EC 1.1.1.1 to EC 1.1.1.50See separate file for EC 1.1.1.151 to EC 1.1.1.200
EC 1.1.1.51 to EC 1.1.1.100
See the following files for:
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: acylglycerone-phosphate reductase
Reaction: 1-palmitoylglycerol 3-phosphate + NADP+ = palmitoylglycerone phosphate + NADPH + H+
Other name(s): palmitoyldihydroxyacetone-phosphate reductase; palmitoyl dihydroxyacetone phosphate reductase; palmitoyl-dihydroxyacetone-phosphate reductase; acyldihydroxyacetone phosphate reductase; palmitoyl dihydroxyacetone phosphate reductase
Systematic name: 1-palmitoylglycerol-3-phosphate:NADP+ oxidoreductase
Comments: Also acts on alkylglycerone 3-phosphate and alkylglycerol 3-phosphate.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37250-35-4
References:
1. LaBelle, E.F., Jr. and Hajira, A.K. Enzymatic reduction of alkyl and acyl derivatives of dihydroxyacetone phosphate by reduced pyridine nucleotides. J. Biol. Chem. 247 (1972) 5825-5834. [PMID: 4403490]
Accepted name: 3-dehydrosphinganine reductase
Reaction: sphinganine + NADP+ = 3-dehydrosphinganine + NADPH + H+
Other name(s): D-3-dehydrosphinganine reductase; D-3-oxosphinganine reductase; DSR; 3-oxosphinganine reductase; 3-oxosphinganine:NADPH oxidoreductase; D-3-oxosphinganine:B-NADPH oxidoreductase
Systematic name: D-erythro-dihydrosphingosine:NADP+ 3-oxidoreductase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 37250-36-5
References:
1. Stoffel, W., Le Kim, D. and Sticht, G. Biosynthesis of dihydrosphingosine in vitro. Hoppe-Seyler's Z. Physiol. Chem. 349 (1968) 664-670. [PMID: 4386961]
2. Stoffel, W., Le Kim, D. and Sticht, G. Metabolism of sphingosine bases. 8. Distribution, isolation and properties of D-3-oxosphinganine reductase. Stereospecificity of the NADPH-dependent reaction of 3-oxodihydrospingosine (2-amino-1-hydroxyoctadecane-3-one). Hoppe-Seyler's Z. Physiol. Chem. 349 (1968) 1637-1644. [PMID: 4387676]
Accepted name: L-threonine 3-dehydrogenase
Reaction: L-threonine + NAD+ = L-2-amino-3-oxobutanoate + NADH + H+
Other name(s): L-threonine dehydrogenase; threonine 3-dehydrogenase; threonine dehydrogenase; THD
Systematic name: L-threonine:NAD+ oxidoreductase
Comments: This enzyme acts in concert with EC 2.3.1.29, glycine C-acetyltransferase, in the degradation of threonine to glycine. This threonine-degradation pathway is common to prokaryotic and eukaryotic cells and the two enzymes involved form a complex [2]. In aqueous solution, the product L-2-amino-3-oxobutanoate can spontaneously decarboxylate to form aminoacetone.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9067-99-6
References:
1. Green, M.L. and Elliott, W.H. The enzymic formation of aminoacetone from threonine and its further metabolism. Biochem. J. 92 (1964) 537-549. [PMID: 4284408]
2. Hartshorne, D. and Greenberg, D.M. Studies on liver threonine dehydrogenase. Arch. Biochem. Biophys. 105 (1964) 173-178. [PMID: 14165492]
3. Newman, E.B., Kapoor, V. and Potter, R. Role of L-threonine dehydrogenase in the catabolism of threonine and synthesis of glycine by Escherichia coli. J. Bacteriol. 126 (1976) 1245-. [PMID: 7548]
4. Epperly, B.R. and Dekker, E.E. L-Threonine dehydrogenase from Escherichia coli. Identification of an active site cysteine residue and metal ion studies. J. Biol. Chem. 266 (1991) 6086-6092. [PMID: 2007567]
Accepted name: 4-oxoproline reductase
Reaction: cis-4-hydroxy-L-proline + NAD+ = 4-oxo-L-proline + NADH + H+
Other name(s): cis-hydroxy-L-proline oxidase
Systematic name: cis-4-hydroxy-L-proline:NAD+ oxidoreductase (4-oxo-L-proline forming)
Comments: The enzyme, isolated from animals, is specific for 4-oxo-L-proline and cis-4-hydroxy-L-proline. It has no activity with trans-4-hydroxy-L-proline.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37250-37-6
References:
1. Smith, T.E. and Mitoma, C. Partial purification and some properties of 4-ketoproline reductase. J. Biol. Chem. 237 (1962) 1177-1180. [PMID: 13914427]
2. Kwiatkowski, S., Bozko, M., Zarod, M., Witecka, A., Kocdemir, K., Jagielski, A.K. and Drozak, J. Recharacterization of the mammalian cytosolic type 2 (R)-β-hydroxybutyrate dehydrogenase (BDH2) as 4-oxo-L-proline reductase (EC 1.1.1.104). J. Biol. Chem. 298 (2022) 101708. [PMID: 35150746]
Accepted name: all-trans-retinol dehydrogenase (NAD+)
Reaction: all-trans-retinol-[cellular-retinol-binding-protein] + NAD+ = all-trans-retinal-[cellular-retinol-binding-protein] + NADH + H+
For diagram of reaction click here
Other name(s): retinol (vitamin A1) dehydrogenase; MDR; microsomal retinol dehydrogenase; retinol dehydrogenase (misleading); retinal reductase (ambiguous); retinene reductase; epidermal retinol dehydrogenase 2; SDR16C5 (gene name); RDH16 (gene name)
Systematic name: all-trans retinol:NAD+ oxidoreductase
Comments: The enzyme recognizes all-trans-retinol and all-trans-retinal as substrates and exhibits a strong preference for NAD+/NADH as cofactors. Recognizes the substrate both in free form and when bound to cellular-retinol-binding-protein (CRBP1), but has higher affinity for the bound form [2]. No activity with 11-cis-retinol or 11-cis-retinal (c.f. EC 1.1.1.315, 11-cis retinol dehydrogenase). Also active with 3α-hydroxysteroids [2].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9033-53-8
References:
1. Koen, A.L. and Shaw, C.R. Retinol and alcohol dehydrogenases in retina and liver. Biochim. Biophys. Acta 128 (1966) 48-54. [PMID: 5972368]
2. Gough, W.H., VanOoteghem, S., Sint, T. and Kedishvili, N.Y. cDNA cloning and characterization of a new human microsomal NAD+-dependent dehydrogenase that oxidizes all-trans-retinol and 3α-hydroxysteroids. J. Biol. Chem. 273 (1998) 19778-19785. [PMID: 9677409]
3. Matsuzaka, Y., Okamoto, K., Tsuji, H., Mabuchi, T., Ozawa, A., Tamiya, G. and Inoko, H. Identification of the hRDH-E2 gene, a novel member of the SDR family, and its increased expression in psoriatic lesion. Biochem. Biophys. Res. Commun. 297 (2002) 1171-1180. [PMID: 12372410]
4. Lee, S.A., Belyaeva, O.V. and Kedishvili, N.Y. Biochemical characterization of human epidermal retinol dehydrogenase 2. Chem. Biol. Interact. 178 (2009) 182-187. [PMID: 18926804]
Accepted name: pantoate 4-dehydrogenase
Reaction: (R)-pantoate + NAD+ = (R)-4-dehydropantoate + NADH + H+
For diagram of reaction click here.
