In enzymology, a lithocholate 6beta-hydroxylase (EC 1.14.13.94) is an enzyme that catalyzes the chemical reaction
| Lithocholate 6beta-hydroxylase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.14.13.94 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
- lithocholate + NADPH + H+ + O2 6beta-hydroxylithocholate + NADP+ + H2O
The 4 substrates of this enzyme are lithocholate, NADPH, H+, and O2, whereas its 3 products are 6beta-hydroxylithocholate, NADP+, and H2O.
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 derived from O2 with NADH or NADPH as one donor, and incorporation of one atom o oxygen into the other donor. The systematic name of this enzyme class is lithocholate,NADPH:oxygen oxidoreductase (6beta-hydroxylating). Other names in common use include lithocholate 6beta-monooxygenase, CYP3A10, 6beta-hydroxylase, and cytochrome P450 3A10/lithocholic acid 6beta-hydroxylase.
References
edit- Teixeira J, Gil G (1991). "Cloning, expression, and regulation of lithocholic acid 6 beta-hydroxylase". J. Biol. Chem. 266 (31): 21030–6. PMID 1840595.
- Chang TK, Teixeira J, Gil G, Waxman DJ. "The lithocholic acid 6 beta-hydroxylase cytochrome P-450, CYP 3A10, is an active catalyst of steroid-hormone 6 beta-hydroxylation". Biochem. J. 291: 429–33. PMC 1132543. PMID 8484723.
- Subramanian A, Wang J, Gil G (1998). "STAT 5 and NF-Y are involved in expression and growth hormone-mediated sexually dimorphic regulation of cytochrome P450 3A10/lithocholic acid 6beta-hydroxylase". Nucleic Acids Res. 26 (9): 2173–8. doi:10.1093/nar/26.9.2173. PMC 147524. PMID 9547277.
- Russell DW (2003). "The enzymes, regulation, and genetics of bile acid synthesis". Annu. Rev. Biochem. 72 (1): 137–74. doi:10.1146/annurev.biochem.72.121801.161712. PMID 12543708.
