 849-869.
Accepted name: inositol 2-dehydrogenase
Reaction: myo-inositol + NAD+ = 2,4,6/3,5-pentahydroxycyclohexanone + NADH + H+
For diagram of reaction click here.
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.
3. Vidal-Lieria, M. and van Uden, N. Inositol dehydrogenase from the yeast Cryptococcus melibiosum. Biochim. Biophys. Acta 293 (1973) 295-303. [PMID: 4351258]
Accepted name: glucuronate reductase
Reaction: L-gulonate + NADP+ = D-glucuronate + NADPH + H+
For diagram click here.
Other name(s): L-hexonate:NADP dehydrogenase; TPN-L-gulonate dehydrogenase; aldehyde reductase II; NADP-L-gulonate dehydrogenase; D-glucuronate dehydrogenase; D-glucuronate reductase; L-glucuronate reductase (incorrect)
Systematic name: L-gulonate:NADP+ 6-oxidoreductase
Comments: Also reduces D-galacturonate. May be identical with EC 1.1.1.2 [alcohol dehydrogenase (NADP+)].
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. Biochim. Biophys. Acta 53 (1961) 426-428.
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, p. 249-260.
3. York, J.L., Grollman, A.P. and Bublitz, C. TPN-L-gulonate dehydrogenase. Biochim. Biophys. Acta 47 (1961) 298-306.
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. J. Biochem. (Tokyo) 48 (1960) 313-315.
Accepted name: aldose reductase
Reaction: alditol + NAD(P)+ = aldose + NAD(P)H + H+
For diagram of reaction 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. Biochim. Biophys. Acta 370 (1974) 358-368. [PMID: 4216364]
2. Boghosian, R.A. and McGuinness, E.T. Affinity purification and properties of porcine brain aldose reductase. Biochim. Biophys. Acta 567 (1979) 278-286. [PMID: 36151]
3. Hers, H.G. L’Aldose-réductase. Biochim. Biophys. Acta 37 (1960) 120-126. [PMID: 14401390]
4. Scher, B.M. and Horecker, B.L. Pentose metabolism in Candida. 3. The triphosphopyridine nucleotide-specific polyol dehydrogenase of Candida utilis. Arch. Biochem. Biophys. 116 (1966) 117-128. [PMID: 4381350]
Accepted name: UDP-glucose 6-dehydrogenase
Reaction: UDP-α-D-glucose + 2 NAD+ + H2O = UDP-α-D-glucuronate + 2 NADH + 2 H+
For diagram of reaction 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-glucose:NAD+ 6-oxidoreductase
Comments: Also acts on UDP-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. [PMID: 1091296]
2. Maxwell, E.S., Kalckar, H.M. and Strominger, J.L. Some properties of uridine diphosphoglucose dehydrogenase. Arch. Biochem. Biophys. 65 (1956) 2-10.
3. Strominger, J.L. and Mapson, L.W. Uridine diphosphoglucose dehydrogenase of pea seedlings. Biochem. J. 66 (1957) 567-572.
4. Strominger, J.L., Maxwell, E.S., Axelrod, J. and Kalckar, H.M. Enzymatic formation of uridine diphosphogluconic acid. J. Biol. Chem. 224 (1957) 79-90.
Accepted name: histidinol dehydrogenase
Reaction: L-histidinol + 2 NAD+ + H2O = L-histidine + 2 NADH + 3 H+
For diagram click here.
Other name(s): L-histidinol dehydrogenase
Systematic name: L-histidinol:NAD+ oxidoreductase
Comments: Also oxidizes L-histidinal. The Neurospora enzyme also catalyses the reactions of EC 3.5.4.19 (phosphoribosyl-AMP cyclohydrolase) and EC 3.6.1.31 (phosphoribosyl-ATP diphosphatase).
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. J. Biol. Chem. 209 (1954) 829-846.
2. Adams, E. L-Histidinal, a biosynthetic precursor of histidine. J. Biol. Chem. 217 (1955) 325-344.
3. Loper, J.C. Histidinol dehydrogenase from Salmonella typhimurium. Crystallization and composition studies. J. Biol. Chem. 243 (1968) 3264-3272. [PMID: 4872177]
4. Yourno, J. and Ino, I. Purification and crystallization of histidinol dehydrogenase from Salmonella typhimurium LT-2. J. Biol. Chem. 243 (1968) 3273-3276. [PMID: 4872176]
Accepted name: quinate/shikimate dehydrogenase (NAD+)
Reaction: L-quinate + NAD+ = 3-dehydroquinate + NADH + H+
For diagram of rection, click here
Glossary: quinate = (1R,3R,4R,5R)-1,3,4,5-tetrahydroxycyclohexanecarboxylic acid and is a cyclitol carboxylate
The numbering system used for the 3-dehydroquinate is that of the recommendations on cyclitols, sections I-8 and I-9: and is shown in the reaction diagram. The use of the term '5-dehydroquinate' for this compound is based on an earlier system of numbering.
