ExplorEnz: EC 1.14.14.23

Your query returned 1 entry. Printable version

1.14.14.23

Accepted name:

cholesterol 7α-monooxygenase

Reaction:

cholesterol + [reduced NADPH—hemoprotein reductase] + O₂ = 7α-hydroxycholesterol + [oxidized NADPH—hemoprotein reductase] + H₂O

For diagram of cholesterol catabolism (rings A, B and C), click here

Other name(s):

cholesterol 7α-hydroxylase; CYP7A1 (gene name)

Systematic name:

cholesterol,NADPH—hemoprotein reductase:oxygen oxidoreductase (7α-hydroxylating)

Comments:

A P-450 heme-thiolate liver protein that catalyses the first step in the biosynthesis of bile acids. The direct electron donor to the enzyme is EC 1.6.2.4, NADPH—hemoprotein reductase.

Links to other databases:

BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 9037-53-0

References:

1.	Mitton, J.R., Scholan, N.A. and Boyd, G.S. The oxidation of cholesterol in rat liver sub-cellular particles. The cholesterol-7α-hydroxylase enzyme system. Eur. J. Biochem. 20 (1971) 569–579. [DOI] [PMID: 4397276]
2.	Boyd, G.S., Grimwade, A.M. and Lawson, M.E. Studies on rat-liver microsomal cholesterol 7α-hydroxylase. Eur. J. Biochem. 37 (1973) 334–340. [DOI] [PMID: 4147676]
3.	Ogishima, T., Deguchi, S. and Okuda, K. Purification and characterization of cholesterol 7α-hydroxylase from rat liver microsomes. J. Biol. Chem. 262 (1987) 7646–7650. [PMID: 3584134]
4.	Nguyen, L.B., Shefer, S., Salen, G., Ness, G., Tanaka, R.D., Packin, V., Thomas, P., Shore, V. and Batta, A. Purification of cholesterol 7 α-hydroxylase from human and rat liver and production of inhibiting polyclonal antibodies. J. Biol. Chem. 265 (1990) 4541–4546. [PMID: 2106520]
5.	Nguyen, L.B., Shefer, S., Salen, G., Chiang, J.Y. and Patel, M. Cholesterol 7α-hydroxylase activities from human and rat liver are modulated in vitro posttranslationally by phosphorylation/dephosphorylation. Hepatology 24 (1996) 1468–1474. [DOI] [PMID: 8938182]

[EC 1.14.14.23 created 1976 as EC 1.14.13.17, transferred 2016 to EC 1.14.14.23]