Enzyme Nomenclature

EC 1.1.1 (continued)

with NAD+ or NADP+ as acceptor

Continued from:
EC 1.1.1.1 to EC 1.1.1.50
EC 1.1.1.51 to EC 1.1.1.100
See separate file 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 1.1.1.413

Contents

EC 1.1.1.101 acylglycerone-phosphate reductase
EC 1.1.1.102 3-dehydrosphinganine reductase
EC 1.1.1.103 L-threonine 3-dehydrogenase
EC 1.1.1.104 4-oxoproline reductase
EC 1.1.1.105 all-trans-retinol dehydrogenase (NAD+)
EC 1.1.1.106 pantoate 4-dehydrogenase
EC 1.1.1.107 pyridoxal 4-dehydrogenase
EC 1.1.1.108 carnitine 3-dehydrogenase
EC 1.1.1.109 now EC 1.3.1.28
EC 1.1.1.110 indolelactate dehydrogenase
EC 1.1.1.111 3-(imidazol-5-yl)lactate dehydrogenase
EC 1.1.1.112 indanol dehydrogenase
EC 1.1.1.113 L-xylose 1-dehydrogenase
EC 1.1.1.114 apiose 1-reductase
EC 1.1.1.115 ribose 1-dehydrogenase (NADP+)
EC 1.1.1.116 D-arabinose 1-dehydrogenase (NAD+)
EC 1.1.1.117 D-arabinose 1-dehydrogenase [NAD(P)+]
EC 1.1.1.128 deleted covered by EC 1.1.1.264
EC 1.1.1.119 glucose 1-dehydrogenase (NADP+)
EC 1.1.1.120 galactose 1-dehydrogenase (NADP+)
EC 1.1.1.121 aldose 1-dehydrogenase (NAD+)
EC 1.1.1.122 D-threo-aldose 1-dehydrogenase
EC 1.1.1.123 sorbose 5-dehydrogenase (NADP+)
EC 1.1.1.124 fructose 5-dehydrogenase (NADP+)
EC 1.1.1.125 2-deoxy-D-gluconate 3-dehydrogenase
EC 1.1.1.126 2-dehydro-3-deoxy-D-gluconate 6-dehydrogenase
EC 1.1.1.127 2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase
EC 1.1.1.128 L-idonate 2-dehydrogenase
EC 1.1.1.129 L-threonate 3-dehydrogenase
EC 1.1.1.130 3-dehydro-L-gulonate 2-dehydrogenase
EC 1.1.1.131 mannuronate reductase
EC 1.1.1.132 GDP-mannose 6-dehydrogenase
EC 1.1.1.133 dTDP-4-dehydrorhamnose reductase
EC 1.1.1.134 dTDP-6-deoxy-L-talose 4-dehydrogenase (NADP+)
EC 1.1.1.135 GDP-6-deoxy-D-talose 4-dehydrogenase
EC 1.1.1.136 UDP-N-acetylglucosamine 6-dehydrogenase
EC 1.1.1.137 ribitol-5-phosphate 2-dehydrogenase
EC 1.1.1.138 mannitol 2-dehydrogenase (NADP+)
EC 1.1.1.139 deleted, included in EC 1.1.1.21
EC 1.1.1.140 sorbitol-6-phosphate 2-dehydrogenase
EC 1.1.1.141 15-hydroxyprostaglandin dehydrogenase (NAD+)
EC 1.1.1.142 D-pinitol dehydrogenase
EC 1.1.1.143 sequoyitol dehydrogenase
EC 1.1.1.144 perillyl-alcohol dehydrogenase
EC 1.1.1.145 3β-hydroxy-Δ5-steroid dehydrogenase
EC 1.1.1.146 11β-hydroxysteroid dehydrogenase
EC 1.1.1.147 16α-hydroxysteroid dehydrogenase
EC 1.1.1.148 estradiol 17α-dehydrogenase
EC 1.1.1.149 20α-hydroxysteroid dehydrogenase
EC 1.1.1.150 21-hydroxysteroid dehydrogenase (NAD+)

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 1.1.1.413

Entries

When an enzyme can use either NAD+ or NADP+, the symbol NAD(P)+ is used.