Other name(s): quinate dehydrogenase (ambiguous); quinic dehydrogenase (ambiguous); quinate:NAD oxidoreductase; quinate 5-dehydrogenase (ambiguous); quinate:NAD+ 5-oxidoreductase
Systematic name: L-quinate:NAD+ 3-oxidoreductase
Comments: The enzyme, found mostly in bacteria (mostly, but not exclusively in Gram-positive bacteria), fungi, and plants, participates in the degradation of quinate and shikimate with a strong preference for NAD+ as a cofactor. While the enzyme can act on both quinate and shikimate, activity is higher with the former. cf. EC 1.1.5.8, quinate/shikimate dehydrogenase (quinone), EC 1.1.1.282, quinate/shikimate dehydrogenase [NAD(P)+], and EC 1.1.1.25, shikimate dehydrogenase (NADP+).
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. Biochim. Biophys. Acta 15 (1954) 268-280. [PMID: 13208693]
2. Gamborg, O.L. Aromatic metabolism in plants. III. Quinate dehydrogenase from mung bean cell suspension cultures. Biochim. Biophys. Acta 128 (1966) 483-491.
3. Hawkins, A.R., Giles, N.H. and Kinghorn, J.R. Genetical and biochemical aspects of quinate breakdown in the filamentous fungus Aspergillus nidulans. Biochem. Genet. 20 (1982) 271-286. [PMID: 7049157]
4. Singh, S., Stavrinides, J., Christendat, D. and Guttman, D.S. A phylogenomic analysis of the shikimate dehydrogenases reveals broadscale functional diversification and identifies one functionally distinct subclass. Mol. Biol. Evol. 25 (2008) 2221-2232. [PMID: 18669580]
5. Teramoto, H., Inui, M. and Yukawa, H. Regulation of expression of genes involved in quinate and shikimate utilization in Corynebacterium glutamicum. Appl. Environ. Microbiol. 75 (2009) 3461-3468. [PMID: 19376919]
6. Kubota, T., Tanaka, Y., Hiraga, K., Inui, M. and Yukawa, H. Characterization of shikimate dehydrogenase homologues of Corynebacterium glutamicum. Appl. Microbiol. Biotechnol. 97 (2013) 8139-8149. [PMID: 23306642]
7. Peek, J. and Christendat, D. The shikimate dehydrogenase family: functional diversity within a conserved structural and mechanistic framework. Arch. Biochem. Biophys. 566 (2015) 85-99. [PMID: 25524738]
Accepted name: shikimate dehydrogenase (NADP+)
Reaction: shikimate + NADP+ = 3-dehydroshikimate + NADPH + H+
For diagram of reaction, 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 EC 4.2.1.10, 3-dehydroquinate dehydratase [4]. cf. EC 1.1.1.24, quinate/shikimate dehydrogenase (NAD+), EC 1.1.5.8, quinate/shikimate dehydrogenase (quinone), and EC 1.1.1.282, quinate/shikimate dehydrogenase [NAD(P)+].
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. Biochim. Biophys. Acta 15 (1954) 268-280. [PMID: 13208693]
2. Yaniv, H. and Gilvarg, C. Aromatic biosynthesis. XIV. 5-Dehydroshikimic reductase. J. Biol. Chem. 213 (1955) 787-795. [PMID: 14367339]
3. Balinsky, D. and Davies, D.D. Aromatic biosynthesis in higher plants. 1. Preparation and properties of dehydroshikimic reductase. Biochem. J. 80 (1961) 292-296. [PMID: 13686342]
4. Chaudhuri, S. and Coggins, J.R. The purification of shikimate dehydrogenase from Escherichia coli. Biochem. J. 226 (1985) 217-223. [PMID: 3883995]
5. Anton, I.A. and Coggins, J.R. Sequencing and overexpression of the Escherichia coli aroE gene encoding shikimate dehydrogenase. Biochem. J. 249 (1988) 319-326. [PMID: 3277621]
6. Ye, S., Von Delft, F., Brooun, A., Knuth, M.W., Swanson, R.V. and McRee, D.E. The crystal structure of shikimate dehydrogenase (AroE) reveals a unique NADPH binding mode. J. Bacteriol. 185 (2003) 4144-4151. [PMID: 12837789]
Accepted name: glyoxylate reductase
Reaction: glycolate + NAD+ = glyoxylate + NADH + H+
For diagram of reaction 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, vMetacyc, PDB, CAS registry number: 9028-32-4
References:
1. Zelitch, I. Oxidation and reduction of glycolic and glyoxylic acids in plants. II. Glyoxylic acid reductase. J. Biol. Chem. 201 (1953) 719-726.
