The Enzyme Database

Your query returned 12 entries.    printer_iconPrintable version



EC 1.1.1.51     
Accepted name: 3(or 17)β-hydroxysteroid dehydrogenase
Reaction: testosterone + NAD(P)+ = androstenedione + NAD(P)H + H+
Glossary: androstenedione = androst-4-ene-3,17-dione
Other name(s): β-hydroxy steroid dehydrogenase; 17-ketoreductase; 17β-hydroxy steroid dehydrogenase; 3β-hydroxysteroid dehydrogenase; 3β-hydroxy steroid dehydrogenase
Systematic name: 3(or 17)β-hydroxysteroid:NAD(P)+ oxidoreductase
Comments: Also acts on other 3β- or 17β-hydroxysteroids. cf. EC 1.1.1.209 3(or 17)α-hydroxysteroid dehydrogenase.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, UM-BBD, CAS registry number: 9015-81-0
References:
1.  Dahm, K. and Breuer, H. Anreicherung einer 17β-hydroxysteroid:NAD(P)-oxydoreduktase aus der Nebenniere der Ratte. Hoppe-Seyler's Z. Physiol. Chem. 336 (1964) 63–68. [PMID: 14214322]
2.  Lynn, W.S. and Brown, R.H. The conversion of progesterone to androgens by testes. J. Biol. Chem. 232 (1958) 1015–1030. [PMID: 13549484]
3.  Marcus, P.I. and Talalay, P. Induction and purification of α- and β-hydroxysteroid dehydrogenases. J. Biol. Chem. 218 (1956) 661–674. [PMID: 13295221]
4.  Schultz, R.M., Groman, F.V. and Engel, L.L. 3(17)β-Hydroxysteroid dehydrogenase of Pseudomonas testosteroni. A convenient purification and demonstration of multiple molecular forms. J. Biol. Chem. 252 (1977) 3775–3783. [PMID: 193845]
5.  Talalay, P. and Dobson, M.M. Purification and properties of a α-hydroxysteroid dehydrogenase. J. Biol. Chem. 205 (1953) 823–837. [PMID: 13129261]
[EC 1.1.1.51 created 1961]
 
 
EC 1.1.1.63      
Transferred entry: testosterone 17β-dehydrogenase. Now EC 1.1.1.239, 3α(17β)-hydroxysteroid dehydrogenase (NAD+)
[EC 1.1.1.63 created 1965, deleted 2012]
 
 
EC 1.1.1.64     
Accepted name: testosterone 17β-dehydrogenase (NADP+)
Reaction: testosterone + NADP+ = androstenedione + NADPH + H+
Glossary: androstenedione = androst-4-ene-3,17-dione
Other name(s): 17-ketoreductase; NADP-dependent testosterone-17β-oxidoreductase; testosterone 17β-dehydrogenase (NADP)
Systematic name: 17β-hydroxysteroid:NADP+ 17-oxidoreductase
Comments: Also oxidizes 3-hydroxyhexobarbital to 3-oxohexobarbital.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9028-63-1
References:
1.  Endahl, G.L., Kochakia, C.D. and Hamm, D. Separation of a triphosphopyridine nucleotide-specific from a diphosphopyridine-specific 17β-hydroxy (testosterone) dehydrogenase of guinea pig liver. J. Biol. Chem. 235 (1960) 2792–2796. [PMID: 13696735]
2.  Sweat, M.L., Samuels, L.T. and Lumry, R. Preparation and characterisation of the enzyme which converts testosterone to androstendione. J. Biol. Chem. 185 (1950) 75–84. [PMID: 15436478]
3.  Villee, C.A. and Spencer, J.M. Some properties of the pyridine nucleotide-specific 17β-hydroxy steroid dehydrogenase of guinea pig liver. J. Biol. Chem. 235 (1960) 3615–3619. [PMID: 13781425]
[EC 1.1.1.64 created 1965]
 