EC 1.1.1.101

Accepted name: acylglycerone-phosphate reductase

Reaction: 1-palmitoylglycerol 3-phosphate + NADP+ = palmitoylglycerone phosphate + NADPH + H+

Other name(s): palmitoyldihydroxyacetone-phosphate reductase; palmitoyl dihydroxyacetone phosphate reductase; palmitoyl-dihydroxyacetone-phosphate reductase; acyldihydroxyacetone phosphate reductase; palmitoyl dihydroxyacetone phosphate reductase

Systematic name: 1-palmitoylglycerol-3-phosphate:NADP+ oxidoreductase

Comments: Also acts on alkylglycerone 3-phosphate and alkylglycerol 3-phosphate.

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]

[EC 1.1.1.101 created 1972, modified 1976]

EC 1.1.1.102

Accepted name: 3-dehydrosphinganine reductase

Reaction: sphinganine + NADP+ = 3-dehydrosphinganine + NADPH + H+

Other name(s): D-3-dehydrosphinganine reductase; D-3-oxosphinganine reductase; DSR; 3-oxosphinganine reductase; 3-oxosphinganine:NADPH oxidoreductase; D-3-oxosphinganine:B-NADPH oxidoreductase

Systematic name: D-erythro-dihydrosphingosine:NADP+ 3-oxidoreductase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, 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]

[EC 1.1.1.102 created 1972]

EC 1.1.1.103

Accepted name: L-threonine 3-dehydrogenase

Reaction: L-threonine + NAD+ = L-2-amino-3-oxobutanoate + NADH + H+

Other name(s): L-threonine dehydrogenase; threonine 3-dehydrogenase; threonine dehydrogenase; 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]

[EC 1.1.1.103 created 1972]

EC 1.1.1.104

Accepted name: 4-oxoproline reductase

Reaction: 4-hydroxy-L-proline + NAD+ = 4-oxoproline + NADH + H+

Other name(s): hydroxy-L-proline oxidase

Systematic name: 4-hydroxy-L-proline:NAD+ oxidoreductase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, 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.

[EC 1.1.1.104 created 1972]

EC 1.1.1.105

Accepted name: all-trans-retinol dehydrogenase (NAD+)

Reaction: all-trans-retinol-[cellular-retinol-binding-protein] + NAD+ = all-trans-retinal-[cellular-retinol-binding-protein] + NADH + H+

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, 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]

[EC 1.1.1.105 created 1972, modified 2011]

EC 1.1.1.106

Accepted name: pantoate 4-dehydrogenase

Reaction: (R)-pantoate + NAD+ = (R)-4-dehydropantoate + NADH + H+

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]

[EC 1.1.1.106 created 1972, modified 1976]

EC 1.1.1.107

Accepted name: pyridoxal 4-dehydrogenase

Reaction: pyridoxal + NAD+ = 4-pyridoxolactone + NADH + H+

Other name(s): pyridoxal dehydrogenase

Systematic name: pyridoxal:NAD+ 4-oxidoreductase

Comments: The enzyme acts on the hemiacetal form of the substrate.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, UM-BBD, 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]

[EC 1.1.1.107 created 1972]

EC 1.1.1.108

Accepted name: carnitine 3-dehydrogenase

Reaction: carnitine + NAD+ = 3-dehydrocarnitine + NADH + H+

Systematic name: carnitine:NAD+ 3-oxidoreductase

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 1.1.1.108 created 1972]

[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)]

EC 1.1.1.110

Accepted name: indolelactate dehydrogenase

Reaction: (indol-3-yl)lactate + NAD+ = (indol-3-yl)pyruvate + NADH + H+

Other name(s): indolelactate:NAD+ oxidoreductase

Systematic name: (indol-3-yl)lactate:NAD+ oxidoreductase

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]

[EC 1.1.1.110 created 1972]

EC 1.1.1.111

Accepted name: 3-(imidazol-5-yl)lactate dehydrogenase

Reaction: (S)-3-(imidazol-5-yl)lactate + NAD(P)+ = 3-(imidazol-5-yl)pyruvate + NAD(P)H + H+

Other name(s): imidazol-5-yl lactate dehydrogenase

Systematic name: (S)-3-(imidazol-5-yl)lactate:NAD(P)+ oxidoreductase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37250-42-3

References:

