Biology:5beta-cholestane-3alpha,7alpha-diol 12alpha-hydroxylase
| 5beta-cholestane-3alpha,7alpha-diol 12alpha-hydroxylase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 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 | ||||||||
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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 [math]\displaystyle{ \rightleftharpoons }[/math] 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
- "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. July 1982. doi:10.1111/j.1432-1033.1982.tb06700.x. PMID 6811268.
- "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. February 1980. PMID 6766451.
- "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. November 2003. doi:10.1016/j.bbalip.2003.09.002. PMID 14643796.
- "Purification and antigenicity of flavone synthase I from irradiated parsley cells". Archives of Biochemistry and Biophysics 393 (1): 177–83. September 2001. doi:10.1006/abbi.2001.2491. PMID 11516175.
- "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. June 2002. doi:10.1016/s1388-1981(02)00186-5. PMID 12069850.
- "The enzymes, regulation, and genetics of bile acid synthesis". Annual Review of Biochemistry 72 (1): 137–74. 2003. doi:10.1146/annurev.biochem.72.121801.161712. PMID 12543708.
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