Steroid 17alpha-monooxygenase
steroid 17-alpha-monooxygenase | |||||||||
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Identifiers | |||||||||
EC no. | 1.14.99.9 | ||||||||
CAS no. | 9029-67-8 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
Gene Ontology | AmiGO / QuickGO | ||||||||
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In enzymology, a steroid 17alpha-monooxygenase (EC 1.14.99.9) is an enzyme that catalyzes the chemical reaction
- a steroid + AH2 + O2 a 17alpha-hydroxysteroid + A + H2O
The 3 substrates of this enzyme are steroid, an electron acceptor AH2, and O2, whereas its 3 products are 17alpha-hydroxysteroid, the reduction product A, and H2O.[1][2]
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derive from O miscellaneous. The systematic name of this enzyme class is steroid,hydrogen-donor:oxygen oxidoreductase (17alpha-hydroxylating). Other names in common use include steroid 17alpha-hydroxylase, cytochrome P-45017alpha, cytochrome P-450 (P-45017alpha,lyase), and 17alpha-hydroxylase-C17,20 lyase. This enzyme participates in c21-steroid hormone metabolism. It has 3 cofactors: NADH, NADPH, and Heme.
References
[edit]- ^ Lynn WS, Brown RH (June 1958). "The conversion of progesterone to androgens by testes". The Journal of Biological Chemistry. 232 (2): 1015–30. PMID 13549484.
- ^ Yoshida KI, Oshima H, Troen P (May 1980). "Studies of the human testis. XIII. Properties of nicotinamide adenine dinucleotide (reduced form)-linked 17 alpha-hydroxylation". The Journal of Clinical Endocrinology and Metabolism. 50 (5): 895–9. doi:10.1210/jcem-50-5-895. PMID 6966286.
External links
[edit]- Steroid+17alpha-monooxygenase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)