1. Coote, J.G. and Hassall, H. The role of imidazol-5-yl-lactate-nicotinamide-adenine dinucleotide phosphate oxidoreductase and histidine-2-oxoglutarate aminotransferase in the degradation of imidazol-5-yl-lactate by Pseudomonas acidovorans. Biochem. J. 111 (1969) 237-239. [PMID: 4303364]

2. Cortese, R., Brevet, J., Hedegaard, J. and Roche, J. [Identification and purification of an α-ketoacid aromatic reductase of Escherichia coli B]. C.R. Seances Soc. Biol. Fil. 162 (1968) 390-395. [French] [PMID: 4237631]

[EC 1.1.1.111 created 1972]

EC 1.1.1.112

Accepted name: indanol dehydrogenase

Reaction: indan-1-ol + NAD(P)+ = indanone + NAD(P)H + H+

Systematic name: indan-1-ol:NAD(P)+ 1-oxidoreductase

Comments: 3(20)α-Hydroxysteroids are also oxidized, more slowly.

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]

[EC 1.1.1.112 created 1972]

EC 1.1.1.113

Accepted name: L-xylose 1-dehydrogenase

Reaction: L-xylose + NADP+ = L-xylono-1,4-lactone + NADPH + H+

Other name(s): L-xylose dehydrogenase; NADPH-xylose reductase

Systematic name: L-xylose:NADP+ 1-oxidoreductase

Comments: Also oxidizes D-arabinose and D-lyxose.

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.

[EC 1.1.1.113 created 1972]

EC 1.1.1.114

Accepted name: apiose 1-reductase

Reaction: D-apiitol + NAD+ = D-apiose + NADH + H+

Other name(s): D-apiose reductase; D-apiitol reductase

Systematic name: D-apiitol:NAD+ 1-oxidoreductase

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]

[EC 1.1.1.114 created 1972]

EC 1.1.1.115

Accepted name: ribose 1-dehydrogenase (NADP+)

Reaction: D-ribose + NADP+ + H2O = D-ribonate + NADPH + H+

Other name(s): D-ribose dehydrogenase (NADP+); NADP-pentose-dehydrogenase; ribose 1-dehydrogenase (NADP)

Systematic name: D-ribose:NADP+ 1-oxidoreductase

Comments: Also acts, more slowly, on D-xylose and other pentoses.

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]

[EC 1.1.1.115 created 1972]

EC 1.1.1.116

Accepted name: D-arabinose 1-dehydrogenase (NAD+)

Reaction: D-arabinose + NAD+ = D-arabinono-1,4-lactone + NADH + H+

Other name(s): NAD-pentose-dehydrogenase; arabinose(fucose)dehydrogenase

Systematic name: D-arabinose:NAD+ 1-oxidoreductase

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]

[EC 1.1.1.116 created 1972]

EC 1.1.1.117

Accepted name: D-arabinose 1-dehydrogenase [NAD(P)+]

Reaction: D-arabinose + NAD(P)+ = D-arabinono-1,4-lactone + NAD(P)H + H+

Other name(s): D-arabinose 1-dehydrogenase [NAD(P)]

Systematic name: D-arabinose:NAD(P)+ 1-oxidoreductase

Comments: Also acts on L-galactose, 6-deoxy- and 3,6-dideoxy-L-galactose.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, 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]

[EC 1.1.1.117 created 1972]

EC 1.1.1.118

Accepted name: glucose 1-dehydrogenase (NAD+)

Reaction: D-glucose + NAD+ = D-glucono-1,5-lactone + NADH + H+

Other name(s): D-glucose:NAD oxidoreductase; D-aldohexose dehydrogenase; glucose 1-dehydrogenase (NAD)

Systematic name: D-glucose:NAD+ 1-oxidoreductase

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.

[EC 1.1.1.118 created 1972, modified 1976]

EC 1.1.1.119

Accepted name: glucose 1-dehydrogenase (NADP+)

Reaction: D-glucose + NADP+ = D-glucono-1,5-lactone + NADPH + H+

Other name(s): nicotinamide adenine dinucleotide phosphate-linked aldohexose dehydrogenase; NADP-linked aldohexose dehydrogenase; NADP-dependent glucose dehydrogenase; glucose 1-dehydrogenase (NADP)

Systematic name: D-glucose:NADP+ 1-oxidoreductase

Comments: Also oxidizes D-mannose, 2-deoxy-D-glucose and 2-amino-2-deoxy-D-mannose.

