The Enzyme Database

Your query returned 11 entries.    printer_iconPrintable version



EC 1.3.1.2     
Accepted name: dihydropyrimidine dehydrogenase (NADP+)
Reaction: 5,6-dihydrouracil + NADP+ = uracil + NADPH + H+
For diagram of pyrimidine catabolism, click here
Other name(s): dihydrothymine dehydrogenase; dihydrouracil dehydrogenase (NADP+); 4,5-dihydrothymine: oxidoreductase; DPD; DHPDH; dehydrogenase, dihydrouracil (nicotinamide adenine dinucleotide phosphate); 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. [PMID: 13825299]
2.  Shiotani, T. and Weber, G. Purification and properties of dihydrothymine dehydrogenase from rat liver. J. Biol. Chem. 256 (1981) 219–224. [PMID: 7451435]
[EC 1.3.1.2 created 1961, modified 1986]
 
 
EC 1.3.1.20     
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. [DOI] [PMID: 13651190]
[EC 1.3.1.20 created 1972]
 
 
EC 1.3.1.21     
Accepted name: 7-dehydrocholesterol reductase
Reaction: cholesterol + NADP+ = cholesta-5,7-dien-3β-ol + NADPH + H+
For diagram of sterol ring b, c, D modification, click here
Other name(s): 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 pathway.
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. [DOI] [PMID: 9465114]
[EC 1.3.1.21 created 1972, modified 2013]
 
 
EC 1.3.1.22     
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, 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. [DOI] [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. [DOI] [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. [DOI] [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. [DOI] [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. [DOI] [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. [DOI] [PMID: 15993049]
[EC 1.3.1.22 created 1972, modified 2012]
 
 
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]
 
 
EC 1.3.1.24     
Accepted name: biliverdin reductase
Reaction: bilirubin + NAD(P)+ = biliverdin + NAD(P)H + H+
For diagram of biliverdin metabolism, 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]
[EC 1.3.1.24 created 1972]
 
 
EC 1.3.1.25     
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 of benzoate metabolism, 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; (1R,6R)-1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate:NAD+ oxidoreductase (decarboxylating)
Systematic name: (1R,6S)-1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate:NAD+ oxidoreductase (decarboxylating)
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, UM-BBD, 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., Hartnett, C., Ornston, L.N., 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. [DOI] [PMID: 1740120]
[EC 1.3.1.25 created 1976, modified 2004 (EC 1.3.1.55 created 1999, incorporated 2004)]
 
 
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]
 
 
EC 1.3.1.27     
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]
[EC 1.3.1.27 created 1976]
 
 
EC 1.3.1.28     
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 shikimate and chorismate biosynthesis, 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
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. [DOI] [PMID: 4306838]
[EC 1.3.1.28 created 1972 as EC 1.1.1.109, transferred 1976 to EC 1.3.1.28]
 
 
EC 1.3.1.29     
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 naphthalene metabolism, 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, EXPASY, KEGG, MetaCyc, UM-BBD, 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 1.3.1.29 created 1976]
 
 


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