 
EC 1.1.1.239     
Accepted name: 3α(17β)-hydroxysteroid dehydrogenase (NAD+)
Reaction: testosterone + NAD+ = androstenedione + NADH + H+
Glossary: androstenedione = androst-4-ene-3,17-dione
Other name(s): 3α,17β-hydroxy steroid dehydrogenase; 3α(17β)-HSD; 17-ketoreductase (ambiguous); 17β-HSD (ambiguous); HSD17B6 (gene name); HSD17B8 (gene name)
Systematic name: 3α(or 17β)-hydroxysteroid:NAD+ oxidoreductase
Comments: Also acts on other 17β-hydroxysteroids and on the 3α-hydroxy group of pregnanes and bile acids. Different from EC 1.1.1.50 3α-hydroxysteroid dehydrogenase (Si-specific) or EC 1.1.1.213 3α-hydroxysteroid dehydrogenase (Re-specific).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 126469-82-7
References:
1.  Sweat, M.L., Samuels, L.T. and Lumry, R. Preparation and characterisation of the enzyme which converts testosterone to androstendione. J. Biol. Chem. 185 (1950) 75–84. [PMID: 15436478]
2.  Villee, C.A. and Spencer, J.M. Some properties of the pyridine nucleotide-specific 17β-hydroxy steroid dehydrogenase of guinea pig liver. J. Biol. Chem. 235 (1960) 3615–3619. [PMID: 13781425]
3.  Endahl, G.L., Kochakia, C.D. and Hamm, D. Separation of a triphosphopyridine nucleotide-specific from a diphosphopyridine-specific 17β-hydroxy (testosterone) dehydrogenase of guinea pig liver. J. Biol. Chem. 235 (1960) 2792–2796. [PMID: 13696735]
4.  Ohmura, M., Hara, A., Nakagawa, M. and Sawada, H. Demonstration of 3α(17β)-hydroxysteroid dehydrogenase distinct from 3α-hydroxysteroid dehydrogenase in hamster liver. Biochem. J. 266 (1990) 583–589. [PMID: 2317205]
[EC 1.1.1.239 created 1992, modified 2012 (EC 1.1.1.63 created 1965, incorporated 2012)]
 
 
EC 1.3.1.3     
Accepted name: Δ4-3-oxosteroid 5β-reductase
Reaction: (1) 5β-cholestan-3-one + NADP+ = cholest-4-en-3-one + NADPH + H+
(2) 17,21-dihydroxy-5β-pregnane-3,11,20-trione + NADP+ = cortisone + NADPH + H+
For diagram of cholesterol catabolism (rings A, B and C), click here
Glossary: cortisone = 17,21-dihydroxypregn-4-ene-3,11,20-trione
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
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. 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. [DOI] [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. [DOI] [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 1.3.1.3 created 1961 (EC 1.3.1.23 created 1972, incorporated 2005), modified 2005]
 
