| EC |
1.14.18.8 |
| Accepted name: |
7α-hydroxycholest-4-en-3-one 12α-hydroxylase |
| Reaction: |
7α-hydroxycholest-4-en-3-one + 2 ferrocytochrome b5 + 2 H+ + O2 = 7α,12α-dihydroxycholest-4-en-3-one + 2 ferricytochrome b5 + + H2O |
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For diagram of cholesterol catabolism (rings A, B and C), click here |
| Other name(s): |
7α-hydroxy-4-cholesten-3-one 12α-monooxygenase; CYP12; sterol 12α-hydroxylase (ambiguous); HCO 12α-hydroxylase |
| Systematic name: |
7α-hydroxycholest-4-en-3-one,ferrocytochrome-b5:oxygen oxidoreductase (12α-hydroxylating) |
| Comments: |
A P-450 heme-thiolate protein. Requires EC 1.6.2.4, NADPH—hemoprotein reductase and cytochrome b5 for maximal activity. This enzyme is important in bile acid biosynthesis, being responsible for the balance between the formation of cholic acid and chenodeoxycholic acid [2]. |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
| References: |
| 1. |
Ishida, H., Noshiro, M., Okuda, K. and Coon, M.J. Purification and characterization of 7α-hydroxy-4-cholesten-3-one 12α-hydroxylase. J. Biol. Chem. 267 (1992) 21319–21323. [PMID: 1400444] |
| 2. |
Eggertsen, G., Olin, M., Andersson, U., Ishida, H., Kubota, S., Hellman, U., Okuda, K.I. and Björkhem, I. Molecular cloning and expression of rabbit sterol 12α-hydroxylase. J. Biol. Chem. 271 (1996) 32269–32275. [DOI] [PMID: 8943286] |
| 3. |
Russell, D.W. The enzymes, regulation, and genetics of bile acid synthesis. Annu. Rev. Biochem. 72 (2003) 137–174. [DOI] [PMID: 12543708] |
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| [EC 1.14.18.8 created 2005 as EC 1.14.13.95, transferred 2015 to EC 1.14.18.8] |
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