2. Zelitch, I. The isolation and action of crystalline glyoxylic acid reductase from tobacco leaves. J. Biol. Chem. 216 (1955) 553-575.
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. J. Biol. Chem. 235 (1960) 810-818.
2. Everse, J. and Kaplan, N.O. Lactate dehydrogenases: structure and function. Adv. Enzymol. Relat. Subj. Biochem. 37 (1973) 61-133. [PMID: 4146647]
3. Holbrook, J.J., Liljas, A., Steindel, S.J. and Rossmann, M.G. Lactate dehydrogenase. In: Boyer, P.D. (Ed.), The Enzymes, 3rd ed., vol. 11, Academic Press, New York, 1975, p. 191-292.
4. Schär, H.-P. and Zuber, H. Structure and function of L-lactate dehydrogenases from thermophilic and mesophilic bacteria. I) Isolation and characterization of lactate dehydrogenases from thermophilic and mesophilic bacilli. Hoppe-Seyler's Z. Physiol. Chem. 360 (1979) 795-807. [PMID: 114469]
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. J. Biol. Chem. 235 (1960) 810-818.
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. Biochem. Z. 329 (1957) 292-312 (in German). [PMID: 13522707]
2. Stafford, H.A., Magaldi, A. and Vennesland, B. The enzymatic reduction of hydroxypyruvic acid to D-glyceric acid in higher plants. J. Biol. Chem. 207 (1954) 621-629. [PMID: 13163046]
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. Biochem. J. 102 (1967) 423-431. [PMID: 4291491]
2. Delafield, F.P., Cooksey, K.E. and Doudoroff, M. β-Hydroxybutyric dehydrogenase and dimer hydrolase of Pseudomonas lemoignei. J. Biol. Chem. 240 (1965) 4023-4028. [PMID: 4954074]
3. Lehninger, A.L., Sudduth, H.C. and Wise, J.B. D-β-Hydroxybutyric dehydrogenase of mitochondria. J. Biol. Chem. 235 (1960) 2450-2455.
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. J. Biol. Chem. 225 (1957) 511-521.
[EC 1.1.1.32 Deleted entry: mevaldate reductase, now included with EC 1.1.1.1, alcohol dehydrogenase. (EC 1.1.1.32 created 1961, deleted 2022)]
[EC 1.1.1.33 Deleted entry: mevaldate reductase (NADPH), now included with EC 1.1.1.2, alcohol dehydrogenase (NADP+). (EC 1.1.1.33 created 1961, deleted 2022)]
Accepted name: hydroxymethylglutaryl-CoA reductase (NADPH)
Reaction: (R)-mevalonate + CoA + 2 NADP+ = (S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
For diagram 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 EC 2.7.1.109 {[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase} and reactivated by 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. Biochim. Biophys. Acta 40 (1960) 491-501.
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.
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]
Accepted name: 3-hydroxyacyl-CoA dehydrogenase
Reaction: (S)-3-hydroxyacyl-CoA + NAD+ = 3-oxoacyl-CoA + NADH + H+
For diagram of reaction click here or another example click here.
Other name(s): β-hydroxyacyl dehydrogenase; β-keto-reductase; 3-keto reductase; 3-hydroxyacyl coenzyme A dehydrogenase; β-hydroxyacyl-coenzyme A synthetase; β-hydroxyacylcoenzyme A dehydrogenase; β-hydroxybutyrylcoenzyme A dehydrogenase; 3-hydroxyacetyl-coenzyme A dehydrogenase; L-3-hydroxyacyl coenzyme A dehydrogenase; L-3-hydroxyacyl CoA dehydrogenase; β-hydroxyacyl CoA dehydrogenase; 3β-hydroxyacyl coenzyme A dehydrogenase; 3-hydroxybutyryl-CoA dehydrogenase; β-ketoacyl-CoA reductase; β-hydroxy acid dehydrogenase; 3-L-hydroxyacyl-CoA dehydrogenase; 3-hydroxyisobutyryl-CoA dehydrogenase; 1-specific DPN-linked β-hydroxybutyric dehydrogenase
Systematic name: (S)-3-hydroxyacyl-CoA:NAD+ oxidoreductase
Comments: Also oxidizes S-3-hydroxyacyl-N-acylthioethanolamine and S-3-hydroxyacyl-hydrolipoate. Some enzymes act, more slowly, with NADP+. Broad specificity to acyl chain-length (cf. EC 1.1.1.211 [long-chain-3-hydroxyacyl-CoA dehydrogenase]).