Glossary:
pantoate = 2,4-dihydroxy-3,3-dimethylbutanoate
Other name(s): pantoate dehydrogenase; pantothenase; D-pantoate:NAD+ 4-oxidoreductase
Systematic name: (R)-pantoate:NAD+ 4-oxidoreductase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37250-38-7
References:
1. Goodhue, C.T. and Snell, E.E. The bacterial degradation of pantothenic acid. 3. Enzymatic formation of aldopantoic acid. Biochemistry 5 (1966) 403-408. [PMID: 4287370]
Accepted name: pyridoxal 4-dehydrogenase
Reaction: pyridoxal + NAD+ = 4-pyridoxolactone + NADH + H+
For diagram of reaction click here.
Other name(s): pyridoxal dehydrogenase
Systematic name: pyridoxal:NAD+ 4-oxidoreductase
Comments: The enzyme acts on the hemiacetal form of the substrate.
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 37250-39-8
References:
1. Burg, R.W. and Snell, E.E. The bacterial oxidation of vitamin B6. VI. Pyridoxal dehydrogenase and 4-pyridoxolactonase. J. Biol. Chem. 244 (1969) 2585-2589. [PMID: 4306030]
Accepted name: carnitine 3-dehydrogenase
Reaction: carnitine + NAD+ = 3-dehydrocarnitine + NADH + H+
Systematic name: carnitine:NAD+ 3-oxidoreductase
Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, CAS registry number: 9045-45-8
References:
1. Aurich, H., Kleber, H.-P., Sorger, H. and Tauchert, H. Reinigung und Eigenschaften der Carnitindehydrogenase aus Pseudomonas aeruginosa. Eur. J. Biochem. 6 (1968) 196-201. [PMID: 4302217]
2. Schöpp, W., Sorger, H., Kleber, H.-P. and Aurich, H. Kinetische Untersuchungen zum Reaktionmechanisms der Carnitindehydrogenase aus Pseudomonas aeruginosa. Eur. J. Biochem. 10 (1969) 56-60. [PMID: 4310279]
[EC 1.1.1.109 Transferred entry: now EC 1.3.1.28 2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase (EC 1.1.1.109 created 1972, deleted 1976)]
Accepted name: aromatic 2-oxoacid reductase
Reaction: (1) (R)-3-(phenyl)lactate + NAD+ = 3-phenyl-2-oxopropanoate + NADH + H+
(2) (R)-3-(4-hydroxyphenyl)lactate + NAD+ = 3-(4-hydroxyphenyl)pyruvate + NADH + H+
(3) (R)-(indol-3-yl)lactate + NAD+ = (indol-3-yl)pyruvate + NADH + H+
Glossary: aromatic 2-oxoacid reductase
Other name(s): (R)-aromatic lactate dehydrogenase; (R)-4-hydroxyphenyllactate dehydrogenase; indolelactate:NAD+ oxidoreductase; indolelactate dehydrogenase; fldH (gene name); (indol-3-yl)lactate:NAD+ oxidoreductase
Systematic name: aromatic 2-oxoacid:NAD+ oxidoreductase
Comments: The enzymes from anaerobic bacteria such as Clostridium sporogenes participate in the fermentation pathways of L-phenylalanine, L-tyrosine and L-tryptophan. The enzyme from the yeast Candida maltosa has similar activity, but, unlike the bacterial enzyme, requires Mn2+ and can also use NADPH with lower activity.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, CAS registry number: 37250-41-2
References:
1. Jean, M. and DeMoss, R.D. Indolelactate dehydrogenase from Clostridium sporogenes. Can. J. Microbiol. 14 (1968) 429-435. [PMID: 4384683]
2. Giesel, H. and Simon, H. On the occurrence of enoate reductase and 2-oxo-carboxylate reductase in clostridia and some observations on the amino acid fermentation by Peptostreptococcus anaerobius. Arch. Microbiol. 135 (1983) 51-57. [PMID: 6354130]
3. Bode, R., Lippoldt, A. and Birnbaum, D. Purification and properties of D-aromatic lactate dehydrogenase an enzyme involved in the catabolism of the aromatic amino acids of Candida maltosa. Biochem. Physiol. Pflanzen 181 (1986) 189-198.
4. Dickert, S., Pierik, A.J., Linder, D. and Buckel, W. The involvement of coenzyme A esters in the dehydration of (R)-phenyllactate to (E)-cinnamate by Clostridium sporogenes. Eur. J. Biochem. 267 (2000) 3874-3884. [PMID: 10849007]
5. Dodd, D., Spitzer, M.H., Van Treuren, W., Merrill, B.D., Hryckowian, A.J., Higginbottom, S.K., Le, A., Cowan, T.M., Nolan, G.P., Fischbach, M.A. and Sonnenburg, J.L. A gut bacterial pathway metabolizes aromatic amino acids into nine circulating metabolites. Nature 551 (2017) 648-652. [PMID: 29168502]
Accepted name: indanol dehydrogenase
Reaction: indan-1-ol + NAD(P)+ = indanone + NAD(P)H + H+
Systematic name: indan-1-ol:NAD(P)+ 1-oxidoreductase
Comments: 3(20)α-Hydroxysteroids are also oxidized, more slowly.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 37250-43-4
References:
1. Billings, R.E., Sullivan, H.R. and McMahon, R.E. The dehydrogenation of 1-indanol by a soluble oxidoreductase from bovine liver. J. Biol. Chem. 246 (1971) 3512-3517. [PMID: 4397102]
2. Hara, A., Nakagawa, M., Taniguchi, H. and Sawada, H. 3(20)α-Hydroxysteroid dehydrogenase activity of monkey liver indanol dehydrogenase. J. Biochem. (Tokyo) 106 (1989) 900-903. [PMID: 2559080]
Accepted name: L-xylose 1-dehydrogenase
Reaction: L-xylose + NADP+ = L-xylono-1,4-lactone + NADPH + H+
Other name(s): L-xylose dehydrogenase; NADPH-xylose reductase
Systematic name: L-xylose:NADP+ 1-oxidoreductase
Comments: Also oxidizes D-arabinose and D-lyxose.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37250-44-5
References:
1. Uehara, K. and Takeda, M. L-Xylose dehydrogenase in bakers' yeast. J. Biochem. (Tokyo) 52 (1962) 461-463.
Accepted name: apiose 1-reductase
Reaction: D-apiitol + NAD+ = D-apiose + NADH + H+
Other name(s): D-apiose reductase; D-apiitol reductase
Systematic name: D-apiitol:NAD+ 1-oxidoreductase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37250-45-6
References:
1. Hanna, R., Picken, M. and Mendicino, J. Purification of a specific D-apiitol dehydrogenase from a Micrococcus isolated from the surface of germinating parsley seeds. Biochim. Biophys. Acta 315 (1973) 259-271.
2. Neal, D.L. and Kindel, P.K. D-Apiose reductase from Aerobacter aerogenes. J. Bacteriol. 101 (1970) 910-915. [PMID: 4314545]
Accepted name: ribose 1-dehydrogenase (NADP+)
Reaction: D-ribose + NADP+ + H2O = D-ribonate + NADPH + H+
Other name(s): D-ribose dehydrogenase (NADP+); NADP-pentose-dehydrogenase; ribose 1-dehydrogenase (NADP)
Systematic name: D-ribose:NADP+ 1-oxidoreductase
Comments: Also acts, more slowly, on D-xylose and other pentoses.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37250-46-7
References:
1. Scher, B.M. and Horecker, B.L. Pentose metabolism in Candida. 3. The triphosphopyridine nucleotide-specific polyol dehydrogenase of Candida utilis. Arch. Biochem. Biophys. 116 (1966) 117-128. [PMID: 4381350]
2. Schiwara, H.W., Domschke, W. and Domagk, G.F. Über die Zucker-Dehydrogenase in der Säugetierleber. I. Differenzierung verschiedener Zucker-Dehydrogenasen in der Schweineleber durch Disk-Elektrophorese und Ionenaustausch-chromatographie. Hoppe-Seyler's Z. Physiol. Chem. 349 (1968) 1575-1581. [PMID: 4393642]
Accepted name: D-arabinose 1-dehydrogenase (NAD+)
Reaction: D-arabinose + NAD+ = D-arabinono-1,4-lactone + NADH + H+
For diagram of reaction click here.
Other name(s): NAD-pentose-dehydrogenase; arabinose(fucose)dehydrogenase
Systematic name: D-arabinose:NAD+ 1-oxidoreductase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37250-47-8
References:
1. Palleroni, N.J. and Doudoroff, M. Metabolism of carbohydrates by Pseudomonas saccharophilla. III. Oxidation of D-arabinose. J. Bacteriol. 74 (1957) 180-185.
2. Schiwara, H.W., Domschke, W. and Domagk, G.F. Über die Zucker-Dehydrogenase in der Säugetierleber. I. Differenzierung verschiedener Zucker-Dehydrogenasen in der Schweineleber durch Disk-Elektrophorese und Ionenaustausch-chromatographie. Hoppe-Seyler's Z. Physiol. Chem. 349 (1968) 1575-1581. [German] [PMID: 4393642]
Accepted name: D-arabinose 1-dehydrogenase [NAD(P)+]
Reaction: D-arabinose + NAD(P)+ = D-arabinono-1,4-lactone + NAD(P)H + H+
For diagram of reaction click here.
Other name(s): D-arabinose 1-dehydrogenase [NAD(P)]
Systematic name: D-arabinose:NAD(P)+ 1-oxidoreductase
Comments: Also acts on L-galactose, 6-deoxy- and 3,6-dideoxy-L-galactose.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 37250-48-9
References:
1. Cline, A.L. and Hu, A.S.L. The isolation of three sugar dehydrogenases from a psuedomonad. J. Biol. Chem. 240 (1965) 4488-4492. [PMID: 5845847]
2. Cline, A.L. and Hu, A.S.L. Enzymatic characterization and comparison of three sugar dehydrogenases from a pseudomonad. J. Biol. Chem. 240 (1965) 4493-4497. [PMID: 5845848]
3. Cline, A.L. and Hu, A.S.L. Some physical properties of three sugar dehydrogenases from a pseudomonad. J. Biol. Chem. 240 (1965) 4498-4502. [PMID: 5845849]
Accepted name: glucose 1-dehydrogenase (NAD+)
Reaction: D-glucose + NAD+ = D-glucono-1,5-lactone + NADH + H+
Other name(s): D-glucose:NAD oxidoreductase; D-aldohexose dehydrogenase; glucose 1-dehydrogenase (NAD)
Systematic name: D-glucose:NAD+ 1-oxidoreductase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37250-49-0
References:
1. Hu, A.S.L. and Cline, A.L. The regulation of some sugar dehydrogenases in a pseuudomonad. Biochim. Biophys. Acta 93 (1964) 237-245.