 
EC 1.14.13.54     
Accepted name: ketosteroid monooxygenase
Reaction: a ketosteroid + NADPH + H+ + O2 = a steroid ester/lactone + NADP+ + H2O (general reaction)
(1) progesterone + NADPH + H+ + O2 = testosterone acetate + NADP+ + H2O
(2) androstenedione + NADPH + H+ + O2 = testololactone + NADP+ + H2O
(3) 17α-hydroxyprogesterone + NADPH + H+ + O2 = androstenedione + acetate + NADP+ + H2O
Glossary: progesterone = pregn-4-ene-3,20-dione
testosterone acetate = 3-oxoandrost-4-en-17β-yl acetate
androstenedione = androst-4-ene-3,17-dione
testololactone = 3-oxo-13,17-secoandrost-4-eno-17,13α-lactone
17α-hydroxyprogesterone = 17α-hydroxypregn-4-ene-3,20-dione
Other name(s): steroid-ketone monooxygenase; progesterone, NADPH2:oxygen oxidoreductase (20-hydroxylating, ester-producing); 17α-hydroxyprogesterone, NADPH2:oxygen oxidoreductase (20-hydroxylating, side-chain cleaving); androstenedione, NADPH2:oxygen oxidoreductase (17-hydroxylating, lactonizing)
Systematic name: ketosteroid,NADPH:oxygen oxidoreductase (20-hydroxylating, ester-producing/20-hydroxylating, side-chain cleaving/17-hydroxylating, lactonizing)
Comments: A single FAD-containing enzyme catalyses three types of monooxygenase (Baeyer-Villiger oxidation) reaction. The oxidative esterification of a number of derivatives of progesterone to produce the corresponding 17α-hydroxysteroid 17-acetate ester, such as testosterone acetate, is shown in Reaction (1). The oxidative lactonization of a number of derivatives of androstenedione to produce the 13,17-secoandrosteno-17,13α-lactone, such as testololactone, is shown in Reaction (2). The oxidative cleavage of the 17β-side-chain of 17α-hydroxyprogesterone to produce androstenedione and acetate is shown in Reaction (3). Reaction (1) is also catalysed by EC 1.14.99.4 (progesterone monooxygenase), and Reactions (2) and (3) correspond to that catalysed by EC 1.14.99.12 (androst-4-ene-3,17-dione monooxygenase). The possibility that a single enzyme is responsible for the reactions ascribed to EC 1.14.99.4 and EC 1.14.99.12 in other tissues cannot be excluded.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9044-53-5
References:
1.  Katagiri, M. and Itagaki, E. A steroid ketone monooxygenase from Cylindrocarpon radicicola. In: Müller, F. (Ed.), Chemistry and Biochemistry of Flavoenzymes, CRC Press, Florida, 1991, pp. 102–108.
2.  Itagaki, E. Studies on a steroid monooxygenase from Cylindrocarpon radicicola ATCC 11011. Purification and characterization. J. Biochem. (Tokyo) 99 (1986) 815–824. [PMID: 3486863]
3.  Itagaki, E. Studies on a steroid monooxygenase from Cylindrocarpon radicicola ATCC11011. Oxygenative lactonization of androstenedione to testololactone. J. Biochem. (Tokyo) 99 (1986) 825–832. [PMID: 3486864]
[EC 1.14.13.54 created 1999]
 
 
EC 1.14.14.19     
Accepted name: steroid 17α-monooxygenase
Reaction: a C21-steroid + [reduced NADPH—hemoprotein reductase] + O2 = a 17α-hydroxy-C21-steroid + [oxidized NADPH—hemoprotein reductase] + H2O
Other name(s): steroid 17α-hydroxylase; cytochrome P-450 17α; cytochrome P-450 (P-450 17α,lyase); 17α-hydroxylase-C17,20 lyase; CYP17; CYP17A1 (gene name)
Systematic name: steroid,NADPH—hemoprotein reductase:oxygen oxidoreductase (17α-hydroxylating)
Comments: Requires NADPH and EC 1.6.2.4, NADPH—hemoprotein reductase. A microsomal hemeprotein that catalyses two independent reactions at the same active site - the 17α-hydroxylation of pregnenolone and progesterone, which is part of glucocorticoid hormones biosynthesis, and the conversion of the 17α-hydroxylated products via a 17,20-lyase reaction to form androstenedione and dehydroepiandrosterone, leading to sex hormone biosynthesis (EC 1.14.14.32, 17α-hydroxyprogesterone deacetylase). The ratio of the 17α-hydroxylase and 17,20-lyase activities is an important factor in determining the directions of steroid hormone biosynthesis towards biosynthesis of glucocorticoid or sex hormones.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9029-67-8
References:
1.  Lynn, W.S. and Brown, R.H. The conversion of progesterone to androgens by testes. J. Biol. Chem. 232 (1958) 1015–1030. [PMID: 13549484]
2.  Yoshida, K.-I., Oshima, H. and Troen, P. Studies of the human testis. XIII. Properties of nicotinamide adenine dinucleotide (reduced form)-linked 17α-hydroxylation. J. Clin. Endocrinol. Metab. 50 (1980) 895–899. [DOI] [PMID: 6966286]
3.  Gilep, A.A., Estabrook, R.W. and Usanov, S.A. Molecular cloning and heterologous expression in E. coli of cytochrome P45017α. Comparison of structural and functional properties of substrate-specific cytochromes P450 from different species. Biochemistry (Mosc.) 68 (2003) 86–98. [PMID: 12693981]
4.  Kolar, N.W., Swart, A.C., Mason, J.I. and Swart, P. Functional expression and characterisation of human cytochrome P45017α in Pichia pastoris. J. Biotechnol. 129 (2007) 635–644. [DOI] [PMID: 17386955]
5.  Pechurskaya, T.A., Lukashevich, O.P., Gilep, A.A. and Usanov, S.A. Engineering, expression, and purification of "soluble" human cytochrome P45017α and its functional characterization. Biochemistry (Mosc.) 73 (2008) 806–811. [PMID: 18707589]
[EC 1.14.14.19 created 1961 as EC 1.99.1.9, transferred 1965 to EC 1.14.1.7, transferred 1972 to EC 1.14.99.9, modified 2013, transferred 2015 to EC 1.14.14.19]
 