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. Biochim. Biophys. Acta 334 (1974) 12-23.
2. Lehninger, A.L. and Greville, G.D. The enzymatic oxidation of d- and l-β-hydroxybutyrate. Biochim. Biophys. Acta 12 (1953) 188-202. [PMID: 13115428]
3. Stern, J.R. Crystalline β-hydroxybutyrate dehydrogenase from pig heart. Biochim. Biophys. Acta 26 (1957) 448-449.
4. Wakil, S.J., Green, D.E., Mii, S. and Mahler, H.R. Studies on the fatty acid oxidizing system of animal tissues. VI. β-Hydroxyacyl coenzyme A dehydrogenase. J. Biol. Chem. 207 (1954) 631-638.
Accepted name: acetoacetyl-CoA reductase
Reaction: (R)-3-hydroxyacyl-CoA + NADP+ = 3-oxoacyl-CoA + NADPH + H+
For diagram of reaction click here or 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. J. Biol. Chem. 237 (1962) 687-693.
Accepted name: malate dehydrogenase
Reaction: (S)-malate + NAD+ = oxaloacetate + NADH + H+
For diagram of reaction click here (another example or another example).
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: Also oxidizes some other 2-hydroxydicarboxylic acids.
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 ed., vol. 11, Academic Press, New York, 1975, p. 369-396.
2. Guha, A., Englard, S. and Listowsky, I. Beef heart malic dehydrogenases. VII. Reactivity of sulfhydryl groups and conformation of the supernatant enzyme. J. Biol. Chem. 243 (1968) 609-615. [PMID: 5637713]
3. McReynolds, M.S. and Kitto, G.B. Purification and properties of Drosophila malate dehydrogenases. Biochim. Biophys. Acta 198 (1970) 165-175. [PMID: 4313528]
4. Wolfe, R.G. and Nielands, J.B. Some molecular and kinetic properties of heart malic dehydrogenase. J. Biol. Chem. 221 (1956) 61-69.
Accepted name: malate dehydrogenase (oxaloacetate-decarboxylating)
Reaction: (1) (S)-malate + NAD+ = pyruvate + CO2 + NADH
(2) oxaloacetate = pyruvate + CO2
Other name(s): 'malic' enzyme (ambiguous); pyruvic-malic carboxylase (ambiguous); NAD-specific malic enzyme; NAD-malic enzyme; NAD-linked malic enzyme
Systematic name: (S)-malate:NAD+ oxidoreductase (oxaloacetate-decarboxylating)
Comments: Unlike EC 1.1.1.39, malate dehydrogenase (decarboxylating), this enzyme can also decarboxylate oxaloacetate. cf. EC 1.1.1.40, malate dehydrogenase (oxaloacetate-decarboxylating) (NADP+).
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. J. Biol. Chem. 192 (1951) 301-312.
Accepted name: malate dehydrogenase (decarboxylating)
Reaction: (S)-malate + NAD+ = pyruvate + CO2 + NADH
Other name(s): 'malic' enzyme; pyruvic-malic carboxylase; NAD-specific malic enzyme; NAD-malic enzyme
Systematic name: (S)-malate:NAD+ oxidoreductase (decarboxylating)
Comments: There are several forms of malate dehydrogenases that differ in their use of substrates and cofactors. This particular form is found only in the plant kingdom. Unlike EC 1.1.1.38, which catalyses a similar reaction, this enzyme can not bind oxaloacetate, and thus does not decarboxylate exogeneously-added oxaloacetate. cf. EC 1.1.1.37, malate dehydrogenase; EC 1.1.1.38, malate dehydrogenase (oxaloacetate-decarboxylating); and EC 1.1.1.83, D-malate dehydrogenase (decarboxylating).
