Continued from EC 1.2.2 to EC 1.2.99
EC 1.3.1 With NAD+ or NADP+ as acceptor
EC 1.3.2 With a cytochrome as acceptor
EC 1.3.3 With oxygen as acceptor
EC 1.3.5 With a quinone or related compound as acceptor
EC 1.3.7 With an iron-sulfur protein as acceptor
EC 1.3.98 With other, known, physiological acceptors
EC 1.3.99 With unknown physiological acceptors
See separate file for EC 1.3.1.51 to EC 1.3.1.126
See the following files for:
EC 1.3.1.51 to EC 1.3.1.123
Accepted name: dihydropyrimidine dehydrogenase (NAD+)
Reaction: (1) 5,6-dihydrouracil + NAD+ = uracil + NADH + H+
(2) 5,6-dihydrothymine + NAD+ = thymine + NADH + H+
For diagram of reaction click here.
Other name(s): dihydropyrimidine dehydrogenase; dihydrothymine dehydrogenase; pyrimidine reductase; thymine reductase; uracil reductase; dihydrouracil dehydrogenase (NAD+)
Systematic name: 5,6-dihydropyrimidine:NAD+ oxidoreductase
Comments: An iron-sulfur flavoenzyme. The enzyme was originally discovered in the uracil-fermenting bacterium, Clostridium uracilicum, which utilizes uracil and thymine as nitrogen and carbon sources for growth [1]. Since then the enzyme was found in additional organisms including Alcaligenes eutrophus [2], Pseudomonas strains [3,4] and Escherichia coli [5,6].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9026-89-5
References:
1. Campbell, L.L. Reductive degradation of pyrimidines. III. Purificaion and properties of dihydrouracil dehydrogenase. J. Biol. Chem. 227 (1957) 693-700. [PMID: 13462991]
2. Schmitt, U., Jahnke, K., Rosenbaum, K., Cook, P.F. and Schnackerz, K.D. Purification and characterization of dihydropyrimidine dehydrogenase from Alcaligenes eutrophus. Arch. Biochem. Biophys. 332 (1996) 175-182. [PMID: 8806723]
3. Kim, S. and West, T.P. Pyrimidine catabolism in Pseudomonas aeruginosa. FEMS Microbiol. Lett. 61 (1991) 175-179. [PMID: 1903745]
4. West, T.P. Pyrimidine base catabolism in Pseudomonas putida biotype B. Antonie Van Leeuwenhoek 80 (2001) 163-167. [PMID: 11759049]
5. West, T.P. Isolation and characterization of an Escherichia coli B mutant strain defective in uracil catabolism. Can. J. Microbiol. 44 (1998) 1106-1109. [PMID: 10030006]
6. Hidese, R., Mihara, H., Kurihara, T. and Esaki, N. Escherichia coli dihydropyrimidine dehydrogenase is a novel NAD-dependent heterotetramer essential for the production of 5,6-dihydrouracil. J. Bacteriol. 193 (2011) 989-993. [PMID: 21169495]
Accepted name: dihydropyrimidine dehydrogenase (NADP+)
Reaction: 5,6-dihydrouracil + NADP+ = uracil + NADPH + H+
For diagram of reaction click here.
Other name(s): dihydrothymine dehydrogenase; dihydrouracil dehydrogenase (NADP); 4,5-dihydrothymine: oxidoreductase; DPD; DHPDH; dehydrogenase, dihydrouracil (nicotinamide adenine dinucleotide phosphate); dihydrouracil dehydrogenase (NADP); DHU dehydrogenase; hydropyrimidine dehydrogenase; dihydropyrimidine dehydrogenase (NADP)
Systematic name: 5,6-dihydrouracil:NADP+ 5-oxidoreductase
Comments: Also acts on dihydrothymine.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9029-01-0
References:
1. Fritzson, P. Properties and assay of dihydrouracil dehydrogenase of rat liver. J. Biol. Chem. 235 (1960) 719-725.
2. Shiotani, T. and Weber, G. Purification and properties of dihydrothymine dehydrogenase from rat liver. J. Biol. Chem. 256 (1981) 219-224. [PMID: 7451435]
Accepted name: Δ4-3-oxosteroid 5β-reductase
Reaction: a 3-oxo-5β-steroid + NADP+ = a 3-oxo-Δ4-steroid + NADPH + H+
For diagram click here.
Other name(s): 3-oxo-Δ4-steroid 5β-reductase; 5β-reductase; androstenedione 5β-reductase; cholestenone 5β-reductase; cortisone 5β-reductase; cortisone β-reductase; cortisone Δ4-5β-reductase; steroid 5β-reductase; testosterone 5β-reductase; Δ4-3-ketosteroid 5β-reductase; Δ4-5β-reductase; Δ4-hydrogenase; 4,5β-dihydrocortisone:NADP+ Δ4-oxidoreductase; 3-oxo-5β-steroid:NADP+ Δ4-oxidoreductase; 5β-cholestan-3-one:NADP+ 4,5-oxidoreductase
Systematic name: 5β-cholestan-3-one:NADP+ 4,5-oxidoreductase
Comments: The enzyme from human efficiently catalyses the reduction of progesterone, androstenedione, 17α-hydroxyprogesterone and testosterone to 5β-reduced metabolites; it can also act on aldosterone, corticosterone and cortisol, but to a lesser extent [8]. The bile acid intermediates 7α,12α-dihydroxy-4-cholesten-3-one and 7α-hydroxy-4-cholesten-3-one can also act as substrates [9].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9029-08-7
References:
1. Forchielli, E. and Dorfman, R.I. Separation of Δ4-5α- and Δ4-5β-hydrogenases from rat liver homogenates. J. Biol. Chem. 223 (1956) 443-448. [PMID: 13376613]
2. Brown-Grant, K., Forchielli, E. and Dorfman, R.I. The Δ4-hydrogenases of guinea pig adrenal gland. J. Biol. Chem. 235 (1960) 1317-1320. [PMID: 13805063]
3. Levy, H.R. and Talalay, P. Enzymatic introduction of double bonds into steroid ring A. J. Am. Chem. Soc. 79 (1957) 2658-2659.