Accepted name: glucose 1-dehydrogenase (NADP+)
Reaction: D-glucose + NADP+ = D-glucono-1,5-lactone + NADPH + H+
Other name(s): nicotinamide adenine dinucleotide phosphate-linked aldohexose dehydrogenase; NADP-linked aldohexose dehydrogenase; NADP-dependent glucose dehydrogenase; glucose 1-dehydrogenase (NADP)
Systematic name: D-glucose:NADP+ 1-oxidoreductase
Comments: Also oxidizes D-mannose, 2-deoxy-D-glucose and 2-amino-2-deoxy-D-mannose.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, CAS registry number: 37250-50-3
References:
1. Adachi, O. and Ameyama, M. D-Glucose dehydrogenase from Gluconobacter suboxydans. Methods Enzymol. 89 (1982) 159-163.
2. Avigad, G., Alroy, Y. and Englard, S. Purification and properties of a nicotinamide adenine dinucleotide phosphate-linked aldohexose dehydrogenase from Gluconobacter cerinus. J. Biol. Chem. 243 (1968) 1936-1941. [PMID: 4384672]
Accepted name: galactose 1-dehydrogenase (NADP+)
Reaction: D-galactose + NADP+ = D-galactono-1,5-lactone + NADPH + H+
Other name(s): D-galactose dehydrogenase (NADP+); galactose 1-dehydrogenase (NADP)
Systematic name: D-galactose:NADP+ 1-oxidoreductase
Comments: Also acts on L-arabinose, 6-deoxy- and 2-deoxy-D-galactose.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 37250-51-4
References:
1. Cline, A.L. and Hu, A.S.L. The isolation of three sugar dehydrogenases from a psuedomonad. J. Biol. Chem. 240 (1965) 4488-4492. [PMID: 5845847]
2. Cline, A.L. and Hu, A.S.L. Enzymatic characterization and comparison of three sugar dehydrogenases from a pseudomonad. J. Biol. Chem. 240 (1965) 4493-4497. [PMID: 5845848]
3. Cline, A.L. and Hu, A.S.L. Some physical properties of three sugar dehydrogenases from a pseudomonad. J. Biol. Chem. 240 (1965) 4498-4502. [PMID: 5845849]
4. Schiwara, H.W. and Domagk, G.F. Über den Abbau der Desoxyzucker durch Bakterienenzyme. V. Anreicherung und Charakterisierung einer NADP-abhängigen Abequosedehydrogenase aus Pseudomonas putida. Hoppe-Seyler's Z. Physiol. Chem. 349 (1968) 1321-1329. [PMID: 4387016]
Accepted name: aldose 1-dehydrogenase (NAD+)
Reaction: D-aldose + NAD+ = D-aldonolactone + NADH + H+
Other name(s): aldose dehydrogenase; D-aldohexose dehydrogenase; aldose 1-dehydrogenase
Systematic name: D-aldose:NAD+ 1-oxidoreductase
Comments: Acts on D-glucose, 2-deoxy- and 6-deoxy-D-glucose, D-galactose, 6-deoxy-D-galactose, 2-deoxy-L-arabinose and D-xylose.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9076-61-3
References:
1. Cline, A.L. and Hu, A.S.L. The isolation of three sugar dehydrogenases from a pseudomonad. J. Biol. Chem. 240 (1965) 4488-4492. [PMID: 5845847]
2. Cline, A.L. and Hu, A.S.L. Enzymatic characterization and comparison of three sugar dehydrogenases from a pseudomonad. J. Biol. Chem. 240 (1965) 4493-4497. [PMID: 5845848]
3. Cline, A.L. and Hu, A.S.L. Some physical properties of three sugar dehydrogenases from a pseudomonad. J. Biol. Chem. 240 (1965) 4498-4502. [PMID: 5845849]
Accepted name: D-threo-aldose 1-dehydrogenase
Reaction: a D-threo-aldose + NAD+ = a D-threo-aldono-1,5-lactone + NADH + H+
For diagram of reaction click here
Other name(s): L-fucose dehydrogenase; (2S,3R)-aldose dehydrogenase; dehydrogenase, L-fucose; L-fucose (D-arabinose) dehydrogenase
Systematic name: D-threo-aldose:NAD+ 1-oxidoreductase
Comments: Acts on L-fucose, D-arabinose and L-xylose; the animal enzyme was also shown to act on L-arabinose, and the enzyme from Pseudomonas caryophylli on L-glucose.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9082-70-6
References:
1. Sasajima, K.-I. and Sinskey, A.J. Oxidation of L-glucose by a Pseudomonad. Biochim. Biophys. Acta 571 (1979) 120-126. [PMID: 40609]
2. Schachter, H., Sarney, J., McGuire, E.J. and Roseman, S. Isolation of diphosphopyridine nucleotide-dependent L-fucose dehydrogenase from pork liver. J. Biol. Chem. 244 (1969) 4785-4792. [PMID: 4309152]
Accepted name: sorbose 5-dehydrogenase (NADP+)
Reaction: L-sorbose + NADP+ = 5-dehydro-D-fructose + NADPH + H+
Other name(s): 5-ketofructose reductase; 5-keto-D-fructose reductase; sorbose (nicotinamide adenine dinucleotide phosphate) dehydrogenase; reduced nicotinamide adenine dinucleotide phosphate-linked reductase; sorbose 5-dehydrogenase (NADP)
Systematic name: L-sorbose:NADP+ 5-oxidoreductase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37250-52-5
References:
1. Englard, S., Kaysen, G. and Avigad, G. 5-keto-D-Fructose. VI. A specific reduced nicotinamide adenine dinucleotide phosphate-linked reductase from yeast. J. Biol. Chem. 245 (1970) 1311-1318. [PMID: 4392628]
Accepted name: fructose 5-dehydrogenase (NADP+)
Reaction: D-fructose + NADP+ = 5-dehydro-D-fructose + NADPH + H+
Other name(s): 5-ketofructose reductase (NADP); 5-keto-D-fructose reductase (NADP+); fructose 5-(nicotinamide adenine dinucleotide phosphate) dehydrogenase; D-(–)fructose:(NADP+) 5-oxidoreductase; fructose 5-dehydrogenase (NADP)
Systematic name: D-fructose:NADP+ 5-oxidoreductase
Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, CAS registry number: 37250-53-6
References:
1. Ameyama, M., Matsushita, K., Shinagawa, E. and Adachi, O. 5-keto-D-Fructose reductase of Gluconobacter industrius – Purification, crystallization and properties. Agric. Biol. Chem. 45 (1981) 863-869.
2. Avigad, G., Englard, S. and Pifco, S. 5-keto-D-Fructose. IV. A specific reduced nicotinamide adenine dinucleotide phosphate-linked reductase from Gluconobacter cerinus. J. Biol. Chem. 241 (1966) 373-378. [PMID: 4379259]
Accepted name: 2-deoxy-D-gluconate 3-dehydrogenase
Reaction: 2-deoxy-D-gluconate + NAD+ = 3-dehydro-2-deoxy-D-gluconate + NADH + H+
Other name(s): 2-deoxygluconate dehydrogenase
Systematic name: 2-deoxy-D-gluconate:NAD+ 3-oxidoreductase
Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 37250-54-7
References:
1. Eichhorn, M.M. and Cynkin, M.A. Microbial metabolism of 2-deoxyglucose; 2-deoxyglucose acid dehydrogenase. Biochemistry 4 (1965) 159-165.