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. Biochem. J. 122 (1971) 495Ð501. [PMID: 4399380]
2. Grover, S.D., Canellas, P.F. and Wedding, R.T. Purification of NAD malic enzyme from potato and investigation of some physical and kinetic properties. Arch. Biochem. Biophys. 209 (1981) 396Ð407. [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) 1021Ð1028. [PMID: 16663114]
4. Wedding, R.T. Malic enzymes of higher plants: characteristics, regulation, and physiological function. Plant Physiol. 90 (1989) 367Ð371. [PMID: 16666776]
Accepted name: malate dehydrogenase (oxaloacetate-decarboxylating) (NADP+)
Reaction: (1) (S)-malate + NADP+ = pyruvate + CO2 + NADPH
(2) oxaloacetate = pyruvate + CO2
Other name(s): 'malic' enzyme (ambiguous); pyruvic-malic carboxylase (ambiguous); malate dehydrogenase (decarboxylating, NADP+); NADP+-linked decarboxylating malic enzyme; NADP+-malic enzyme; NADP+-specific malic enzyme; NADP-specific malate dehydrogenase; malate dehydrogenase (NADP+, decarboxylating); L-malate:NADP+ oxidoreductase
Systematic name: (S)-malate:NADP+ oxidoreductase (oxaloacetate-decarboxylating)
Comments: The enzyme catalyses the oxidative decarboxylation of (S)-malate in the presence of NADP+ and divalent metal ions, and the decarboxylation of oxaloacetate. cf. EC 1.1.1.38, malate dehydrogenase (oxaloacetate-decarboxylating), and EC 1.1.1.39, malate dehydrogenase (decarboxylating).
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. J. Biol. Chem. 203 (1953) 595-604.
2. Ochoa, S., Mehler, A.H. and Kornberg, A. Biosynthesis of dicarboxylic acids by carbon dioxide fixation. I. Isolation and properties of an enzyme from pigeon liver catalyzing the reversible oxidative decarboxylation of l-malic acid. J. Biol. Chem. 174 (1948) 979-1000.
3. Rutter, W.J. and Lardy, H.A. Purification and properties of pigeon liver malic enzyme. J. Biol. Chem. 233 (1958) 374-382.
4. Stickland, R.G. Some properties of the malic enzyme of pigeon liver. 1. Conversion of malate into pyruvate. Biochem. J. 73 (1959) 646-654.
5. Stickland, R.G. Some properties of the malic enzyme of pigeon liver. 2. Synthesis of malate from pyruvate. Biochem. J. 73 (1959) 654-659.
6. Walker, D.A. Physiological studies on acid metabolism. 7. Malic enzyme from Kalanchoë crenata: effects of carbon dioxide concentration. Biochem. J. 74 (1960) 216-223.
Accepted name: isocitrate dehydrogenase (NAD+)
Reaction: isocitrate + NAD+ = 2-oxoglutarate + CO2 + NADH
For diagram 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 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. J. Biol. Chem. 238 (1963) 2875-2881. [PMID: 14063317]
2. Kornberg, A. and Pricer, W.E. Di- and triphosphopyridine nucleotide isocitric dehydrogenase in yeast. J. Biol. Chem. 189 (1951) 123-136. [PMID: 14832224]
3. Plaut, G.W.E. Isocitrate dehydrogenases. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Eds.), The Enzymes, 2nd ed., vol. 7, Academic Press, New York, 1963, pp. 105-126.
4. Plaut, G.W.E. and Sung, S.-C. Diphosphopyridine nucleotide isocitric dehydrogenase from animal tissues. J. Biol. Chem. 207 (1954) 305-314. [PMID: 13152105]
5. Ramakrishnan, C.V. and Martin, S.M. Isocitric dehydrogenase in Aspergillus niger. Arch. Biochem. Biophys. 55 (1955) 403-407.