4. Tomkins, G.M. The enzymatic reduction of Δ4-3-ketosteroids. J. Biol. Chem. 225 (1957) 13-24. [PMID: 13416214]
5. Sugimoto, Y., Yoshida, M. and Tamaoki, B. Purification of 5β-reductase from hepatic cytosol fraction of chicken. J. Steroid Biochem. Mol. Biol. 37 (1990) 717-724. [PMID: 2278855]
6. Furuebisu, M., Deguchi, S. and Okuda, K. Identification of cortisone 5β-reductase as Δ4-3-ketosteroid 5β-reductase. Biochim. Biophys. Acta 912 (1987) 110-114. [PMID: 3828348]
7. Okuda, A. and Okuda, K. Purification and characterization of Δ4-3-ketosteroid 5β-reductase. J. Biol. Chem. 259 (1984) 7519-7524. [PMID: 6736016]
8. Charbonneau, A. and The, V.L. Genomic organization of a human 5β-reductase and its pseudogene and substrate selectivity of the expressed enzyme. Biochim. Biophys. Acta 1517 (2001) 228-235. [PMID: 11342103]
9. Kondo, K.H., Kai, M.H., Setoguchi, Y., Eggertsen, G., Sjöblom, P., Setoguchi, T., Okuda, K.I. and Björkhem, I. Cloning and expression of cDNA of human Δ4-3-oxosteroid 5β-reductase and substrate specificity of the expressed enzyme. Eur. J. Biochem. 219 (1994) 357-363. [PMID: 7508385]
[EC 1.3.1.4 Transferred entry: EC 1.3.1.4, cortisone α-reductase, transferred to EC 1.3.1.22, 3-oxo-5α-steroid 4-dehydrogenase (NADP+) (EC 1.3.1.4 created 1965, deleted 2012)]
Accepted name: cucurbitacin Δ23-reductase
Reaction: 23,24-dihydrocucurbitacin B + NAD(P)+ = cucurbitacin B + NAD(P)H + H+
Other name(s): NAD(P)H: cucurbitacin B Δ23-oxidoreductase
Systematic name: 23,24-dihydrocucurbitacin:NAD(P)+ Δ23-oxidoreductase
Comments: Requires Mn2+. Fe2+ or Zn2+ can replace Mn2+ to some extent.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37256-38-5
References:
1. Schabort, J.C. and Potgieter, D.J.J. Cucurbitacin B Δ23-reductase from Cucurbita maxima. II. Cofactor requirements, enzyme kinetics, substrate specificity and other characteristics. Biochim. Biophys. Acta 151 (1968) 47-53. [PMID: 4384331]
2. Schabort, J.C., Potgieter, D.J.J. and de Villiers, V. Cucurbitacin B Δ23-reductase from Cucurbita maxima. I. Assay methods, isolation and purification. Biochim. Biophys. Acta 151 (1968) 33-46. [PMID: 5640163]
Accepted name: fumarate reductase (NADH)
Reaction: succinate + NAD+ = fumarate + NADH + H+
Other name(s): NADH-fumarate reductase; NADH-dependent fumarate reductase; fumarate reductase (NADH2)
Systematic name: succinate:NAD+ oxidoreductase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9076-99-7
References:
1. Hopgood, M.F. and Walker, D.J. Succinic acid production by rumen bacteria. III. Enzymic studies on the formation of succinate by Ruminococcus flavefaciens. Aust. J. Biol. Sci. 22 (1969) 1413-1424.
Accepted name: meso-tartrate dehydrogenase
Reaction: meso-tartrate + NAD+ = dihydroxyfumarate + NADH + H+
Systematic name: meso-tartrate:NAD+ oxidoreductase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37251-06-2
References:
1. Kohn, L.D. and Jakoby, W.B. L- and mesotartaric acid dehydrogenase (crystalline). Methods Enzymol. 9 (1966) 236-240.
Accepted name: acyl-CoA dehydrogenase (NADP+)
Reaction: acyl-CoA + NADP+ = 2,3-dehydroacyl-CoA + NADPH + H+
Other name(s): 2-enoyl-CoA reductase; dehydrogenase, acyl coenzyme A (nicotinamide adenine dinucleotide phosphate); enoyl coenzyme A reductase; crotonyl coenzyme A reductase; crotonyl-CoA reductase; acyl-CoA dehydrogenase (NADP)
Systematic name: acyl-CoA:NADP+ 2-oxidoreductase
Comments: The liver enzyme acts on enoyl-CoA derivatives of carbon chain length 4 to 16, with optimum activity on 2-hexenoyl-CoA. In Escherichia coli, cis-specific and trans-specific enzymes exist [EC 1.3.1.37 cis-2-enoyl-CoA reductase (NADPH) and EC 1.3.1.38 trans-2-enoyl-CoA reductase (NADPH)].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 37251-07-3
References:
1. Dommes, V., Luster, W., Cvetanovic, M. and Kunau, W.-H. Purification by affinity chromatography of 2,4-dienoyl-CoA reductases from bovine liver and Escherichia coli. Eur. J. Biochem. 125 (1982) 335-341. [PMID: 6749495]
2. Seubert, W., Lamberts, I., Kramer, R. and Ohly, B. On the mechanism of malonyl-CoA-independent fatty acid synthesis. I. The mechanism of elongation of long-chain fatty acids by acetyl-CoA. Biochim. Biophys. Acta 164 (1968) 498-517. [PMID: 4387390]
Accepted name: enoyl-[acyl-carrier-protein] reductase (NADH)
Reaction: an acyl-[acyl-carrier protein] + NAD+ = a trans-2,3-dehydroacyl-[acyl-carrier protein] + NADH + H+
Other name(s): enoyl-[acyl carrier protein] reductase; enoyl-ACP reductase; NADH-enoyl acyl carrier protein reductase; NADH-specific enoyl-ACP reductase; acyl-[acyl-carrier-protein]:NAD+ oxidoreductase; fabI (gene name); inhA (gene name)
Systematic name: acyl-[acyl-carrier protein]:NAD+ oxidoreductase
Comments: The enzyme catalyses an essential step in fatty acid biosynthesis, the reduction of the 2,3-double bond in enoyl-acyl-[acyl-carrier-protein] derivatives of the elongating fatty acid moiety. The enzyme from the bacterium Escherichia coli accepts substrates with carbon chain length from 4 to 18 [3]. The enzyme from the bacterium Mycobacterium tuberculosis prefers substrates with carbon chain length from 12 to 24 carbons [4,5].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 37251-08-4
References:
1. Shimakata, T. and Stumpf, P.K. Purification and characterizations of β-ketoacyl-[acyl-carrier-protein] reductase, β-hydroxyacyl-[acylcarrier-protein] dehydrase, and enoyl-[acyl-carrier-protein] reductase from Spinacia oleracea leaves. Arch. Biochem. Biophys. 218 (1982) 77-91. [PMID: 6756317]
2. Weeks, G. and Wakil, S.J. Studies on the mechanism of fatty acid synthesis. 18. Preparation and general properties of the enoyl acyl carrier protein reductases from Escherichia coli. J. Biol. Chem. 243 (1968) 1180-1189. [PMID: 4384650]
3. Yu, X., Liu, T., Zhu, F. and Khosla, C. In vitro reconstitution and steady-state analysis of the fatty acid synthase from Escherichia coli. Proc. Natl. Acad. Sci. USA 108 (2011) 18643-18648. [PMID: 22042840]
4. Quemard, A., Sacchettini, J.C., Dessen, A., Vilcheze, C., Bittman, R., Jacobs, W.R., Jr. and Blanchard, J.S. Enzymatic characterization of the target for isoniazid in Mycobacterium tuberculosis. Biochemistry 34 (1995) 8235-8241. [PMID: 7599116]
5. Rozwarski, D.A., Vilcheze, C., Sugantino, M., Bittman, R. and Sacchettini, J.C. Crystal structure of the Mycobacterium tuberculosis enoyl-ACP reductase, InhA, in complex with NAD+ and a C16 fatty acyl substrate. J. Biol. Chem. 274 (1999) 15582-15589. [PMID: 10336454]
Accepted name: enoyl-[acyl-carrier-protein] reductase (NADPH, Si-specific)
Reaction: an acyl-[acyl-carrier protein] + NADP+ = a trans-2,3-dehydroacyl-[acyl-carrier protein] + NADPH + H+
Other name(s): acyl-ACP dehydrogenase (ambiguous); enoyl-[acyl carrier protein] (reduced nicotinamide adenine dinucleotide phosphate) reductase; NADPH 2-enoyl Co A reductase; enoyl acyl-carrier-protein reductase (ambiguous); enoyl-ACP reductase (ambiguous); acyl-[acyl-carrier-protein]:NADP+ oxidoreductase (B-specific); acyl-[acyl-carrier protein]:NADP+ oxidoreductase (B-specific); enoyl-[acyl-carrier-protein] reductase (NADPH, B-specific)
Systematic name: acyl-[acyl-carrier protein]:NADP+ oxidoreductase (Si-specific)
Comments: One of the activities of EC 2.3.1.86, fatty-acyl-CoA synthase system, an enzyme found in yeasts (Ascomycota and Basidiomycota). Catalyses the reduction of enoyl-acyl-[acyl-carrier protein] derivatives of carbon chain length from 4 to 16. The yeast enzyme is Si-specific with respect to NADP+. cf. EC 1.3.1.39, enoyl-[acyl-carrier-protein] reductase (NADPH, Re-specific) and EC 1.3.1.104, enoyl-[acyl-carrier-protein] reductase (NADPH), which describes enzymes whose stereo-specificity towards NADPH is not known. See also EC 1.3.1.9, enoyl-[acyl-carrier-protein] reductase (NADH).