Accepted name: 2-dehydro-3-deoxy-D-gluconate 6-dehydrogenase
Reaction: 2-dehydro-3-deoxy-D-gluconate + NADP+ = (4S,5S)-4,5-dihydroxy-2,6-dioxohexanoate + NADPH + H+
Other name(s): 2-keto-3-deoxy-D-gluconate dehydrogenase (ambiguous); 2-keto-3-deoxygluconate dehydrogenase (ambiguous)
Systematic name: 2-dehydro-3-deoxy-D-gluconate:NADP+ 6-oxidoreductase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 37250-55-8
References:
1. Preiss, J. and Ashwell, G. Alginic acid metabolism in bacteria. II. The enzymatic reduction of 4-deoxy-L-erythro-5-hexoseulose uronic acid to 2-keto-3-deoxy-D-gluconic acid. J. Biol. Chem. 237 (1962) 317-321.
Accepted name: 2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase
Reaction: 2-dehydro-3-deoxy-D-gluconate + NAD+ = (4S)-4,6-dihydroxy-2,5-dioxohexanoate + NADH + H+
Other name(s): 2-keto-3-deoxygluconate 5-dehydrogenase; 2-keto-3-deoxy-D-gluconate dehydrogenase (ambiguous); 2-keto-3-deoxygluconate (nicotinamide adenine dinucleotide (phosphate)) dehydrogenase; 2-keto-3-deoxy-D-gluconate (3-deoxy-D-glycero-2,5-hexodiulosonic acid) dehydrogenase (ambiguous)
Systematic name: 2-dehydro-3-deoxy-D-gluconate:NAD+ 5-oxidoreductase
Comments: The enzyme from Pseudomonas acts equally well on NAD+ or NADP+, while that from Erwinia chrysanthemi and Escherichia coli is more specific for NAD+.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 37250-56-9
References:
1. Condemine, G., Hugouvieux-Cotte-Pattat, N. and Robert-Baudouy, J. An enzyme in the pectolytic pathway of Erwinia chrysanthemi: 3-keto-3-deoxygluconate oxidoreductase. J. Gen. Microbiol. 130 (1984) 2839-2844.
2. Preiss, J. and Ashwell, G. Polygalacturonic acid metabolism in bacteria. II. Formation and metabolism of 3-deoxy-D-glycero-2,5-hexodiulosonic acid. J. Biol. Chem. 238 (1963) 1577-1583.
[EC 1.1.1.128 Deleted entry: L-idonate 2-dehydrogenase. The reaction described is covered by EC 1.1.1.264. (EC 1.1.1.128 created 1972, modified 1976, deleted 2012)]
Accepted name: L-threonate 3-dehydrogenase
Reaction: L-threonate + NAD+ = 3-dehydro-L-erythronate + NADH + H+
Other name(s): threonate dehydrogenase; L-threonic acid dehydrogenase
Systematic name: L-threonate:NAD+ 3-oxidoreductase
Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, CAS registry number: 37250-59-2
References:
1. Aspen, A.J. and Jakoby, W.B. L-Threonic acid dehydrogenase: purification and properties. J. Biol. Chem. 239 (1964) 710-713.
Accepted name: 3-dehydro-L-gulonate 2-dehydrogenase
Reaction: 3-dehydro-L-gulonate + NAD(P)+ = (4R,5S)-4,5,6-trihydroxy-2,3-dioxohexanoate + NAD(P)H + H+
Other name(s): 3-keto-L-gulonate dehydrogenase; 3-ketogulonate dehydrogenase; 3-keto-L-gulonate dehydrogenase; 3-ketogulonate dehydrogenase
Systematic name: 3-dehydro-L-gulonate:NAD(P)+ 2-oxidoreductase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 37250-61-6
References:
1. Volk, W.A. and Larsen, J.L. β-Keto-L-gulonic acid as an intermediate in the bacterial metabolism of ascorbic acid. J. Biol. Chem. 237 (1962) 2454-2457.
Accepted name: mannuronate reductase
Reaction: D-mannonate + NAD(P)+ = D-mannuronate + NAD(P)H + H+
Other name(s): mannonate dehydrogenase; mannonate (nicotinamide adenine dinucleotide (phosphate))dehydrogenase; mannonate dehydrogenase; mannuronate reductase; mannonate dehydrogenase (NAD(P)+); D-mannonate:nicotinamide adenine dinucleotide (phosphate oxidoreductase (D-mannuronate-forming))
Systematic name: D-mannonate:NAD(P)+ 6-oxidoreductase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37250-62-7
References:
1. Farmer, J.J., III and Eagon, R.G. Aldohexuronic acid catabolism by a soil Aeromonas. J. Bacteriol. 97 (1969) 97-106. [PMID: 4388117]
Accepted name: GDP-mannose 6-dehydrogenase
Reaction: GDP-D-mannose + 2 NAD+ + H2O = GDP-D-mannuronate + 2 NADH + 2 H+
Other name(s): guanosine diphosphomannose dehydrogenase; GDP-mannose dehydrogenase; guanosine diphosphomannose dehydrogenase; guanosine diphospho-D-mannose dehydrogenase
Systematic name: GDP-D-mannose:NAD+ 6-oxidoreductase
Comments: Also acts on the corresponding deoxynucleoside diphosphate derivative as a substrate.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 37250-63-8
References:
1. Preiss, J. Sugar nucleotide reaction in Arthrobacter. II. Biosynthesis of guanosine diphosphomannuronate. J. Biol. Chem. 239 (1964) 3127-3132.
Accepted name: dTDP-4-dehydrorhamnose reductase
Reaction: dTDP-β-L-rhamnose + NADP+ = dTDP-4-dehydro-β-L-rhamnose + NADPH + H+
For diagram click here.
