5beta-cholestane-3alpha,7alpha-diol 12alpha-hydroxylase
| 5beta-cholestane-3alpha,7alpha-diol 12alpha-hydroxylase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.14.13.96 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
In enzymology, a 5beta-cholestane-3alpha,7alpha-diol 12alpha-hydroxylase (EC 1.14.13.96) is an enzyme that catalyzes the chemical reaction
- 5beta-cholestane-3alpha,7alpha-diol + NADPH + H+ + O2 5beta-cholestane-3alpha,7alpha,12alpha-triol + NADP+ + H2O
The 4 substrates of this enzyme are 5beta-cholestane-3alpha,7alpha-diol, NADPH, H+, and O2, whereas its 3 products are 5beta-cholestane-3alpha,7alpha,12alpha-triol, NADP+, and H2O.
Nomenclature
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 5beta-cholestane-3alpha,7alpha-diol,NADPH:oxygen oxidoreductase (12alpha-hydroxylating). Other names in common use include 5beta-cholestane-3alpha,7alpha-diol 12alpha-monooxygenase, sterol 12alpha-hydroxylase (ambiguous), CYP8B1, and cytochrome P450 8B1.
References
Further reading
- Hansson R, Wikvall K (July 1982). "Hydroxylations in biosynthesis of bile acids. Cytochrome P-450 LM4 and 12alpha-hydroxylation of 5beta-cholestane-3alpha, 7alpha-diol". European Journal of Biochemistry. 125 (2): 423–9. doi:10.1111/j.1432-1033.1982.tb06700.x. PMID 6811268.
- Hansson R, Wikvall K (February 1980). "Hydroxylations in biosynthesis and metabolism of bile acids. Catalytic properties of different forms of cytochrome P-450". The Journal of Biological Chemistry. 255 (4): 1643–9. PMID 6766451.
- Lundell K, Wikvall K (November 2003). "Gene structure of pig sterol 12alpha-hydroxylase (CYP8B1) and expression in fetal liver: comparison with expression of taurochenodeoxycholic acid 6alpha-hydroxylase (CYP4A21)". Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids. 1634 (3): 86–96. doi:10.1016/j.bbalip.2003.09.002. PMID 14643796.
- Lukacin R, Matern U, Junghanns KT, Heskamp ML, Britsch L, Forkmann G, Martens S (September 2001). "Purification and antigenicity of flavone synthase I from irradiated parsley cells". Archives of Biochemistry and Biophysics. 393 (1): 177–83. doi:10.1006/abbi.2001.2491. PMID 11516175.
- Yang Y, Zhang M, Eggertsen G, Chiang JY (June 2002). "On the mechanism of bile acid inhibition of rat sterol 12alpha-hydroxylase gene (CYP8B1) transcription: roles of alpha-fetoprotein transcription factor and hepatocyte nuclear factor 4alpha". Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids. 1583 (1): 63–73. doi:10.1016/s1388-1981(02)00186-5. PMID 12069850.
- Russell DW (2003). "The enzymes, regulation, and genetics of bile acid synthesis". Annual Review of Biochemistry. 72 (1): 137–74. doi:10.1146/annurev.biochem.72.121801.161712. PMID 12543708.