Links to other databases: BRENDA, EXPASY, ExplorEnz, KEGG, MetaCyc, PDB, CAS registry number: 37251-09-5
References:
1. Seyama, T., Kasama, T., Yamakawa, T., Kawaguchi, A., Saito, K. and Okuda, S. Origin of hydrogen atoms in the fatty acids synthesized with yeast fatty acid synthetase. J. Biochem. (Tokyo) 82 (1977) 1325-1329. [PMID: 338601]
Accepted name: 2-coumarate reductase
Reaction: 3-(2-hydroxyphenyl)propanoate + NAD+ = 2-coumarate + NADH + H+
Other name(s): melilotate dehydrogenase
Systematic name: 3-(2-hydroxyphenyl)propanoate:NAD+ oxidoreductase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37251-10-8
References:
1. Levy, C.C. and Weinstein, G.D. The metabolism of coumarin by a microorganism. II. The reduction of o-coumaric acid to melilotic acid. Biochemistry 3 (1964) 1944-1947.
Accepted name: prephenate dehydrogenase
Reaction: prephenate + NAD+ = 4-hydroxyphenylpyruvate + CO2 + NADH
For diagram click here.
Other name(s): hydroxyphenylpyruvate synthase; chorismate mutase—prephenate dehydrogenase
Systematic name: prephenate:NAD+ oxidoreductase (decarboxylating)
Comments: This enzyme in the enteric bacteria also possesses chorismate mutase activity (EC 5.4.99.5 chorismate mutase) and converts chorismate into prephenate.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9044-92-2
References:
1. Koch, G.L.E., Shaw, D.C. and Gibson, F. Tyrosine biosynthesis in Aerobacter aerogenes. Purification and properties of chorismate mutase-prephenate dehydrogenase. Biochim. Biophys. Acta 212 (1970) 375-386. [PMID: 5456988]
Accepted name: prephenate dehydrogenase (NADP+)
Reaction: prephenate + NADP+ = 4-hydroxyphenylpyruvate + CO2 + NADPH
For diagram click here.
Other name(s): prephenate dehydrogenase (ambiguous); prephenate (nicotinamide adenine dinucleotide phosphate) dehydrogenase; prephenate dehydrogenase (NADP)
Systematic name: prephenate:NADP+ oxidoreductase (decarboxylating)
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 37251-11-9
References:
1. Gamborg, O.L. and Keeley, F.W. Aromatic metabolism in plants. I. A study of the prephenate dehydrogenase from bean plants. Biochim. Biophys. Acta 115 (1966) 65-72. [PMID: 4379953]
Accepted name: dihydroorotate dehydrogenase (NAD+)
Reaction: (S)-dihydroorotate + NAD+ = orotate + NADH + H+
Other name(s): orotate reductase (NADH); orotate reductase (NADH2); DHOdehase (ambiguous); DHOD (ambiguous); DHODase (ambiguous); dihydroorotate oxidase, pyrD (gene name)
Systematic name: (S)-dihydroorotate:NAD+ oxidoreductase
Comments: Binds FMN, FAD and a [2Fe-2S] cluster. The enzyme consists of two subunits, an FMN binding catalytic subunit and a FAD and iron-sulfur binding electron transfer subunit [4]. The reaction, which takes place in the cytosol, is the only redox reaction in the de-novo biosynthesis of pyrimidine nucleotides. Other class 1 dihydroorotate dehydrogenases use either fumarate (EC 1.3.98.1) or NADP+ (EC 1.3.1.15) as electron acceptor. The membrane bound class 2 dihydroorotate dehydrogenase (EC 1.3.5.2) uses quinone as electron acceptor.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 37255-26-8
References:
1. Friedmann, H.C. and Vennesland, B. Purification and properties of dihydroorotic acid dehydrogenase. J. Biol. Chem. 233 (1958) 1398-1406. [PMID: 13610849]
2. Friedmann, H.C. and Vennesland, B. Crystalline dihydroorotic dehydrogenase. J. Biol. Chem. 235 (1960) 1526-1532. [PMID: 13825167]
3. Lieberman, I. and Kornberg, A. Enzymic synthesis and breakdown of a pyrimidine, orotic acid. I. Dihydro-orotic dehydrogenase. Biochim. Biophys. Acta 12 (1953) 223-234. [PMID: 13115431]
4. Nielsen, F.S., Andersen, P.S. and Jensen, K.F. The B form of dihydroorotate dehydrogenase from Lactococcus lactis consists of two different subunits, encoded by the pyrDb and pyrK genes, and contains FMN, FAD, and [FeS] redox centers. J. Biol. Chem. 271 (1996) 29359-29365. [PMID: 8910599]
5. Rowland, P., Nørager, S., Jensen, K.F. and Larsen, S. Structure of dihydroorotate dehydrogenase B: electron transfer between two flavin groups bridged by an iron-sulphur cluster. Structure 8 (2000) 1227-1238. [PMID: 11188687]
6. Kahler, A.E., Nielsen, F.S. and Switzer, R.L. Biochemical characterization of the heteromeric Bacillus subtilis dihydroorotate dehydrogenase and its isolated subunits. Arch. Biochem. Biophys. 371 (1999) 191-201. [PMID: 10545205]
7. Marcinkeviciene, J., Tinney, L.M., Wang, K.H., Rogers, M.J. and Copeland, R.A. Dihydroorotate dehydrogenase B of Enterococcus faecalis. Characterization and insights into chemical mechanism. Biochemistry 38 (1999) 13129-13137. [PMID: 10529184]
Accepted name: dihydroorotate dehydrogenase (NADP+)
Reaction: (S)-dihydroorotate + NADP+ = orotate + NADPH + H+
Other name(s): orotate reductase; dihydro-orotic dehydrogenase; L-5,6-dihydro-orotate:NAD+ oxidoreductase; orotate reductase (NADPH)
Systematic name: (S)-dihydroorotate:NADP+ oxidoreductase
Comments: Binds FMN and FAD [2]. Other class 1 dihydroorotate dehydrogenases use either fumarate (EC 1.3.98.1) or NAD+ (EC 1.3.1.14) as electron acceptor. The membrane bound class 2 dihydroorotate dehydrogenase (EC 1.3.5.2) uses quinone as electron acceptor .