 
EC 1.14.14.32     
Accepted name: 17α-hydroxyprogesterone deacetylase
Reaction: (1) 17α-hydroxyprogesterone + [reduced NADPH—hemoprotein reductase] + O2 = androstenedione + acetate + [oxidized NADPH—hemoprotein reductase] + H2O
(2) 17α-hydroxypregnenolone + [reduced NADPH—hemoprotein reductase] + O2 = 3β-hydroxyandrost-5-en-17-one + acetate + [oxidized NADPH—hemoprotein reductase] + H2O
Glossary: androstenedione = androst-4-ene-3,17-dione
Other name(s): C-17/C-20 lyase; 17α-hydroxyprogesterone acetaldehyde-lyase; CYP17; CYP17A1 (gene name); 17α-hydroxyprogesterone 17,20-lyase
Systematic name: 17α-hydroxyprogesterone,NADPH—hemoprotein reductase:oxygen oxidoreductase (17α-hydroxylating, acetate-releasing)
Comments: A microsomal cytochrome P-450 (heme-thiolate) protein that catalyses two independent reactions at the same active site - the 17-hydroxylation of pregnenolone and progesterone, which is part of glucocorticoid hormones biosynthesis (EC 1.14.14.19), and the conversion of the 17-hydroxylated products via a 17,20-lyase reaction to form androstenedione and 3β-hydroxyandrost-5-en-17-one, leading to sex hormone biosynthesis. The activity of this reaction is dependent on the allosteric interaction of the enzyme with cytochrome b5 without any transfer of electrons from the cytochrome [2,4]. The enzymes from different organisms differ in their substrate specificity. While the enzymes from pig, hamster, and rat accept both 17α-hydroxyprogesterone and 17α-hydroxypregnenolone, the enzymes from human, bovine, sheep, goat, and bison do not accept the former, and the enzyme from guinea pig does not accept the latter [1].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 62213-24-5
References:
1.  Gilep, A.A., Estabrook, R.W. and Usanov, S.A. Molecular cloning and heterologous expression in E. coli of cytochrome P45017α. Comparison of structural and functional properties of substrate-specific cytochromes P450 from different species. Biochemistry (Mosc.) 68 (2003) 86–98. [PMID: 12693981]
2.  Auchus, R.J., Lee, T.C. and Miller, W.L. Cytochrome b5 augments the 17,20-lyase activity of human P450c17 without direct electron transfer. J. Biol. Chem. 273 (1998) 3158–3165. [DOI] [PMID: 9452426]
3.  Mak, P.J., Gregory, M.C., Denisov, I.G., Sligar, S.G. and Kincaid, J.R. Unveiling the crucial intermediates in androgen production. Proc. Natl. Acad. Sci. USA 112 (2015) 15856–15861. [DOI] [PMID: 26668369]
4.  Simonov, A.N., Holien, J.K., Yeung, J.C., Nguyen, A.D., Corbin, C.J., Zheng, J., Kuznetsov, V.L., Auchus, R.J., Conley, A.J., Bond, A.M., Parker, M.W., Rodgers, R.J. and Martin, L.L. Mechanistic scrutiny identifies a kinetic role for cytochrome b5 regulation of human cytochrome P450c17 (CYP17A1, P450 17A1). PLoS One 10:e0141252 (2015). [DOI] [PMID: 26587646]
5.  Bhatt, M.R., Khatri, Y., Rodgers, R.J. and Martin, L.L. Role of cytochrome b5 in the modulation of the enzymatic activities of cytochrome P450 17α-hydroxylase/17,20-lyase (P450 17A1). J. Steroid Biochem. Mol. Biol. (2016) . [DOI] [PMID: 26976652]
[EC 1.14.14.32 created 1976 as EC 4.1.2.30, transferred 2016 to EC 1.14.14.32]
 