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]

[EC 1.1.1.119 created 1972]

EC 1.1.1.120

Accepted name: galactose 1-dehydrogenase (NADP+)

Reaction: D-galactose + NADP+ = D-galactono-1,5-lactone + NADPH + H+

Other name(s): D-galactose dehydrogenase (NADP+); galactose 1-dehydrogenase (NADP)

Systematic name: D-galactose:NADP+ 1-oxidoreductase

Comments: Also acts on L-arabinose, 6-deoxy- and 2-deoxy-D-galactose.

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]

[EC 1.1.1.120 created 1972]

EC 1.1.1.121

Accepted name: aldose 1-dehydrogenase (NAD+)

Reaction: D-aldose + NAD+ = D-aldonolactone + NADH + H+

Other name(s): aldose dehydrogenase; D-aldohexose dehydrogenase; aldose 1-dehydrogenase

Systematic name: D-aldose:NAD+ 1-oxidoreductase

Comments: Acts on D-glucose, 2-deoxy- and 6-deoxy-D-glucose, D-galactose, 6-deoxy-D-galactose, 2-deoxy-L-arabinose and D-xylose.

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]

[EC 1.1.1.121 created 1972]

EC 1.1.1.122

Accepted name: D-threo-aldose 1-dehydrogenase

Reaction: a D-threo-aldose + NAD+ = a D-threo-aldono-1,5-lactone + NADH + H+

Other name(s): L-fucose dehydrogenase; (2S,3R)-aldose dehydrogenase; dehydrogenase, L-fucose; L-fucose (D-arabinose) dehydrogenase

Systematic name: D-threo-aldose:NAD+ 1-oxidoreductase

Comments: Acts on L-fucose, D-arabinose and L-xylose; the animal enzyme was also shown to act on L-arabinose, and the enzyme from Pseudomonas caryophylli on L-glucose.

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]

[EC 1.1.1.122 created 1972]

EC 1.1.1.123

Accepted name: sorbose 5-dehydrogenase (NADP+)

Reaction: L-sorbose + NADP+ = 5-dehydro-D-fructose + NADPH + H+

Other name(s): 5-ketofructose reductase; 5-keto-D-fructose reductase; sorbose (nicotinamide adenine dinucleotide phosphate) dehydrogenase; reduced nicotinamide adenine dinucleotide phosphate-linked reductase; sorbose 5-dehydrogenase (NADP)

Systematic name: L-sorbose:NADP+ 5-oxidoreductase

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]

[EC 1.1.1.123 created 1972, modified 1976]

EC 1.1.1.124

Accepted name: fructose 5-dehydrogenase (NADP+)

Reaction: D-fructose + NADP+ = 5-dehydro-D-fructose + NADPH + H+

Other name(s): 5-ketofructose reductase (NADP); 5-keto-D-fructose reductase (NADP+); fructose 5-(nicotinamide adenine dinucleotide phosphate) dehydrogenase; D-(–)fructose:(NADP+) 5-oxidoreductase; fructose 5-dehydrogenase (NADP)

Systematic name: D-fructose:NADP+ 5-oxidoreductase

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]

[EC 1.1.1.124 created 1972, modified 1976]

EC 1.1.1.125

Accepted name: 2-deoxy-D-gluconate 3-dehydrogenase

Reaction: 2-deoxy-D-gluconate + NAD+ = 3-dehydro-2-deoxy-D-gluconate + NADH + H+

Other name(s): 2-deoxygluconate dehydrogenase

Systematic name: 2-deoxy-D-gluconate:NAD+ 3-oxidoreductase

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.

[EC 1.1.1.125 created 1972]

EC 1.1.1.126

Accepted name: 2-dehydro-3-deoxy-D-gluconate 6-dehydrogenase

Reaction: 2-dehydro-3-deoxy-D-gluconate + NADP+ = (4S,5S)-4,5-dihydroxy-2,6-dioxohexanoate + NADPH + H+

Other name(s): 2-keto-3-deoxy-D-gluconate dehydrogenase; 2-keto-3-deoxygluconate dehydrogenase

Systematic name: 2-dehydro-3-deoxy-D-gluconate:NADP+ 6-oxidoreductase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, 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.

