Updated BioCyc iOS App now
available in iTunes store
Updated BioCyc iOS App now
available in iTunes store
Updated BioCyc iOS App now
available in iTunes store
Updated BioCyc iOS App now
available in iTunes store
Updated BioCyc iOS App now
available in iTunes store
twitter

MetaCyc Reaction: 1.14.99.9

Superclasses: Reactions Classified By Conversion TypeSimple ReactionsChemical Reactions
Reactions Classified By SubstrateSmall-Molecule Reactions

EC Number: 1.14.99.9

Enzymes and Genes:

Homo sapiens: steroid 17-alpha-hydroxylase/17,20 lyase: CYP17A1

Supersedes EC numbers: 1.99.1.9, 1.14.1.7

The direction shown, i.e. which substrates are on the left and right sides, is in accordance with the direction in which it was curated.

Mass balance status: Balanced.

Enzyme Commission Primary Name: steroid 17α-monooxygenase

Enzyme Commission Synonyms: steroid 17α-hydroxylase, cytochrome P-45017α, cytochrome P-450 (P-45017α,lyase), 17α-hydroxylase-C17,20 lyase, CYP17, CYP17A1 (gene name)

Taxonomic Range: Metazoa

Standard Gibbs Free Energy (ΔrG in kcal/mol): -33.78675Inferred by computational analysis [Latendresse13]

Enzyme Commission Summary:
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 4.1.2.30, 7α-hydroxyprogesterone aldolase). 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.

Citations: [Lynn58, Yoshida80, Gilep03, Kolar07, Pechurskaya08]

Gene-Reaction Schematic

Gene-Reaction Schematic

Unification Links: KEGG:R02131

Relationship Links: BRENDA:EC:1.14.99.9, ENZYME:EC:1.14.99.9, IUBMB-ExplorEnz:EC:1.14.99.9, UniProt:RELATED-TO:P05093, UniProt:RELATED-TO:P05185, UniProt:RELATED-TO:P11715, UniProt:RELATED-TO:P12394, UniProt:RELATED-TO:P19100, UniProt:RELATED-TO:P27786, UniProt:RELATED-TO:P30437, UniProt:RELATED-TO:Q64410, UniProt:RELATED-TO:Q92113


References

Gilep03: Gilep AA, Estabrook RW, Usanov SA (2003). "Molecular cloning and heterologous expression in E. coli of cytochrome P45017alpha. Comparison of structural and functional properties of substrate-specific cytochromes P450 from different species." Biochemistry (Mosc) 68(1);86-98. PMID: 12693981

Kolar07: Kolar NW, Swart AC, Mason JI, Swart P (2007). "Functional expression and characterisation of human cytochrome P45017alpha in Pichia pastoris." J Biotechnol 129(4);635-44. PMID: 17386955

Latendresse13: Latendresse M. (2013). "Computing Gibbs Free Energy of Compounds and Reactions in MetaCyc."

Lynn58: Lynn WS, Brown RH (1958). "The conversion of progesterone to androgens by testes." J Biol Chem 232(2);1015-30. PMID: 13549484

Pechurskaya08: Pechurskaya TA, Lukashevich OP, Gilep AA, Usanov SA (2008). "Engineering, expression, and purification of "soluble" human cytochrome P45017alpha and its functional characterization." Biochemistry (Mosc) 73(7);806-11. PMID: 18707589

Yoshida80: Yoshida KI, Oshima H, Troen P (1980). "Studies of the human testis. XIII. Properties of nicotinamide adenine dinucleotide (reduced form)-linked 17 alpha-hydroxylation." J Clin Endocrinol Metab 50(5);895-9. PMID: 6966286


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by SRI International Pathway Tools version 19.5 on Sat Apr 30, 2016, BIOCYC11A.