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37255-27-9
References:
1. Taylor, W.H., Taylor, M.L. and Eames, D.F. Two functionally different dihydroorotic dehydrogenases in bacteria. J. Bacteriol. 91 (1966) 2251-2256. [PMID: 4380263]
2. Udaka, S. and Vennesland, B. Properties of triphosphopyridine nucleotide-linked dihydroorotic dehydrogenase. J. Biol. Chem. 237 (1962) 2018-2024. [PMID: 13923427]
Accepted name: β-nitroacrylate reductase
Reaction: 3-nitropropanoate + NADP+ = 3-nitroacrylate + NADPH + H+
Systematic name: 3-nitropropanoate:NADP+ oxidoreductase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37255-28-0
References:
1. Shaw, P.D. Biosynthesis of nitro compounds. III. The enzymatic reduction of β-nitroacrylic acid to β-nitropropionic acid. Biochemistry 6 (1967) 2253-2260.
Accepted name: 3-methyleneoxindole reductase
Reaction: 3-methyl-1,3-dihydroindol-2-one + NADP+ = 3-methylene-1,3-dihydro-2H-indol-2-one + NADPH + H+
Other name(s): 3-methyloxindole:NADP+ oxidoreductase
Systematic name: 3-methyl-1,3-dihydroindol-2-one:NADP+ oxidoreductase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37255-29-1
References:
1. Moyed, H.S. and Williamson, V. Multiple 3-methyleneoxindole reductases of peas, differential inhibition by synthetic auxins. J. Biol. Chem. 242 (1967) 1075-1077. [PMID: 6021071]
Accepted name: kynurenate-7,8-dihydrodiol dehydrogenase
Reaction: 7,8-dihydro-7,8-dihydroxykynurenate + NAD+ = 7,8-dihydroxykynurenate + NADH + H+
Other name(s): 7,8-dihydro-7,8-dihydroxykynurenate dehydrogenase; 7,8-dihydroxykynurenic acid 7,8-diol dehydrogenase
Systematic name: 7,8-dihydro-7,8-dihydroxykynurenate:NAD+ oxidoreductase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37255-30-4
References:
1. Taniuchi, H. and Hayaishi, O. Studies on the metabolism of kynurenic acid. III. Enzymatic formation of 7,8-dihydroxykynurenic acid from kynurenic acid. J. Biol. Chem. 238 (1963) 283-293.
Accepted name: cis-1,2-dihydrobenzene-1,2-diol dehydrogenase
Reaction: cis-1,2-dihydrobenzene-1,2-diol + NAD+ = catechol + NADH + H+
Other name(s): cis-benzene glycol dehydrogenase; cis-1,2-dihydrocyclohexa-3,5-diene (nicotinamide adenine dinucleotide) oxidoreductase;
Systematic name: cis-1,2-dihydrobenzene-1,2-diol:NAD+ oxidoreductase
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, KEGG, Metacyc, CAS registry number: 51923-03-6
References:
1. Axcell, B.C. and Geary, P.J. The metabolism of benzene by bacteria. Purification and some properties of the enzyme cis-1,2-dihydroxycyclohexa-3,5-diene (nicotinamide adenine dinucleotide) oxidoreductase (cis-benzene glycol dehydrogenase). Biochem. J. 136 (1973) 927-934. [PMID: 4362337]
2. Gibson, D.T., Koch, J.R. and Kallio, R.E. Oxidative degradation of aromatic hydrocarbons by microorganisms. I. Enzymatic formation of catechol from benzene. Biochemistry 7 (1968) 2653-2662. [PMID: 4298226]
Accepted name: trans-1,2-dihydrobenzene-1,2-diol dehydrogenase
Reaction: trans-1,2-dihydrobenzene-1,2-diol + NADP+ = catechol + NADPH + H+
Other name(s): dihydrodiol dehydrogenase
Systematic name: trans-1,2-dihydrobenzene-1,2-diol:NADP+ oxidoreductase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 37255-32-6
References:
1. Ayengar, P.K., Hayaishi, O., Nakajima, M. and Tomida, I. Enzymic aromatization of 3,5-cyclohexadiene-1,2-diol. Biochim. Biophys. Acta 33 (1959) 111-119.
Accepted name: 7-dehydrocholesterol reductase
Reaction: cholesterol + NADP+ = cholesta-5,7-dien-3β-ol + NADPH + H+
For diagram of reaction click here.
Other name(s): DAF-36 (gene name); DHCR7 (gene name); 7-DHC reductase; 7-dehydrocholesterol dehydrogenase/cholesterol oxidase; Δ7-sterol reductase
Systematic name: cholesterol:NADP+ Δ7-oxidoreductase
Comments: The enzyme is part of the cholesterol biosynthesis.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9080-21-1
References:
1. Dempsey, M.E., Seaton, J.D., Schroepfer, G.J. and Trockman, R.W. The intermediary role of Δ5,7-cholestadien-3β-ol in cholesterol biosynthesis. J. Biol. Chem. 239 (1964) 1381-1387. [PMID: 14189869]
2. Moebius, F.F., Fitzky, B.U., Lee, J.N., Paik, Y.K. and Glossmann, H. Molecular cloning and expression of the human Δ7-sterol reductase. Proc. Natl. Acad. Sci. USA 95 (1998) 1899-1902. [PMID: 9465114]
Accepted name: 3-oxo-5α-steroid 4-dehydrogenase (NADP+)
Reaction: a 3-oxo-5α-steroid + NADP+ = a 3-oxo-Δ4-steroid + NADPH + H+
Other name(s): cholestenone 5α-reductase; testosterone Δ4-5α-reductase; steroid 5α-reductase; 3-oxosteroid Δ4-dehydrogenase; 5α-reductase; steroid 5α-hydrogenase; 3-oxosteroid 5α-reductase; testosterone Δ4-hydrogenase; 4-ene-3-oxosteroid 5α-reductase; reduced nicotinamide adenine dinucleotide phosphate:Δ4-3-ketosteroid 5α-oxidoreductase; 4-ene-5α-reductase; Δ4-3-ketosteroid 5α-oxidoreductase; cholest-4-en-3-one 5α-reductase; testosterone 5α-reductase; 3-oxo-5α-steroid 4-dehydrogenase
Systematic name: 3-oxo-5α-steroid:NADP+ Δ4-oxidoreductase
Comments: The enzyme catalyses the conversion of assorted 3-oxo-Δ4 steroids into their corresponding 5α form. Substrates for the mammalian enzyme include testosterone, progesterone, and corticosterone. Substrates for the plant enzyme are brassinosteroids such as campest-4-en-3-one and (22α)-hydroxy-campest-4-en-3-one. cf. EC 1.3.99.5, 3-oxo-5α-steroid 4-dehydrogenase (acceptor).