6. Vickery, H.B. A suggested new nomenclature for the isomers of isocitric acid. J. Biol. Chem. 237 (1962) 1739-1741. [PMID: 13925783]
7. Camacho, M.L., Brown, R.A., Bonete, M.J., Danson, M.J. and Hough, D.W. Isocitrate dehydrogenases from Haloferax volcanii and Sulfolobus solfataricus: enzyme purification, characterisation and N-terminal sequence. FEMS Microbiol. Lett. 134 (1995) 85-90. [PMID: 8593959]
8. Kim, Y.O., Koh, H.J., Kim, S.H., Jo, S.H., Huh, J.W., Jeong, K.S., Lee, I.J., Song, B.J. and Huh, T.L. Identification and functional characterization of a novel, tissue-specific NAD+-dependent isocitrate dehydrogenase β subunit isoform. J. Biol. Chem. 274 (1999) 36866-36875. [PMID: 10601238]
9. Inoue, H., Tamura, T., Ehara, N., Nishito, A., Nakayama, Y., Maekawa, M., Imada, K., Tanaka, H. and Inagaki, K. Biochemical and molecular characterization of the NAD+-dependent isocitrate dehydrogenase from the chemolithotroph Acidithiobacillus thiooxidans. FEMS Microbiol. Lett. 214 (2002) 127-132. [PMID: 12204383]
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 click here or 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; isocitrate dehydrogenase (NADP); oxalsuccinic decarboxylase; isocitrate (NADP) dehydrogenase; isocitrate (nicotinamide adenine dinucleotide phosphate) dehydrogenase; NADP-specific isocitrate dehydrogenase; NADP-linked isocitrate dehydrogenase; NADP-dependent isocitrate dehydrogenase; NADP isocitric dehydrogenase; isocitrate dehydrogenase (NADP-dependent); NADP-dependent isocitric dehydrogenase; triphosphopyridine nucleotide-linked isocitrate dehydrogenase-oxalosuccinate carboxylase; NADP+-linked isocitrate dehydrogenase; IDH (ambiguous); dual-cofactor-specific isocitrate dehydrogenase; NADP+-ICDH; NADP+-IDH; IDP; IDP1; IDP2; IDP3
Systematic name: isocitrate:NADP+ oxidoreductase (decarboxylating)
Comments: Requires Mn2+ or Mg2+ for activity. Unlike EC 1.1.1.41, isocitrate dehydrogenase (NAD+), oxalosuccinate can be used as a substrate. In eukaryotes, isocitrate dehydrogenase exists in two forms: an NAD+-linked enzyme found only in mitochondria and displaying allosteric properties, and a non-allosteric, NADP+-linked enzyme that is found in both mitochondria and cytoplasm [6]. The enzyme from some species can also use NAD+ but much more slowly [6,7].
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. Biochim. Biophys. Acta 21 (1956) 117-126. [PMID: 13363868]
2. Moyle, J. and Dixon, M. Purification of the isocitrate enzyme (triphosphopyridine nucleotide-linked isocitrate dehydrogenase-oxalosuccinate carboxylase). Biochem. J. 63 (1956) 548-552. [PMID: 13355848]
3. Plaut, G.W.E. Isocitrate dehydrogenases. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Eds.), The Enzymes, 2nd ed., vol. 7, Academic Press, New York, 1963, p. 105-126.
4. Siebert, G., Dubuc, J., Warner, R.C. and Plaut, G.W.E. The preparation of isocitrate dehydrogenase from mammalian heart. J. Biol. Chem. 226 (1957) 965-975. [PMID: 13438885]
5. Vickery, H.B. A suggested new nomenclature for the isomers of isocitric acid. J. Biol. Chem. 237 (1962) 1739-1741. [PMID: 13925783]
6. Camacho, M.L., Brown, R.A., Bonete, M.J., Danson, M.J. and Hough, D.W. Isocitrate dehydrogenases from Haloferax volcanii and Sulfolobus solfataricus: enzyme purification, characterisation and N-terminal sequence. FEMS Microbiol. Lett. 134 (1995) 85-90. [PMID: 8593959]
7. Steen, I.H., Lien, T. and Birkeland, N.-K. Biochemical and phylogenetic characterization of isocitrate dehydrogenase from a hyperthermophilic archaeon, Archaeoglobus fulgidus. Arch. Microbiol. 168 (1997) 412-420. [PMID: 9325430]
8. Koh, H.J., Lee, S.M., Son, B.G., Lee, S.H., Ryoo, Z.Y., Chang, K.T., Park, J.W., Park, D.C., Song, B.J., Veech, R.L., Song, H. and Huh, T.L. Cytosolic NADP+-dependent isocitrate dehydrogenase plays a key role in lipid metabolism. J. Biol. Chem. 279 (2004) 39968-39974. [PMID: 15254034]
9. Ceccarelli, C., Grodsky, N.B., Ariyaratne, N., Colman, R.F. and Bahnson, B.J. Crystal structure of porcine mitochondrial NADP+-dependent isocitrate dehydrogenase complexed with Mn2+ and isocitrate. Insights into the enzyme mechanism. J. Biol. Chem. 277 (2002) 43454-43462. [PMID: 12207025]
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. J. Biol. Chem. 236 (1961) 2571-2577.
