The Enzyme Database

Displaying entries 101-150 of 2505.

<< Previous | Next >>    printer_iconPrintable version

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, 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]
[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; TDH
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. [DOI] [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) 1245–1249. [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: 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. 298:101708 (2022). [DOI] [PMID: 35150746]
[EC 1.1.1.104 created 1972, modified 2022]
 
 
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 retinal and derivatives biosynthesis, 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 (cf. 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. [DOI] [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. [DOI] [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. [DOI] [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 pantothenate catabolism, 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, 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]
[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. [DOI] [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. [DOI] [PMID: 4310279]
[EC 1.1.1.108 created 1972]
 
 
EC 1.1.1.109      
Transferred entry: 2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase. 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: aromatic 2-oxoacid reductase
Reaction: (1) (R)-3-(phenyl)lactate + NAD+ = 3-phenylpyruvate + 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: 3-phenylpyruvate = 2-oxo-3-phenylpropanoate
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. [DOI] [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]
[EC 1.1.1.110 created 1972 (EC 1.1.1.222 created 2000, incorporated 2018), modified 2018]
 
 
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. [PMID: 4237631] (in French)
[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. [PMID: 13995171]
[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+
For diagram of D-arabinose catabolism, 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. [PMID: 13475218]
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 1.1.1.116 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+
For diagram of D-arabinose catabolism, 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]
[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, PDB, CAS registry number: 37250-49-0
References:
1.  Hu, A.S.L. and Cline, A.L. The regulation of some sugar dehydrogenases in a pseudomonad. Biochim. Biophys. Acta 93 (1964) 237–245. [DOI] [PMID: 14251301]
[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 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 1.1.1.121 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+
For diagram of L-fucose catabolism, 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. [DOI] [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. [PMID: 14285233]
[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 (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. [PMID: 14488585]
[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 (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. [PMID: 13986017]
[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-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. [PMID: 14154441]
[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. [PMID: 13926592]
[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. [PMID: 14245351]
[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 of dtdp-6-deoxyhexose biosynthesis, click here and for diagram of 6-deoxyhexose biosynthesis, click here
Glossary: dTDP-4-dehydro-β-L-rhamnose = dTDP-4-dehydro-6-deoxy-β-L-mannose
dTDP-4-β-L-rhamnose = dTDP-6-deoxy-β-L-mannose
Other name(s): dTDP-4-keto-L-rhamnose reductase; dTDP-4-ketorhamnose reductase; TDP-4-keto-rhamnose reductase; thymidine diphospho-4-ketorhamnose reductase; dTDP-6-deoxy-L-mannose:NADP+ 4-oxidoreductase; dTDP-6-deoxy-β-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; dTDP-6-deoxy-L-talose dehydrogenase (4-reductase); 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 of gdp-l-fucose and GDP-mannose biosynthesis, 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. [PMID: 14209931]
[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 UDP-N-acetylgalactosamine and UDP-N-acetylmannosamine biosynthesis, 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. [DOI] [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. [DOI] [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. [PMID: 14109183]
2.  Strobel, G.A. and Kosuge, T. Polyol metabolism in Diplodia viticola Desm. Arch. Biochem. Biophys. 109 (1965) 622–626. [DOI] [PMID: 14320506]
[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, 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. [DOI] [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. [PMID: 14465816]
[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+); (5Z,13E)-(15S)-11α,15-dihydroxy-9-oxoprost-13-enoate:NAD+ 15-oxidoreductase
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.  Änggaard, E. and Samuelsson, B. Purification and properties of a 15-hydroxyprostaglandin dehydrogenase from swine lung. Prostaglandins 25 (1996) 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+
Other name(s): 5D-5-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. [DOI] [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+
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. [DOI] [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+
For diagram of (-)-carvone, perillyl aldehyde and pulegone biosynthesis, click here
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, EAWAG-BBD, EXPASY, KEGG, MetaCyc, 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. [DOI] [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 of cholesterol catabolism (rings a, B and c), 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 cosubstrate, 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. [PMID: 14220672]
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) 20.
[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. [DOI] [PMID: 3139396]
4.  Phillips, D.M., Lakshmi, V. and Monder, C. Corticosteroid 11β-dehydrogenase in rat testis. Endocrinology 125 (1989) 209–216. [DOI] [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. [DOI] [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-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 17β-estradiol 17-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. [PMID: 14253469]
[EC 1.1.1.150 created 1972]
 
 


Data © 2001–2024 IUBMB
Web site © 2005–2024 Andrew McDonald