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 37255-34-8
References:
1. Levy, H.R. and Talalay, P. Bacterial oxidation of steroids. II. Studies on the enzymatic mechanisms of ring A dehydrogenation. J. Biol. Chem. 234 (1959) 2014-2021. [PMID: 13673006]
2. Shefer, S., Hauser, S. and Mosbach, E.H. Studies on the biosynthesis of 5α-cholestan-3β-ol. I. Cholestenone 5α-reductase of rat liver. J. Biol. Chem. 241 (1966) 946-952. [PMID: 5907469]
3. Cheng, Y.-J. and Karavolas, H.J. Properties and subcellular distribution of Δ4-steroid (progesterone) 5α-reductase in rat anterior pituitary. Steroids 26 (1975) 57-71. [PMID: 1166484]
4. Sargent, N.S. and Habib, F.K. Partial purification of human prostatic 5α-reductase (3-oxo-5α-steroid:NADP+ 4-ene-oxido-reductase; EC 1.3.1.22) in a stable and active form. J. Steroid Biochem. Mol. Biol. 38 (1991) 73-77. [PMID: 1705142]
5. Quemener, E., Amet, Y., di Stefano, S., Fournier, G., Floch, H.H. and Abalain, J.H. Purification of testosterone 5α-reductase from human prostate by a four-step chromatographic procedure. Steroids 59 (1994) 712-718. [PMID: 7900170]
6. Poletti, A., Celotti, F., Rumio, C., Rabuffetti, M. and Martini, L. Identification of type 1 5α-reductase in myelin membranes of male and female rat brain. Mol. Cell. Endocrinol. 129 (1997) 181-190. [PMID: 9202401]
7. Li, J., Biswas, M.G., Chao, A., Russell, D.W. and Chory, J. Conservation of function between mammalian and plant steroid 5α-reductases. Proc. Natl. Acad. Sci. USA 94 (1997) 3554-3559. [PMID: 9108014]
8. Rosati, F., Bardazzi, I., De Blasi, P., Simi, L., Scarpi, D., Guarna, A., Serio, M., Racchi, M.L. and Danza, G. 5α-Reductase activity in Lycopersicon esculentum: cloning and functional characterization of LeDET2 and evidence of the presence of two isoenzymes. J. Steroid Biochem. Mol. Biol. 96 (2005) 287-299. [PMID: 15993049]
[EC 1.3.1.23 Deleted entry: cholestenone β-reductase. The enzyme is identical to EC 1.3.1.3, Δ4-3-oxosteroid 5β-reductase. (EC 1.3.1.23 created 1972, deleted 2005)]
Accepted name: biliverdin reductase
Reaction: bilirubin + NAD(P)+ = biliverdin + NAD(P)H + H+
For diagram click here.
Systematic name: bilirubin:NAD(P)+ oxidoreductase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9074-10-6
References:
1. Singleton, J.W. and Laster, L. Biliverdin reductase of guinea pig liver. J. Biol. Chem. 240 (1965) 4780-4789. [PMID: 4378982]
Accepted name: 1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase
Reaction: (1R,6S)-1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate + NAD+ = catechol + CO2 + NADH + H+
For diagram click here.
Other name(s): 3,5-cyclohexadiene-1,2-diol-1-carboxylate dehydrogenase; 3,5-cyclohexadiene-1,2-diol-1-carboxylic acid dehydrogenase; dihydrodihydroxybenzoate dehydrogenase; DHBDH; cis-1,2-dihydroxycyclohexa-3,5-diene-1-carboxylate dehydrogenase; 2-hydro-1,2-dihydroxybenzoate dehydrogenase; cis-1,2-dihydroxycyclohexa-3,5-diene-1-carboxylate:NAD+ oxidoreductase; dihydrodihydroxybenzoate dehydrogenase
Systematic name: (1R,6R)-1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate:NAD+ oxidoreductase (decarboxylating)
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, KEGG, Metacyc, CAS registry number: 60496-16-4
References:
1. Reiner, A.M. Metabolism of aromatic compounds in bacteria. Purification and properties of the catechol-forming enzyme, 3,5-cyclohexadiene-1,2-diol-1-carboxylic acid (NAD+) oxidoreductase (decarboxylating). J. Biol. Chem. 247 (1972) 4960-4965. [PMID: 4341530]
2. Neidle, E.L., Hartnett, C., Ornston, N.L., Bairoch, A., Rekik, M. and Harayama, S. cis-Diol dehydrogenases encoded by the TOL pWW0 plasmid xylL gene and the Acinetobacter calcoaceticus chromosomal benD gene are members of the short-chain alcohol dehydrogenase superfamily. Eur. J. Biochem. 204 (1992) 113-120. [PMID: 1740120]
[EC 1.3.1.26 Transferred entry: dihydrodipicolinate reductase. Now EC 1.17.1.8, 4-hydroxy-tetrahydrodipicolinate reductase. (EC 1.3.1.26 created 1976, modified 2011, deleted 2013)]
Accepted name: 2-hexadecenal reductase
Reaction: hexadecanal + NADP+ = 2-trans-hexadecenal + NADPH + H+
Other name(s): 2-alkenal reductase; hexadecanal: NADP+ oxidoreductase
Systematic name: hexadecanal:NADP+ Δ2-oxidoreductase
Comments: Specific for long chain 2-trans- and 2-cis-alkenals, with chain length optimum around 14 to 16 carbon atoms.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 52227-95-9
References:
1. Stoffel, W. and Därr, W. 2-Alkenal reductase isolation, properties and specificities. Hoppe-Seyler's Z. Physiol. Chem. 355 (1974) 54-60. [PMID: 4154890]
Accepted name: 2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase
Reaction: (2S,3S)-2,3-dihydro-2,3-dihydroxybenzoate + NAD+ = 2,3-dihydroxybenzoate + NADH + H+
For diagram of reaction, click here.
Other name(s): 2,3-DHB dehydrogenase; 2,3-dihydro-2,3-dihydroxybenzoate:NAD+ oxidoreductase
Systematic name: (2S,3S)-2,3-dihydro-2,3-dihydroxybenzoate:NAD+ oxidoreductase
Comments: Formerly EC 1.1.1.109.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 37250-40-1
References:
1. Young, I.G. and Gibson, F. Regulation of the enzymes involved in the biosynthesis of 2,3-dihydroxybenzoic acid in Aerobacter aerogenes and Escherichia coli. Biochim. Biophys. Acta 177 (1969) 401-411. [PMID: 4306838]
Accepted name: cis-1,2-dihydro-1,2-dihydroxynaphthalene dehydrogenase
Reaction: (1R,2S)-1,2-dihydronaphthalene-1,2-diol + NAD+ = naphthalene-1,2-diol + NADH + H+
For diagram of reaction click here.
Other name(s): (+)-cis-naphthalene dihydrodiol dehydrogenase; naphthalene dihydrodiol dehydrogenase; cis-dihydrodiol naphthalene dehydrogenase; cis-1,2-dihydronaphthalene-1,2-diol:NAD+ 1,2-oxidoreductase
Systematic name: (1R,2S)-1,2-dihydronaphthalene-1,2-diol:NAD+ 1,2-oxidoreductase
Comments: Also acts, at half the rate, on cis-anthracene dihydrodiol and cis-phenanthrene dihydrodiol.
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, KEGG, Metacyc, CAS registry number: 53986-49-5
References:
1. Patel, T.R. and Gibson, D.T. Purification and properties of (+)-cis-naphthalene dihydrodiol dehydrogenase of Pseudomonas putida. J. Bacteriol. 119 (1974) 879-888. [PMID: 4369091]
[EC 1.3.1.30 Transferred entry: EC 1.3.1.30, progesterone 5α-reductase, transferred to EC 1.3.1.22, 3-oxo-5α-steroid 4-dehydrogenase (NADP+). (EC 1.3.1.30 created 1978, deleted 2012)]
Accepted name: 2-enoate reductase
Reaction: butanoate + NAD+ = but-2-enoate + NADH + H+
Other name(s): enoate reductase
Systematic name: butanoate:NAD+ Δ2-oxidoreductase
Comments: An iron-sulfur-flavoprotein (FAD). Acts (in the reverse direction) on a wide range of alkyl and aryl αβ-unsaturated carboxylate ions; but-2-enoate was the best substrate tested.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 70712-51-5
References:
1. Tischer, W., Bader, J. and Simon, H. Purification and some properties of a hitherto-unknown enzyme reducing the carbon-carbon double bond of α,β-unsaturated carboxylate anions. Eur. J. Biochem. 97 (1979) 103-112. [PMID: 477658]
Accepted name: maleylacetate reductase
Reaction: 3-oxoadipate + NAD(P)+ = 2-maleylacetate + NAD(P)H + H+
For diagram of reaction click here.