Accepted name: phosphogluconate dehydrogenase (NADP+-dependent, decarboxylating)
Reaction: 6-phospho-D-gluconate + NADP+ = D-ribulose 5-phosphate + CO2 + NADPH + H+
For diagram of reaction 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. 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. Biochem. J. 50 (1951) 81-95. [PMID: 14904376]
2. Pontremoli, S., de Flora, A., Grazi, E., Mangiarotti, G., Bonsignore, A. and Horecker, B.L. Purification and properties of β-L-hydroxy acid dehydrogenase. II. Isolation of β-keto-L-gluconic acid, an intermediate in L-xylulose biosynthesis. J. Biol. Chem. 236 (1961) 2975-2980. [PMID: 14487824]
3. Scott, D.B.M. and Cohen, S.S. The oxidative pathway of carbohydrate metabolism in Escherichia coli. 1. The isolation and properties of glucose 6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase. Biochem. J. 55 (1953) 23-33. [PMID: 13093611]
4. Scott, D.B.M. and Cohen, S.S. The oxidative pathway of carbohydrate metabolism in Escherichia coli. 5. Isolation and identification of ribulose phosphate produced from 6-phosphogluconate by the dehydrogenase of E. coli. Biochem. J. 65 (1957) 686-689. [PMID: 13426085]
5. Bridges, R.B., Palumbo, M.P. and Wittenberger, C.L. Purification and properties of an NADP-specific 6-phosphogluconate dehydrogenase from Streptococcus faecalis. J. Biol. Chem. 250 (1975) 6093-6100. [PMID: 238996]
6. Yoon, H., Anderson, C.D. and Anderson, B.M. Kinetic studies of Haemophilus influenzae 6-phosphogluconate dehydrogenase. Biochim. Biophys. Acta 994 (1989) 75-80. [PMID: 2783298]
7. Zamboni, N., Fischer, E., Laudert, D., Aymerich, S., Hohmann, H.P. and Sauer, U. The Bacillus subtilis yqjI gene encodes the NADP+-dependent 6-P-gluconate dehydrogenase in the pentose phosphate pathway. J. Bacteriol. 186 (2004) 4528-4534. [PMID: 15231785]
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. Acta Biochim. Pol. 11 (1964) 269-277.
2. Smiley, J.D. and Ashwell, G. Purification and properties of β-L-hydroxy acid dehydrogenase. II. Isolation of β-keto-L-gluconic acid, an intermediate in L-xylulose biosynthesis. J. Biol. Chem. 236 (1961) 357-364.
Accepted name: L-arabinose 1-dehydrogenase
Reaction: L-arabinose + NAD+ = L-arabinono-1,4-lactone + NADH + H+
For diagram of reaction click here.
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.
Accepted name: glucose 1-dehydrogenase [NAD(P)+]
Reaction: D-glucose + NAD(P)+ = D-glucono-1,5-lactone + NAD(P)H + H+
Other name(s): D-glucose dehydrogenase (NAD(P)+); hexose phosphate dehydrogenase; β-D-glucose:NAD(P)+ 1-oxidoreductase; glucose 1-dehydrogenase
Systematic name: D-glucose:NAD(P)+ 1-oxidoreductase
Comments: This enzyme has similar activity with either NAD+ or NADP+. cf. EC 1.1.1.118, glucose 1-dehydrogenase (NAD+) and EC 1.1.1.119, glucose 1-dehydrogenase (NADP+).
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. Z. Klin. Chem. Klin. Biochem. 13 (1975) 101-107. [PMID: 810982]