[EC 1.1.1.126 created 1972]

EC 1.1.1.127

Accepted name: 2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase

Reaction: 2-dehydro-3-deoxy-D-gluconate + NAD+ = (4S)-4,6-dihydroxy-2,5-dioxohexanoate + NADH + H+

Other name(s): 2-keto-3-deoxygluconate 5-dehydrogenase; 2-keto-3-deoxy-D-gluconate dehydrogenase; 2-keto-3-deoxygluconate (nicotinamide adenine dinucleotide (phosphate)) dehydrogenase; 2-keto-3-deoxy-D-gluconate (3-deoxy-D-glycero-2,5-hexodiulosonic acid) dehydrogenase

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, 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 1.1.1.127 created 1972, modified 1976, modified 1989]

[EC 1.1.1.128 Deleted entry: L-idonate 2-dehydrogenase. The reaction described is covered by EC 1.1.1.264. (EC 1.1.1.128 created 1972, modified 1976, deleted 2012)]

EC 1.1.1.129

Accepted name: L-threonate 3-dehydrogenase

Reaction: L-threonate + NAD+ = 3-dehydro-L-threonate + 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.

[EC 1.1.1.129 created 1972]

EC 1.1.1.130

Accepted name: 3-dehydro-L-gulonate 2-dehydrogenase

Reaction: 3-dehydro-L-gulonate + NAD(P)+ = (4R,5S)-4,5,6-trihydroxy-2,3-dioxohexanoate + NAD(P)H + H+

Other name(s): 3-keto-L-gulonate dehydrogenase; 3-ketogulonate dehydrogenase; 3-keto-L-gulonate dehydrogenase; 3-ketogulonate dehydrogenase

Systematic name: 3-dehydro-L-gulonate:NAD(P)+ 2-oxidoreductase

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.

[EC 1.1.1.130 created 1972]

EC 1.1.1.131

Accepted name: mannuronate reductase

Reaction: D-mannonate + NAD(P)+ = D-mannuronate + NAD(P)H + H+

Other name(s): mannonate dehydrogenase; mannonate (nicotinamide adenine dinucleotide (phosphate))dehydrogenase; mannonate dehydrogenase; mannuronate reductase; mannonate dehydrogenase (NAD(P)+); D-mannonate:nicotinamide adenine dinucleotide (phosphate oxidoreductase (D-mannuronate-forming))

Systematic name: D-mannonate:NAD(P)+ 6-oxidoreductase

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]

[EC 1.1.1.131 created 1972 (EC 1.2.1.34 created 1972, incorporated 1983; EC 1.1.1.180 created 1983, incorporated 1984)]

EC 1.1.1.132

Accepted name: GDP-mannose 6-dehydrogenase

Reaction: GDP-D-mannose + 2 NAD+ + H2O = GDP-D-mannuronate + 2 NADH + 2 H+

Other name(s): guanosine diphosphomannose dehydrogenase; GDP-mannose dehydrogenase; guanosine diphosphomannose dehydrogenase; guanosine diphospho-D-mannose dehydrogenase

Systematic name: GDP-D-mannose:NAD+ 6-oxidoreductase

Comments: Also acts on the corresponding deoxynucleoside diphosphate derivative as a substrate.

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.

[EC 1.1.1.132 created 1972]

EC 1.1.1.133

Accepted name: dTDP-4-dehydrorhamnose reductase

Reaction: dTDP-β-L-rhamnose + NADP+ = dTDP-4-dehydro-β-L-rhamnose + NADPH + H+

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]

[EC 1.1.1.133 created 1972]

EC 1.1.1.134

Accepted name: dTDP-6-deoxy-L-talose 4-dehydrogenase (NADP+)

Reaction: dTDP-6-deoxy-β-L-talose + NADP+ = dTDP-4-dehydro-β-L-rhamnose + NADPH + H+

Glossary: dTDP-4-dehydro-β-L-rhamnose = dTDP-4-dehydro-6-deoxy-β-L-mannose
dTDP-6-deoxy-β-L-talose = dTDP-β-L-pneumose

Other name(s): thymidine diphospho-6-deoxy-L-talose dehydrogenase; TDP-6-deoxy-L-talose dehydrogenase; 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]

[EC 1.1.1.134 created 1972]

EC 1.1.1.135

Accepted name: GDP-6-deoxy-D-talose 4-dehydrogenase

Reaction: GDP-6-deoxy-α-D-talose + NAD(P)+ = GDP-4-dehydro-α-D-rhamnose + NAD(P)H + H+

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.