Other name(s): maleoylacetate reductase
Systematic name: 3-oxoadipate:NAD(P)+ oxidoreductase
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 69669-65-4
References:
1. Gaal, A.B. and Neujahr, H.Y. Maleylacetate reductase from Trichosporon cutaneum. Biochem. J. 185 (1980) 783-786.
2. Gaal, A.B. and Neujahr, H.Y. Induction of phenol-metabolizing enzymes in Trichosporon cutaneum. Arch. Microbiol. 130 (1981) 54-58.
Accepted name: protochlorophyllide reductase
Reaction: chlorophyllide a + NADP+ = protochlorophyllide + NADPH + H+
For diagram of reaction click here.
Other name(s): NADPH2-protochlorophyllide oxidoreductase; NADPH—protochlorophyllide oxidoreductase; NADPH-protochlorophyllide reductase; protochlorophyllide oxidoreductase; protochlorophyllide photooxidoreductase; light-dependent protochlorophyllide reductase
Systematic name: chlorophyllide-a:NADP+ 7,8-oxidoreductase
Comments: The enzyme catalyses a light-dependent trans-reduction of the D-ring of protochlorophyllide; the product has the (7S,8S)-configuration.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 68518-04-7
References:
1. Apel, K., Santel, H.-J., Redlinger, T.E. and Falk, H. The protochlorophyllide holochrome of barley (Hordeum vulgare L.). Isolation and characterization of the NADPH:protochlorophyllide oxidoreductase. Eur. J. Biochem. 111 (1980) 251-258. [PMID: 7439188]
2. Griffiths, W.T. Reconstitution of chlorophyllide formation by isolated etioplast membranes. Biochem. J. 174 (1978) 681-692. [PMID: 31865]
Accepted name: 2,4-dienoyl-CoA reductase [(2E)-enoyl-CoA-producing]
Reaction: (1) a (2E)-2-enoyl-CoA + NADP+ = a (2E,4E)-2,4-dienoyl-CoA + NADPH + H+
(2) a (2E)-2-enoyl-CoA + NADP+ = a (2E,4Z)-2,4-dienoyl-CoA + NADPH + H+
Other name(s): fadH (gene name); 4-enoyl-CoA reductase (NADPH) (ambiguous); 4-enoyl coenzyme A (reduced nicotinamide adenine dinucleotide phosphate) reductase (ambiguous); 4-enoyl-CoA reductase (ambiguous); 2,4-dienoyl-CoA reductase (NADPH) (ambiguous); trans-2,3-didehydroacyl-CoA:NADP+ 4-oxidoreductase
Systematic name: (2E)-2-enoyl-CoA:NADP+ 4-oxidoreductase
Comments: This bacterial enzyme catalyses the reduction of either (2E,4E)-2,4-dienoyl-CoA or (2E,4Z)-2,4-dienoyl-CoA to (2E)-2-enoyl-CoA. The enzyme from Escherichia coli contains FAD, FMN, and an [4Fe-4S] iron sulfur cluster. cf. EC 1.3.1.124, 2,4-dienoyl-CoA reductase [(3E)-enoyl-CoA-producing].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 82869-38-3
References:
1. Dommes, V., Luster, W., Cvetanovic, M. and Kunau, W.-H. Purification by affinity chromatography of 2,4-dienoyl-CoA reductases from bovine liver and Escherichia coli. Eur. J. Biochem. 125 (1982) 335-341. [PMID: 6749495]
2. Dommes, V. and Kunau, W.H. 2,4-Dienoyl coenzyme A reductases from bovine liver and Escherichia coli. Comparison of properties. J. Biol. Chem. 259 (1984) 1781-1788. [PMID: 6363415]
3. You, S.Y., Cosloy, S. and Schulz, H. Evidence for the essential function of 2,4-dienoyl-coenzyme A reductase in the β-oxidation of unsaturated fatty acids in vivo. Isolation and characterization of an Escherichia coli mutant with a defective 2,4-dienoyl-coenzyme A reductase. J. Biol. Chem. 264 (1989) 16489-16495. [PMID: 2506179]
4. He, X.Y., Yang, S.Y. and Schulz, H. Cloning and expression of the fadH gene and characterization of the gene product 2,4-dienoyl coenzyme A reductase from Escherichia coli. Eur. J. Biochem. 248 (1997) 516-520. [PMID: 9346310]
5. Liang, X., Thorpe, C. and Schulz, H. 2,4-Dienoyl-CoA reductase from Escherichia coli is a novel iron-sulfur flavoprotein that functions in fatty acid β-oxidation. Arch. Biochem. Biophys. 380 (2000) 373-379. [PMID: 10933894]
6. Hubbard, P.A., Liang, X., Schulz, H. and Kim, J.J. The crystal structure and reaction mechanism of Escherichia coli 2,4-dienoyl-CoA reductase. J. Biol. Chem. 278 (2003) 37553-37560. [PMID: 12840019]
7. Tu, X., Hubbard, P.A., Kim, J.J. and Schulz, H. Two distinct proton donors at the active site of Escherichia coli 2,4-dienoyl-CoA reductase are responsible for the formation of different products. Biochemistry 47 (2008) 1167-1175. [PMID: 18171025]
[EC 1.3.1.35 Transferred entry: phosphatidylcholine desaturase. Now EC 1.14.19.22, microsomal oleoyl-lipid 12-desaturase (EC 1.3.1.35 created 1984, deleted 2015)]
Accepted name: geissoschizine dehydrogenase
Reaction: geissoschizine + NADP+ = 4,21-didehydrogeissoschizine + NADPH
For diagram click here.
Systematic name: geissoschizine:NADP+ 4,21-oxidoreductase
Comments: Involved in the interconversion of heteroyohimbine alkaloids in Catharanthus roseus.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 84399-94-0
References:
1. Pfitzner, A. and Stöckigt, J. Partial-purification and characterization of geissoschizine dehydrogenase from suspension-cultures of Catharanthus roseus. Phytochemistry 21 (1982) 1585-1588.