2. Brink, N.G. Beef liver glucose dehydrogenase. 1. Purification and properties. Acta Chem. Scand. 7 (1953) 1081-1089.
3. Pauly, H.E. and Pfleiderer, G. D-Glucose dehydrogenase from Bacillus megaterium M 1286: purification, properties and structure. Hoppe-Seylers Z. Physiol. Chem. 356 (1975) 1613-1623. [PMID: 2530]
4. Strecker, H.J. and Korkes, S. Glucose dehydrogenase. J. Biol. Chem. 196 (1952) 769-784. [PMID: 12981017]
5. Thompson, R.E. and Carper, W.R. Glucose dehydrogenase from pig liver. I. Isolation and purification. Biochim. Biophys. Acta 198 (1970) 397-406. [PMID: 4392298]
6. Fujita, Y., Ramaley, R. and Freese, E. Location and properties of glucose dehydrogenase in sporulating cells and spores of Bacillus subtilis. J. Bacteriol. 132 (1977) 282-293. [PMID: 21162]
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. [PMID: 14251301]
Accepted name: glucose-6-phosphate dehydrogenase (NADP+)
Reaction: D-glucose 6-phosphate + NADP+ = 6-phospho-D-glucono-1,5-lactone + NADPH + H+
For diagram of reaction 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. EC 1.1.1.363, glucose-6-phosphate dehydrogenase [NAD(P)+] and 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. Biochim. Biophys. Acta 191 (1969) 509-516. [PMID: 5363983]
2. Glaser, L. and Brown, D.H. Purification and properties of D-glucose-6-phosphate dehydrogenase. J. Biol. Chem. 216 (1955) 67-79. [PMID: 13252007]
3. Julian, G.R., Wolfe, R.G. and Reithel, F.J. The enzymes of mammary gland. II. The preparation of glucose 6-phosphate dehydrogenase. J. Biol. Chem. 236 (1961) 754-758. [PMID: 13790996]
4. Noltmann, E.A., Gubler, C.J. and Kuby, S.A. Glucose 6-phosphate dehydrogenase (Zwischenferment). I. Isolation of the crystalline enzyme from yeast. J. Biol. Chem. 236 (1961) 1225-1230. [PMID: 13729473]
5. Miclet, E., Stoven, V., Michels, P.A., Opperdoes, F.R., Lallemand, J.-Y. and Duffieux, F. NMR spectroscopic analysis of the first two steps of the pentose-phosphate pathway elucidates the role of 6-phosphogluconolactonase. J. Biol. Chem. 276 (2001) 34840-34846. [PMID: 11457850]
6. Olavarria, K., Valdes, D. and Cabrera, R. The cofactor preference of glucose-6-phosphate dehydrogenase from Escherichia coli - modeling the physiological production of reduced cofactors. FEBS J. 279 (2012) 2296-2309. [PMID: 22519976]
7. Hansen, T., Schlichting, B. and Schonheit, P. Glucose-6-phosphate dehydrogenase from the hyperthermophilic bacterium Thermotoga maritima: expression of the g6pd gene and characterization of an extremely thermophilic enzyme. FEMS Microbiol. Lett. 216 (2002) 249-253. [PMID: 12435510]
8. Ibraheem, O., Adewale, I.O. and Afolayan, A. Purification and properties of glucose 6-phosphate dehydrogenase from Aspergillus aculeatus. J. Biochem. Mol. Biol. 38 (2005) 584-590. [PMID: 16202239]
9. Iyer, R.B., Wang, J. and Bachas, L.G. Cloning, expression, and characterization of the gsdA gene encoding thermophilic glucose-6-phosphate dehydrogenase from Aquifex aeolicus. Extremophiles 6 (2002) 283-289. [PMID: 12215813]
10. Cho, S.W. and Joshi, J.G. Characterization of glucose-6-phosphate dehydrogenase isozymes from human and pig brain. Neuroscience 38 (1990) 819-828. [PMID: 2270145]
Accepted name: 3α-hydroxysteroid 3-dehydrogenase (Si-specific)
Reaction: a 3α-hydroxysteroid + NAD(P)+ = a 3-oxosteroid + NAD(P)H + H+
Other name(s): hydroxyprostaglandin dehydrogenase; 3α-hydroxysteroid oxidoreductase; sterognost 3α; 3α-hydroxysteroid dehydrogenase (B-specific); 3α-hydroxysteroid 3-dehydrogenase (B-specific); 3α-hydroxysteroid:NAD(P)+ 3-oxidoreductase (B-specific)
Systematic name: 3α-hydroxysteroid:NAD(P)+ 3-oxidoreductase (Si-specific)
Comments: The enzyme acts on androsterone and other 3α-hydroxysteroids and on 9-, 11- and 15-hydroxyprostaglandin. Si-specific with respect to NAD+ or NADP+. cf. EC 1.1.1.213, 3α-hydroxysteroid 3-dehydrogenase (Re-specific).
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. J. Biol. Chem. 224 (1957) 811-818. [PMID: 13405910]
3. Marcus, P.I. and Talalay, P. Induction and purification of α- and β-hydroxysteroid dehydrogenases. J. Biol. Chem. 218 (1956) 661-674. [PMID: 13295221]
4. Penning, T.M. and Sharp, R.B. Prostaglandin dehydrogenase activity of purified rat liver 3α-hydroxysteroid dehydrogenase. Biochem. Biophys. Res. Commun. 148 (1987) 646-652. [PMID: 3479982]