 
EC 1.14.15.19     
Accepted name: C-19 steroid 1α-hydroxylase
Reaction: testosterone + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+ = 1α-hydroxytestosterone + H2O + 2 oxidized ferredoxin [iron-sulfur] cluster
Other name(s): CYP260A1
Systematic name: testosterone,reduced-ferredoxin:oxygen oxidoreductase (1α-hydroxylating)
Comments: The enzyme, characterized from the bacterium Sorangium cellulosum, is a class I cytochrome P-450, and uses ferredoxin as its electron donor [1]. It was shown to act on several C-19 steroid substrates, including testosterone, androstenedione, testosterone-acetate and 11-oxoandrostenedione [2].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Ewen, K.M., Hannemann, F., Khatri, Y., Perlova, O., Kappl, R., Krug, D., Huttermann, J., Muller, R. and Bernhardt, R. Genome mining in Sorangium cellulosum So ce56: identification and characterization of the homologous electron transfer proteins of a myxobacterial cytochrome P450. J. Biol. Chem. 284 (2009) 28590–28598. [DOI] [PMID: 19696019]
2.  Khatri, Y., Ringle, M., Lisurek, M., von Kries, J.P., Zapp, J. and Bernhardt, R. Substrate hunting for the myxobacterial CYP260A1 revealed new 1α-hydroxylated products from C-19 steroids. ChemBioChem 17 (2016) 90–101. [DOI] [PMID: 26478560]
[EC 1.14.15.19 created 2016]
 
 
EC 1.14.99.9      
Transferred entry: steroid 17α-monooxygenase, now classified as EC 1.14.14.19, steroid 17α-monooxygenase
[EC 1.14.99.9 created 1961 as EC 1.99.1.9, transferred 1965 to EC 1.14.1.7, transferred 1972 to EC 1.14.99.9, modified 2013, deleted 2015]
 
 
EC 1.14.99.12     
Accepted name: androst-4-ene-3,17-dione monooxygenase
Reaction: androstenedione + reduced acceptor + O2 = testololactone + acceptor + H2O
Glossary: androstenedione = androst-4-ene-3,17-dione
testololactone = 3-oxo-13,17-secoandrost-4-eno-17,13-lactone
Other name(s): androstene-3,17-dione hydroxylase; androst-4-ene-3,17-dione 17-oxidoreductase; androst-4-ene-3,17-dione hydroxylase; androstenedione monooxygenase; 4-androstene-3,17-dione monooxygenase
Systematic name: androst-4-ene-3,17-dione-hydrogen-donor:oxygen oxidoreductase (13-hydroxylating, lactonizing)
Comments: Has a wide specificity. A single enzyme from the ascomycete Neonectria radicicola (EC 1.14.13.54, ketosteroid monooxygenase) catalyses both this reaction and that catalysed by EC 1.14.99.4, progesterone monooxygenase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37256-74-9
References:
1.  Prairie, R.L. and Talalay, P. Enzymatic formation of testololactone. Biochemistry 2 (1963) 203–208. [PMID: 13985909]
[EC 1.14.99.12 created 1972, modified 1999]
 
 
EC 4.1.2.30      
Transferred entry: 17α-hydroxyprogesterone aldolase. Now EC 1.14.14.32, 17α-hydroxyprogesterone deacetylase
[EC 4.1.2.30 created 1976, deleted 2016]
 
 


Data © 2001–2022 IUBMB
Web site © 2005–2022 Andrew McDonald