Accepted name: cis-2-enoyl-CoA reductase (NADPH)
Reaction: acyl-CoA + NADP+ = cis-2,3-dehydroacyl-CoA + NADPH + H+
Other name(s): NADPH-dependent cis-enoyl-CoA reductase; reductase, cis-2-enoyl coenzyme A; cis-2-enoyl-coenzyme A reductase; cis-2-enoyl-CoA reductase (NADPH2)
Systematic name: acyl-CoA:NADP+ cis-2-oxidoreductase
Comments: Not identical with EC 1.3.1.38 trans-2-enoyl-CoA reductase (NADPH) [cf. EC 1.3.1.8 acyl-CoA dehydrogenase (NADP+)].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 72841-00-0
References:
1. Mizugaki, M., Nishimaki, T., Shiraishi, T., Kawaguchi, A., Okuda, S. and Yamanaka, H. Studies on the metabolism of unsaturated fatty acids. IX. Stereochemical studies of the reaction catalyzed by trans-2-enoyl-coenzyme A reductase of Escherichia coli. J. Biochem. (Tokyo) 92 (1982) 1649-1654. [PMID: 6759504]
Accepted name: trans-2-enoyl-CoA reductase (NADPH)
Reaction: acyl-CoA + NADP+ = trans-2,3-dehydroacyl-CoA + NADPH + H+
Other name(s): NADPH-dependent trans-2-enoyl-CoA reductase; reductase, trans-enoyl coenzyme A; trans-2-enoyl-CoA reductase (NADPH2)
Systematic name: acyl-CoA:NADP+ trans-2-oxidoreductase
Comments: Not identical with EC 1.3.1.37 cis-2-enoyl-CoA reductase (NADPH) [cf. EC 1.3.1.8 acyl-CoA dehydrogenase (NADP+)].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 77649-64-0
References:
1. Mizugaki, M., Nishimaki, T., Shiraishi, T., Kawaguchi, A., Okuda, S. and Yamanaka, H. Studies on the metabolism of unsaturated fatty acids. IX. Stereochemical studies of the reaction catalyzed by trans-2-enoyl-coenzyme A reductase of Escherichia coli. J. Biochem. (Tokyo) 92 (1982) 1649-1654. [PMID: 6759504]
Accepted name: enoyl-[acyl-carrier-protein] reductase (NADPH, Re-specific)
Reaction: an acyl-[acyl-carrier protein] + NADP+ = a trans-2,3-dehydroacyl-[acyl-carrier protein] + NADPH + H+
Other name(s): acyl-ACP dehydrogenase; enoyl-[acyl carrier protein] (reduced nicotinamide adenine dinucleotide phosphate) reductase; NADPH 2-enoyl Co A reductase; enoyl-ACp reductase; enoyl-[acyl-carrier-protein] reductase (NADPH2, A-specific); acyl-[acyl-carrier-protein]:NADP+ oxidoreductase (A-specific); enoyl-[acyl-carrier-protein] reductase (NADPH, A-specific); acyl-[acyl-carrier protein]:NADP+ oxidoreductase (A-specific)
Systematic name: acyl-[acyl-carrier protein]:NADP+ oxidoreductase (Re-specific)
Comments: This enzyme completes each cycle of fatty acid elongation by catalysing the stereospecific reduction of the double bond at position 2 of a growing fatty acid chain, while linked to an acyl-carrier protein. It is one of the activities of EC 2.3.1.85, fatty-acid synthase system. The mammalian enzyme is Re-specific with respect to NADP+. cf. EC 1.3.1.10, enoyl-[acyl-carrier-protein] reductase (NADPH, Si-specific) and EC 1.3.1.104, enoyl-[acyl-carrier-protein] reductase (NADPH).
Links to other databases: BRENDA, EXPASY, ExplorEnz, KEGG, MetaCyc, PDB, CAS registry number:
References:
1. Dugan, R.E., Slakey, L.L. and Porter, L.W. Stereospecificity of the transfer of hydrogen from reduced nicotinamide adenine dinucleotide phosphate to the acyl chain in the dehydrogenase-catalyzed reactions of fatty acid synthesis. J. Biol. Chem. 245 (1970) 6312-6316. [PMID: 4394955]
2. Carlisle-Moore, L., Gordon, C.R., Machutta, C.A., Miller, W.T. and Tonge, P.J. Substrate recognition by the human fatty-acid synthase. J. Biol. Chem. 280 (2005) 42612-42618. [PMID: 16215233]
Accepted name: 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate reductase
Reaction: 2,6-dioxo-6-phenylhexanoate + NADP+ = 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate + NADPH + H+
Other name(s): 2-hydroxy-6-oxo-phenylhexa-2,4-dienoate (reduced nicotinamide adenine dinucleotide phosphate) reductase
Systematic name: 2,6-dioxo-6-phenylhexanoate:NADP+ Δ2-oxidoreductase
Comments: Broad specificity; reduces a number of compounds produced by Pseudomonas from aromatic hydrocarbons by ring fission.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 104645-83-2
References:
1. Omori, T., Ishigooka, H. and Minoda, Y. Purification and some properties of 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid(HOPDA) reducing enzyme from Pseudomonas cruciviae S93B1 involved in the degradation of biphenyl. Agric. Biol. Chem. 50 (1986) 1513-1518.
Accepted name: xanthommatin reductase
Reaction: 5,12-dihydroxanthommatin + NAD+ = xanthommatin + NADH + H+
Systematic name: 5,12-dihydroxanthommatin:NAD+ oxidoreductase
Comments: From Drosophila melanogaster.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 62972-27-4
References:
1. Santoro, P. and Parisi, G. A new enzyme from Drosophila melanogaster - in vitro conversion of xanthommatin into its dihydroform by means of xanthommatin reductase. J. Exp. Zool. 239 (1986) 169-173.
Accepted name: 12-oxophytodienoate reductase
Reaction: (9S,13S,15Z)-12-oxo-10,11-dihydrophyto-15-enoate + NADP+ = (9S,13S,15Z)-12-oxophyto-10,15-dienoate + NADPH + H+
Glossary: (9S,13S,15Z)-12-oxo-10,11-dihydrophyto-15-enoate = 8-[(1S,2S)-3-oxo-2-{(Z)-pent-2-en-1-yl}cyclopentyl]octanoate
Other name(s): 12-oxo-phytodienoic acid reductase; 8-[(1R,2R)-3-oxo-2-{(Z)-pent-2-enyl}cyclopentyl]octanoate:NADP+ 4-oxidoreductase; (9S,13S)-10,11-dihydro-12-oxo-15-phytoenoate:NADP+ 4-oxidoreductase; 8-[(1R,2R)-3-oxo-2-{(Z)-pent-2-enyl}cyclopentyl]octanoate:NADP+ 4-oxidoreductase
Systematic name: (9S,13S,15Z)-12-oxo-10,11-dihydrophyto-15-enoate:NADP+ 10-oxidoreductase
Comments: The enzyme catalyses the reduction of (9S,13S,15Z)-12-oxophyto-10,15-dienoate during the biosynthesis of jasmonate from α-linolenate in Zea mays.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 101150-03-2
References:
1. Vick, B.A. and Zimmerman, D.C. Characterization of 12-oxo-phytodienoic acid reductase in corn - the jasmonic acid pathway. Plant Physiol. 80 (1986) 202-205.
2. Schaller, F., Biesgen, C., Mussig, C., Altmann, T. and Weiler, E.W. 12-Oxophytodienoate reductase 3 (OPR3) is the isoenzyme involved in jasmonate biosynthesis. Planta 210 (2000) 979-984. [PMID: 10872231]
Accepted name: arogenate dehydrogenase
Reaction: L-arogenate + NAD+ = L-tyrosine + NADH + CO2
For diagram of reaction click here.
