Steroid 17alpha-monooxygenase
| steroid 17-alpha-monooxygenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 1.14.99.9 | ||||||||
| CAS number | 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 / EGO | ||||||||
| |||||||||
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
- ↑ Lynn, W.S.; Brown, R.H. (1958). "The conversion of progesterone to androgens by testes". J. Biol. Chem. 232 (2): 1015–1030. PMID 13549484.
- ↑ Yoshida, K.-I.; Oshima, H.; Troen, P. (1980). "Studies of the human testis. XIII. Properties of nicotinamide adenine dinucleotide (reduced form)-linked 17α-hydroxylation". J. Clin. Endocrinol. Metab. 50: 895–899. doi:10.1210/jcem-50-5-895. PMID 6966286.
External links
- Steroid 17alpha-monooxygenase at the US National Library of Medicine Medical Subject Headings (MeSH)