Glossary: dTDP-4-dehydro-β-L-rhamnose = dTDP-4-dehydro-6-deoxy-β-L-mannose
dTDP-β-L-rhamnose = dTDP-6-deoxy-β-L-mannose
Other name(s): dTDP-4-keto-L-rhamnose reductase; reductase, thymidine diphospho-4-ketorhamnose; dTDP-4-ketorhamnose reductase; TDP-4-keto-rhamnose reductase; thymidine diphospho-4-ketorhamnose reductase; dTDP-6-deoxy-L-mannose:NADP+ 4-oxidoreductase
Systematic name: dTDP-β-L-rhamnose:NADP+ 4-oxidoreductase
Comments: In the reverse direction, reduction on the 4-position of the hexose moiety takes place only while the substrate is bound to another enzyme that catalyses epimerization at C-3 and C-5; the complex has been referred to as dTDP-L-rhamnose synthase.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 37250-64-9
References:
1. Melo, A. and Glaser, L. The mechanism of 6-deoxyhexose synthesis. II. Conversion of deoxythymidine diphosphate 4-keto-6-deoxy-D-glucose to deoxythymidine diphosphate L-rhamnose. J. Biol. Chem. 243 (1968) 1475-1478. [PMID: 4384782]
Accepted name: dTDP-6-deoxy-L-talose 4-dehydrogenase (NADP+)
Reaction: dTDP-6-deoxy-β-L-talose + NADP+ = dTDP-4-dehydro-β-L-rhamnose + NADPH + H+
Glossary: dTDP-4-dehydro-β-L-rhamnose = dTDP-4-dehydro-6-deoxy-β-L-mannose
dTDP-6-deoxy-β-L-talose = dTDP-β-L-pneumose
Other name(s): thymidine diphospho-6-deoxy-L-talose dehydrogenase; TDP-6-deoxy-L-talose dehydrogenase; thymidine diphospho-6-deoxy-L-talose dehydrogenase; dTDP-6-deoxy-L-talose dehydrogenase (4-reductase); dTDP-6-deoxy-L-talose 4-dehydrogenase; dTDP-6-deoxy-L-talose:NADP+ 4-oxidoreductase
Systematic name: dTDP-6-deoxy-β-L-talose:NADP+ 4-oxidoreductase
Comments: Oxidation on the 4-position of the hexose moiety takes place only while the substrate is bound to another enzyme that catalyses epimerization at C-3 and C-5.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37250-65-0
References:
1. Gaugler, R.W. and Gabriel, O. Biological mechanisms involved in the formation of deoxy sugars. VII. Biosynthesis of 6-deoxy-L-talose. J. Biol. Chem. 248 (1973) 6041-6049. [PMID: 4199258]
Accepted name: GDP-6-deoxy-D-talose 4-dehydrogenase
Reaction: GDP-6-deoxy-α-D-talose + NAD(P)+ = GDP-4-dehydro-α-D-rhamnose + NAD(P)H + H+
For diagram click here.
Glossary: GDP-4-dehydro-α-D-rhamnose = GDP-4-dehydro-6-deoxy-α-D-mannose
GDP-6-deoxy-α-D-talose = GDP-α-D-pneumose
Other name(s): guanosine diphospho-6-deoxy-D-talose dehydrogenase; GDP-6-deoxy-D-talose:NAD(P)+ 4-oxidoreductase<
Systematic name: GDP-6-deoxy-α-D-talose:NAD(P)+ 4-oxidoreductase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37250-66-1
References:
1. Markovitz, A. Biosynthesis of guanosine diphosphate D-rhamnose and guanosine diphosphate D-talomethylose from guanosine diphosphate α-D-mannose. J. Biol. Chem. 239 (1964) 2091-2098.
Accepted name: UDP-N-acetylglucosamine 6-dehydrogenase
Reaction: UDP-N-acetyl-α-D-glucosamine + 2 NAD+ + H2O = UDP-2-acetamido-2-deoxy-α-D-glucuronate + 2 NADH + 2 H+
For diagram of reaction click here.
Other name(s): uridine diphosphoacetylglucosamine dehydrogenase; UDP-acetylglucosamine dehydrogenase; UDP-2-acetamido-2-deoxy-D-glucose:NAD oxidoreductase; UDP-GlcNAc dehydrogenase; WbpA; WbpO
Systematic name: UDP-N-acetyl-α-D-glucosamine:NAD+ 6-oxidoreductase
Comments: This enzyme participates in the biosynthetic pathway for UDP-α-D-ManNAc3NAcA (UDP-2,3-diacetamido-2,3-dideoxy-α-D-mannuronic acid), an important precursor of B-band lipopolysaccharide.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9054-83-5
References:
1. Fan, D.-F., John, C.E., Zalitis, J. and Feingold, D.S. UDPacetylglucosamine dehydrogenase from Achromobacter georgiopolitanum. Arch. Biochem. Biophys. 135 (1969) 45-49. [PMID: 4312076]
2. Miller, W.L., Wenzel, C.Q., Daniels, C., Larocque, S., Brisson, J.R. and Lam, J.S. Biochemical characterization of WbpA, a UDP-N-acetyl-D-glucosamine 6-dehydrogenase involved in O-antigen biosynthesis in Pseudomonas aeruginosa PAO1. J. Biol. Chem. 279 (2004) 37551-37558. [PMID: 15226302]
Accepted name: ribitol-5-phosphate 2-dehydrogenase
Reaction: D-ribitol 5-phosphate + NAD(P)+ = D-ribulose 5-phosphate + NAD(P)H + H+
Other name(s): ribitol 5-phosphate dehydrogenase
Systematic name: D-ribitol-5-phosphate:NAD(P)+ 2-oxidoreductase
Comments: The enzyme, characterized from the bacterium Lactobacillus plantarum, can use both NAD+ and NADP+ as electron acceptor [cf. EC 1.1.1.405, ribitol-5-phosphate 2-dehydrogenase (NADP+)].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37250-67-2
References:
1. Glaser, L. Ribitol-5-phosphate dehydrogenase from Lactobacillus plantarum. Biochim. Biophys. Acta 67 (1963) 525-530. [PMID: 13948358]
Accepted name: mannitol 2-dehydrogenase (NADP+)
Reaction: D-mannitol + NADP+ = D-fructose + NADPH + H+
Other name(s): mannitol 2-dehydrogenase (NADP)
Systematic name: D-mannitol:NADP+ 2-oxidoreductase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 37250-68-3
References:
1. Edmundowicz, J.M. and Wriston, J.C., Jr. Mannitol dehydrogenase from Agaricus campestris. J. Biol. Chem. 238 (1963) 3539-3541.