[EC 1.1.1.135 created 1972, modified 1976]

EC 1.1.1.136

Accepted name: UDP-N-acetylglucosamine 6-dehydrogenase

Reaction: UDP-N-acetyl-α-D-glucosamine + 2 NAD+ + H2O = UDP-2-acetamido-2-deoxy-α-D-glucuronate + 2 NADH + 2 H+

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]

[EC 1.1.1.136 created 1972, modified 2012]

EC 1.1.1.137

Accepted name: ribitol-5-phosphate 2-dehydrogenase

Reaction: D-ribitol 5-phosphate + NAD(P)+ = D-ribulose 5-phosphate + NAD(P)H + H+

Other name(s): ribitol 5-phosphate dehydrogenase

Systematic name: D-ribitol-5-phosphate:NAD(P)+ 2-oxidoreductase

Comments: The enzyme, characterized from the bacterium Lactobacillus plantarum, can use both NAD+ and NADP+ as electron acceptor [cf. EC 1.1.1.405, ribitol-5-phosphate 2-dehydrogenase (NADP+)].

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]

[EC 1.1.1.137 created 1972, modified 2017]

EC 1.1.1.138

Accepted name: mannitol 2-dehydrogenase (NADP+)

Reaction: D-mannitol + NADP+ = D-fructose + NADPH + H+

Other name(s): mannitol 2-dehydrogenase (NADP)

Systematic name: D-mannitol:NADP+ 2-oxidoreductase

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 1.1.1.138 created 1972]

[EC 1.1.1.139 Deleted entry: - polyol dehydrogenase (NADP+). Now included with EC 1.1.1.21 aldehyde reductase (EC 1.1.1.139 created 1972, deleted 1978)]

EC 1.1.1.140

Accepted name: sorbitol-6-phosphate 2-dehydrogenase

Reaction: D-sorbitol 6-phosphate + NAD+ = D-fructose 6-phosphate + NADH + H+

Other name(s): ketosephosphate reductase; ketosephosphate reductase; D-sorbitol 6-phosphate dehydrogenase; D-sorbitol-6-phosphate dehydrogenase; sorbitol-6-P-dehydrogenase; D-glucitol-6-phosphate dehydrogenase

Systematic name: D-sorbitol-6-phosphate:NAD+ 2-oxidoreductase

Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, 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.

[EC 1.1.1.140 created 1972]

EC 1.1.1.141

Accepted name: 15-hydroxyprostaglandin dehydrogenase (NAD+)

Reaction: (5Z,13E,(15S)-11α,15-dihydroxy-9-oxoprost-5,13-dienoate + NAD+ = (5Z,13E)-11α-hydroxy-9,15-dioxoprost-5,13-dienoate + NADH + H+

Other name(s): NAD+-dependent 15-hydroxyprostaglandin dehydrogenase (type I); PGDH; 11α,15-dihydroxy-9-oxoprost-13-enoate:NAD+ 15-oxidoreductase; 15-OH-PGDH; 15-hydroxyprostaglandin dehydrogenase; 15-hydroxyprostanoic dehydrogenase; NAD-specific 15-hydroxyprostaglandin dehydrogenase; prostaglandin dehydrogenase; 15-hydroxyprostaglandin dehydrogenase (NAD)

Systematic name: (5Z,13E,15S)-11α,15-dihydroxy-9-oxoprost-5,13-dienoate:NAD+ 15-oxidoreductase

Comments: Acts on prostaglandin E2, F and B1, but not on prostaglandin D2. cf. EC 1.1.1.196 15-hydroxyprostaglandin-D dehydrogenase (NADP+) and EC 1.1.1.197 15-hydroxyprostaglandin dehydrogenase (NADP+).