Glossary: L-arogenate = 1-[(2S)-2-amino-2-carboxyethyl]-4-hydroxycyclohexa-2,5-diene-1-carboxylate
Other name(s): arogenic dehydrogenase (ambiguous); cyclohexadienyl dehydrogenase (ambiguous); pretyrosine dehydrogenase (ambiguous); L-arogenate:NAD+ oxidoreductase; arogenate dehydrogenase (NAD+)
Systematic name: L-arogenate:NAD+ oxidoreductase (decarboxylating)
Comments: Arogenate dehydrogenases may utilize NAD+ (EC 1.3.1.43), NADP+ (EC 1.3.1.78), or both (EC 1.3.1.79). NAD+-specific enzymes have been reported from some bacteria [2] and plants [3]. Some enzymes also possess the activity of EC 1.3.1.12, prephenate dehydrogenase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 64295-75-6
References:
1. Stenmark, S.L., Pierson, D.L., Jensen, R.A. and Glover, G.I. Blue-green bacteria synthesise L-tyrosine by the pretyrosine pathway. Nature 247 (1974) 290-292. [PMID: 4206476]
2. Byng, G.S., Whitaker, R.J., Gherna, R.L. and Jensen, R.A. Variable enzymological patterning in tyrosine biosynthesis as a means of determining natural relatedness among the Pseudomonadaceae. J. Bacteriol. 144 (1980) 247-257. [PMID: 7419490]
3. Byng, G., Whitaker, R., Flick, C. and Jensen, R.A. Enzymology of L-tyrosine biosynthesis in corn (Zea mays). Phytochemistry 20 (1981) 1289-1292.
4. Mayer, E., Waldner-Sander, S., Keller, B., Keller, E. and Lingens, F. Purification of arogenate dehydrogenase from Phenylobacterium immobile. FEBS Lett. 179 (1985) 208-212. [PMID: 3967752]
5. Lingens, F., Keller, E. and Keller, B. Arogenate dehydrogenase from Phenylobacterium immobile. Methods Enzymol. 142 (1987) 513-518.
6. Zamir, L.O., Tiberio, R., Devor, K.A., Sauriol, F., Ahmad, S. and Jensen, R.A. Structure of D-prephenyllactate. A carboxycyclohexadienyl metabolite from Neurospora crassa. J. Biol. Chem. 263 (1988) 17284-17290. [PMID: 2972718]
Accepted name: trans-2-enoyl-CoA reductase (NAD+)
Reaction: acyl-CoA + NAD+ = trans-didehydroacyl-CoA + NADH + H+
Other name(s): trans-2-enoyl-CoA reductase (NAD)
Systematic name: acyl-CoA:NAD+ trans-2-oxidoreductase
Comments: The enzyme from Euglena gracilis acts on crotonoyl-CoA and, more slowly, on trans-hex-2-enoyl-CoA and trans-oct-2-enoyl-CoA.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 77649-64-0
References:
1. Inui, H., Miyatake, K., Nakano, Y. and Kitaoka, S. Purification and some properties of short chain-length specific trans-2-enoyl-CoA reductase in mitochondria of Euglena gracilis. J. Biochem. (Tokyo) 100 (1986) 995-1000. [PMID: 3102464]
Accepted name: 2'-hydroxyisoflavone reductase
Reaction: vestitone + NADP+ = 2'-hydroxyformononetin + NADPH + H+
For diagram click here.
Other name(s): NADPH:2'-hydroxyisoflavone oxidoreductase; isoflavone reductase; 2',7-dihydroxy-4',5'-methylenedioxyisoflavone reductase
Systematic name: vestitone:NADP+ oxidoreductase
Comments: In the reverse reaction, a 2'-hydroxyisoflavone is reduced to an isoflavanone; 2'-hydroxypseudobaptigenin also acts. Involved in the biosynthesis of the pterocarpin phytoalexins medicarpin and maackiain.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 128449-69-4
References:
1. Tiemann, K., Hinderer, W. and Barz, W. Isolation of NADPH:isoflavone oxidoreductase, a new enzyme of pterocarpan biosynthesis in cell suspensions of Cicer arietinum. FEBS Lett. 213 (1987) 324-328.
Accepted name: biochanin-A reductase
Reaction: dihydrobiochanin A + NADP+ = biochanin A + NADPH + H+
For diagram click here.
Systematic name: dihydrobiochanin-A:NADP+ Δ2-oxidoreductase
Comments: Some other isoflavones are reduced to the corresponding isoflavanones.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 112198-90-0
References:
1. Tiemann, K., Hinderer, W. and Barz, W. Isolation of NADPH-isoflavone oxidoreductase, a new enzyme of pterocarpan phytoalexin biosynthesis in cell-suspension cultures of Cicer arietinum. FEBS Lett. 213 (1987) 324-328.
Accepted name: α-santonin 1,2-reductase
Reaction: 1,2-dihydrosantonin + NAD(P)+ = α-santonin + NAD(P)H + H+
Systematic name: 1,2-dihydrosantonin:NAD(P)+ 1,2-oxidoreductase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 111070-23-6
References:
1. Naik, U. and Mavuinkurve, S. α-Santonin 1,2-reductase and its role in the formation of dihydrosantonin and lumisantonin by Pseudomonas cichorii S. Can. J. Microbiol. 33 (1987) 658-662. [PMID: 3690421]
Accepted name: 13,14-dehydro-15-oxoprostaglandin 13-reductase
Reaction: 11α-hydroxy-9,15-dioxoprostanoate + NAD(P)+ = (13E)-11α-hydroxy-9,15-dioxoprost-13-enoate + NAD(P)H + H+
Other name(s): 15-oxo-Δ13-prostaglandin reductase; Δ13-15-ketoprostaglandin reductase; 15-ketoprostaglandin Δ13-reductase; prostaglandin Δ13-reductase; prostaglandin 13-reductase; (5Z)-(15S)-11α-hydroxy-9,15-dioxoprostanoate:NAD(P)+ Δ13-oxidoreductase; (5Z)-11α-hydroxy-9,15-dioxoprost-5-enoate:NAD(P)+ Δ13-oxidoreductase
Systematic name: 11α-hydroxy-9,15-dioxoprostanoate:NAD(P)+ Δ13-oxidoreductase
Comments: Reduces 13,14-dehydro-15-oxoprostaglandins to 13,14-dihydro derivatives. The enzyme from placenta is specific for NAD+.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 57406-74-3
References:
1. Hansen, H.S. Purification and assay of 15-ketoprostaglandin Δ13-reductase from bovine lung. Methods Enzymol. 86 (1982) 156-163. [PMID: 6290839]
2. Jarabak, J. Isolation and properties of a 15-ketoprostaglandin Δ13-reductase from human placenta. Methods Enzymol. 86 (1982) 163-167. [PMID: 7132753]
Accepted name: cis-3,4-dihydrophenanthrene-3,4-diol dehydrogenase
Reaction: (+)-cis-3,4-dihydrophenanthrene-3,4-diol + NAD+ = phenanthrene-3,4-diol + NADH + H+
Systematic name: (+)-cis-3,4-dihydrophenanthrene-3,4-diol:NAD+ 3,4-oxidoreductase
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, KEGG, Metacyc, CAS registry number: 118390-61-7
References:
1. Nagao, K., Takizawa, N. and Kiyahara, H. Purification and properties of cis-phenanthrene dihydrodiol dehydrogenase in Alcaligenes faecalis AFK2. Agric. Biol. Chem. 52 (1988) 2621-2623.
[EC 1.3.1.50 Deleted entry: tetrahydroxynaphthalene reductase. Now EC 1.1.1.252 tetrahydroxynaphthalene reductase (EC 1.3.1.50 created 1992, deleted 1999)]