2. Strobel, G.A. and Kosuge, T. Polyol metabolism in Diplodia viticola Desm. Arch. Biochem. Biophys. 109 (1965) 622-626.
[EC 1.1.1.139 Deleted entry: - polyol dehydrogenase (NADP+). Now included with EC 1.1.1.21 aldehyde reductase (EC 1.1.1.139 created 1972, deleted 1978)]
Accepted name: sorbitol-6-phosphate 2-dehydrogenase
Reaction: D-sorbitol 6-phosphate + NAD+ = D-fructose 6-phosphate + NADH + H+
Other name(s): ketosephosphate reductase; ketosephosphate reductase; D-sorbitol 6-phosphate dehydrogenase; D-sorbitol-6-phosphate dehydrogenase; sorbitol-6-P-dehydrogenase; D-glucitol-6-phosphate dehydrogenase
Systematic name: D-sorbitol-6-phosphate:NAD+ 2-oxidoreductase
Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 37250-69-4
References:
1. Du Toit, P.J. and Kotzé, J.P. The isolation and characterization of sorbitol-6-phosphate dehydrogenase from Clostridium pasteurianum. Biochim. Biophys. Acta 206 (1970) 333-342. [PMID: 4318899]
2. Liss, M., Horwitz, S.B. and Kaplan, N.O. D-Mannitol 1-phosphate dehydrogenase and D-sorbitol 6-phosphate dehydrogenase in Aerobacter aerogenes. J. Biol. Chem. 237 (1962) 1342-1350.
Accepted name: 15-hydroxyprostaglandin dehydrogenase (NAD+)
Reaction: (5Z,13E,15S)-11α,15-dihydroxy-9-oxoprost-5,13-dienoate + NAD+ = (5Z,13E)-11α-hydroxy-9,15-dioxoprost-5,13-dienoate + NADH + H+
Other name(s): NAD+-dependent 15-hydroxyprostaglandin dehydrogenase (type I); PGDH; 11α,15-dihydroxy-9-oxoprost-13-enoate:NAD+ 15-oxidoreductase; 15-OH-PGDH; 15-hydroxyprostaglandin dehydrogenase; 15-hydroxyprostanoic dehydrogenase; NAD-specific 15-hydroxyprostaglandin dehydrogenase; prostaglandin dehydrogenase; 15-hydroxyprostaglandin dehydrogenase (NAD)
Systematic name: (5Z,13E,15S)-11α,15-dihydroxy-9-oxoprost-5,13-dienoate:NAD+ 15-oxidoreductase
Comments: Acts on prostaglandin E2, F2α and B1, but not on prostaglandin D2. cf. EC 1.1.1.196 15-hydroxyprostaglandin-D dehydrogenase (NADP+) and EC 1.1.1.197 15-hydroxyprostaglandin dehydrogenase (NADP+).
Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 9030-87-9
References:
1. Änggård, E. and Samuelsson, B. Purification and properties of a 15-hydroxyprostaglandin dehydrogenase from swine lung. Prostaglandins and related factors. Ark. Kemi 25 (1966) 293-300.
2. Braithwaite, S.S. and Jarabak, J. Studies on a 15-hydroxyprostaglandin dehydrogenase from human placenta. Purification and partial characterization. J. Biol. Chem. 250 (1975) 2315-2318. [PMID: 1117007]
3. Lee, S.-C. and Levine, L. Prostaglandin metabolism. II. Identification of two 15-hydroxyprostaglandin dehydrogenase types. J. Biol. Chem. 250 (1975) 548-552. [PMID: 234431]
4. Lee, S.-C., Pong, S.-S., Katzen, D., Wu, K.-Y. and Levine, L. Distribution of prostaglandin E 9-ketoreductase and types I and II 15-hydroxyprostaglandin dehydrogenase in swine kidney medulla and cortex. Biochemistry 14 (1975) 142-145. [PMID: 803247]
Accepted name: D-pinitol dehydrogenase
Reaction: 1D-3-O-methyl-chiro-inositol + NADP+ = 2D-5-O-methyl-2,3,5/4,6-pentahydroxycyclohexanone + NADPH + H+
For diagram of reaction click here.
Other name(s): 5D-3-O-methyl-chiro-inositol:NADP+ oxidoreductase
Systematic name: 1D-3-O-methyl-chiro-inositol:NADP+ oxidoreductase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37250-71-8
References:
1. Ruis, H. and Hoffmann-Ostenhof, O. Enzymic epimerization of sequoyitol to D-pinitol in Trifolium incarnatum. Eur. J. Biochem. 7 (1969) 442-448. [PMID: 4389340]
Accepted name: sequoyitol dehydrogenase
Reaction: 5-O-methyl-myo-inositol + NAD+ = 2D-5-O-methyl-2,3,5/4,6-pentahydroxycyclohexanone + NADH + H+
For diagram of reaction click here.
Other name(s): D-pinitol dehydrogenase
Systematic name: 5-O-methyl-myo-inositol:NAD+ oxidoreductase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37250-72-9
References:
1. Ruis, H. and Hoffmann-Ostenhof, O. Enzymic epimerization of sequoyitol to D-pinitol in Trifolium incarnatum. Eur. J. Biochem. 7 (1969) 442-448. [PMID: 4389340]
Accepted name: perillyl-alcohol dehydrogenase
Reaction: perillyl alcohol + NAD+ = perillyl aldehyde + NADH + H+
Other name(s): perillyl alcohol dehydrogenase
Systematic name: perillyl-alcohol:NAD+ oxidoreductase
Comments: Oxidizes a number of primary alcohols with the alcohol group allylic to an endocyclic double bond and a 6-membered ring, either aromatic or hydroaromatic.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, EAWAG-BBD , CAS registry number: 37250-73-0
References:
1. Ballal, N.R., Bhattacharyya, P.K. and Rangachari, P.N. Perillyl alcohol dehydrogenase from a soil pseudomonad. Biochem. Biophys. Res. Commun. 23 (1966) 473-478. [PMID: 4289759]
Accepted name: 3β-hydroxy-Δ5-steroid dehydrogenase
Reaction: a 3β-hydroxy-Δ5-steroid + NAD+ = a 3-oxo-Δ5-steroid + NADH + H+
For diagram click here.