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]

[EC 1.1.1.141 created 1972]

EC 1.1.1.142

Accepted name: D-pinitol dehydrogenase

Reaction: 1D-3-O-methyl-chiro-inositol + NADP+ = 2D-5-O-methyl-2,3,5/4,6-pentahydroxycyclohexanone + NADPH + H+

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]

[EC 1.1.1.142 created 1972]

EC 1.1.1.143

Accepted name: sequoyitol dehydrogenase

Reaction: 5-O-methyl-myo-inositol + NAD+ = 2D-5-O-methyl-2,3,5/4,6-pentahydroxycyclohexanone + NADH + H+

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]

[EC 1.1.1.143 created 1972]

EC 1.1.1.144

Accepted name: perillyl-alcohol dehydrogenase

Reaction: perillyl alcohol + NAD+ = perillyl aldehyde + NADH + H+

Other name(s): perillyl alcohol dehydrogenase

Systematic name: perillyl-alcohol:NAD+ oxidoreductase

Comments: Oxidizes a number of primary alcohols with the alcohol group allylic to an endocyclic double bond and a 6-membered ring, either aromatic or hydroaromatic.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, UM-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]

[EC 1.1.1.144 created 1972]

EC 1.1.1.145

Accepted name: 3β-hydroxy-Δ5-steroid dehydrogenase

Reaction: a 3β-hydroxy-Δ5-steroid + NAD+ = a 3-oxo-Δ5-steroid + NADH + H+

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 coenzyme, which remains attached to the enzyme, activates the isomerization of the Δ5 form to a Δ4 form (cf. EC 5.3.3.1, steroid Δ-isomerase). Substrates include dehydroepiandrosterone (which is converted into androst-5-ene-3,17-dione), pregnenolone (converted to progesterone) and cholest-5-en-3-one, an intermediate of cholesterol degradation.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, 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.

[EC 1.1.1.145 created 1972]

EC 1.1.1.146

Accepted name: 11β-hydroxysteroid dehydrogenase

Reaction: an 11β-hydroxysteroid + NADP+ = an 11-oxosteroid + NADPH + H+

Other name(s): corticosteroid 11β-dehydrogenase; β-hydroxysteroid dehydrogenase; 11β-hydroxy steroid dehydrogenase; corticosteroid 11-reductase; dehydrogenase, 11β-hydroxy steroid

Systematic name: 11β-hydroxysteroid:NADP+ 11-oxidoreductase

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]

[EC 1.1.1.146 created 1972]

EC 1.1.1.147

Accepted name: 16α-hydroxysteroid dehydrogenase

Reaction: a 16α-hydroxysteroid + NAD(P)+ = a 16-oxosteroid + NAD(P)H + H+

Other name(s): 16α-hydroxy steroid dehydrogenase

Systematic name: 16α-hydroxysteroid:NAD(P)+ 16-oxidoreductase

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]

[EC 1.1.1.147 created 1972]

EC 1.1.1.148

Accepted name: estradiol 17α-dehydrogenase

Reaction: estradiol-17α + NAD(P)+ = estrone + NAD(P)H + H+

Other name(s): 17α-estradiol dehydrogenase; 17α-hydroxy steroid dehydrogenase; 17α-hydroxy steroid oxidoreductase; 17α-hydroxysteroid oxidoreductase; estradiol 17α-oxidoreductase

Systematic name: 17α-hydroxysteroid:NAD(P)+ 17-oxidoreductase

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]

[EC 1.1.1.148 created 1972]

EC 1.1.1.149

Accepted name: 20α-hydroxysteroid dehydrogenase

Reaction: 17α,20α-dihydroxypregn-4-en-3-one + NAD(P)+ = 17α-hydroxyprogesterone + NAD(P)H + H+

Other name(s): 20α-hydroxy steroid dehydrogenase; 20α-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]

[EC 1.1.1.149 created 1972, deleted 1983, reinstated 1986]

EC 1.1.1.150

Accepted name: 21-hydroxysteroid dehydrogenase (NAD+)

Reaction: pregnan-21-ol + NAD+ = pregnan-21-al + NADH + H+

Other name(s): 21-hydroxysteroid dehydrogenase (NAD)

Systematic name: 21-hydroxysteroid:NAD+ 21-oxidoreductase

Comments: Acts on a number of 21-hydroxycorticosteroids.

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.

[EC 1.1.1.150 created 1972]


Continued with EC 1.1.1.151 to EC 1.1.1.200
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