Other name(s): progesterone reductase; Δ5-3β-hydroxysteroid dehydrogenase; 3β-hydroxy-5-ene steroid dehydrogenase; 3β-hydroxy steroid dehydrogenase/isomerase; 3β-hydroxy-Δ5-C27-steroid dehydrogenase/isomerase; 3β-hydroxy-Δ5-C27-steroid oxidoreductase; 3β-hydroxy-5-ene-steroid oxidoreductase; steroid-Δ5-3β-ol dehydrogenase; 3β-HSDH; 5-ene-3-β-hydroxysteroid dehydrogenase; 3β-hydroxy-5-ene-steroid dehydrogenase
Systematic name: 3β-hydroxy-Δ5-steroid:NAD+ 3-oxidoreductase
Comments: This activity is found in several bifunctional enzymes that catalyse the oxidative conversion of Δ5-3-hydroxy steroids to a Δ4-3-oxo configuration. This conversion is carried out in two separate, sequential reactions; in the first reaction, which requires NAD+, the enzyme catalyses the dehydrogenation of the 3β-hydroxy steroid to a 3-oxo intermediate. In the second reaction the reduced coesubstrate, which remains attached to the enzyme, activates the isomerization of the Δ5 form to a Δ4 form (cf. EC 5.3.3.1, steroid Δ-isomerase). Substrates include dehydroepiandrosterone (which is converted into androst-5-ene-3,17-dione), pregnenolone (converted to progesterone) and cholest-5-en-3-one, an intermediate of cholesterol degradation.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9044-85-3
References:
1. Cheatum, S.G. and Warren, J.C. Purification and properties of 3-β-hydroxysteroid dehydrogenase and Δ-5-3-ketosteroid isomerase from bovine corpora lutea. Biochim. Biophys. Acta 122 (1966) 1-13. [PMID: 4226148]
2. Koritz, S.B. The conversion of prepnenolone to progesterone by small particle from rat adrenal. Biochemistry 3 (1964) 1098-1102.
3. Neville, A.M., Orr, J.C. and Engel, L.L. Δ5-3β-Hydroxy steroid dehydrogenase activities of bovine adrenal cortex. Biochem. J. 107 (1968) 20P.
Accepted name: 11β-hydroxysteroid dehydrogenase
Reaction: an 11β-hydroxysteroid + NADP+ = an 11-oxosteroid + NADPH + H+
Other name(s): corticosteroid 11β-dehydrogenase; β-hydroxysteroid dehydrogenase; 11β-hydroxy steroid dehydrogenase; corticosteroid 11-reductase; dehydrogenase, 11β-hydroxy steroid
Systematic name: 11β-hydroxysteroid:NADP+ 11-oxidoreductase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9041-46-7
References:
1. Agarwal, A.K., Monder, C., Eckstein, B. and White, P.C. Cloning and expression of rat cDNA encoding corticosteroid 11β-dehydrogenase. J. Biol. Chem. 264 (1989) 18939-18943. [PMID: 2808402]
2. Bush, I.E., Hunter, S.A. and Meigs, R.A. Metabolism of 11-oxygenated steroids. Metabolism in vitro by preparations of liver. Biochem. J. 107 (1968) 239-258. [PMID: 4384445]
3. Lakshmi, V. and Monder, C. Purification and characterization of the corticosteroid 11β-dehydrogenase component of the rat liver 11β-hydroxysteroid dehydrogenase complex. Endocrinology 123 (1988) 2390-2398. [PMID: 3139396]
4. Phillips, D.M., Lakshmi, V. and Monder, C. Corticosteroid 11β-dehydrogenase in rat testis. Endocrinology 125 (1989) 209-216. [PMID: 2661206]
Accepted name: 16α-hydroxysteroid dehydrogenase
Reaction: a 16α-hydroxysteroid + NAD(P)+ = a 16-oxosteroid + NAD(P)H + H+
Other name(s): 16α-hydroxy steroid dehydrogenase
Systematic name: 16α-hydroxysteroid:NAD(P)+ 16-oxidoreductase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37250-74-1
References:
1. Meigs, R.A. and Ryan, K.J. 16-α-Hydroxysteroid dehydrogenase of rat kidney. Purification, assay, and properties. J. Biol. Chem. 241 (1966) 4011-4015. [PMID: 4380686]
Accepted name: estradiol 17α-dehydrogenase
Reaction: estradiol-17α + NAD(P)+ = estrone + NAD(P)H + H+
Other name(s): 17α-estradiol dehydrogenase; 17α-hydroxy steroid dehydrogenase; 17α-hydroxy steroid oxidoreductase; 17α-hydroxysteroid oxidoreductase; estradiol 17α-oxidoreductase
Systematic name: 17α-hydroxysteroid:NAD(P)+ 17-oxidoreductase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9044-91-1
References:
1. Renwick, A.G.C. and Engel, L.L. The partial purification of 17α- and 17β-estradiol dehydrogenase activities from chicken liver. Biochim. Biophys. Acta 146 (1967) 336-348. [PMID: 4383682]
Accepted name: 20α-hydroxysteroid dehydrogenase
Reaction: 17α,20α-dihydroxypregn-4-en-3-one + NAD(P)+ = 17α-hydroxyprogesterone + NAD(P)H + H+
Other name(s): 20α-hydroxy steroid dehydrogenase; 20α-hydroxy steroid dehydrogenase; 20α-HSD; 20α-HSDH
Systematic name: 20α-hydroxysteroid:NAD(P)+ 20-oxidoreductase
Comments: Re-specific with respect to NAD(P)+ (cf. EC 1.1.1.62 estradiol 17β-dehydrogenase).
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9040-08-8
References:
1. Shikita, M., Inano, H. and Tamaoki, B. Further studies on 20α-hydroxysteroid dehydrogenase of rat testes. Biochemistry 6 (1967) 1760-1764. [PMID: 4382486]
2. Strickler, R.C., Tobias, B. and Covey, D.F. Human placental 17β-estradiol dehydrogenase and 20α-hydroxysteroid dehydrogenase. Two activities at a single enzyme active site. J. Biol. Chem. 256 (1981) 316-321. [PMID: 6935192]
Accepted name: 21-hydroxysteroid dehydrogenase (NAD+)
Reaction: pregnan-21-ol + NAD+ = pregnan-21-al + NADH + H+
Other name(s): 21-hydroxysteroid dehydrogenase (NAD)
Systematic name: 21-hydroxysteroid:NAD+ 21-oxidoreductase
Comments: Acts on a number of 21-hydroxycorticosteroids.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, CAS registry number: 37250-75-2
References:
1. Monder, C. and White, A. The 21-hydroxysteroid dehydrogenases of liver. A nicotinamide adenine dinucleotide phosphate dehydrogenase and two nicotinamide adenine dinucleotide dehydrogenases. J. Biol. Chem. 240 (1965) 71-77.