KEGG   ENZYME: 1.14.14.138
Entry
EC 1.14.14.138              Enzyme                                 

Name
lithocholate 6beta-hydroxylase;
lithocholate 6beta-monooxygenase;
CYP3A10;
6beta-hydroxylase;
cytochrome P450 3A10;
lithocholic acid 6beta-hydroxylase
Class
Oxidoreductases;
Acting on paired donors, with incorporation or reduction of molecular oxygen;
With reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen into the other donor
Sysname
lithocholate,[reduced NADPH---hemoprotein reductase]:oxygen oxidoreductase (6beta-hydroxylating)
Reaction(IUBMB)
lithocholate + [reduced NADPH---hemoprotein reductase] + O2 = 6beta-hydroxylithocholate + [oxidized NADPH---hemoprotein reductase] + H2O [RN:R07203]
Reaction(KEGG)
R07203
Substrate
lithocholate [CPD:C03990];
[reduced NADPH---hemoprotein reductase] [CPD:C03024];
O2 [CPD:C00007]
Product
6beta-hydroxylithocholate [CPD:C15515];
[oxidized NADPH---hemoprotein reductase] [CPD:C03161];
H2O [CPD:C00001]
Comment
A cytochrome P-450 (heme-thiolate) protein from Mesocricetus auratus (golden hamster). Expression of the gene for this enzyme is 50-fold higher in male compared to female hamsters [1].
History
EC 1.14.14.138 created 2005 as EC 1.14.13.94, transferred 2018 to EC 1.14.14.138
Reference
1  [PMID:1840595]
  Authors
Teixeira J, Gil G
  Title
Cloning, expression, and regulation of lithocholic acid 6 beta-hydroxylase.
  Journal
J Biol Chem 266:21030-6 (1991)
Reference
2  [PMID:8484723]
  Authors
Chang TK, Teixeira J, Gil G, Waxman DJ.
  Title
The lithocholic acid 6 beta-hydroxylase cytochrome P-450, CYP 3A10, is an active catalyst of steroid-hormone 6 beta-hydroxylation.
  Journal
Biochem J 291 ( Pt 2):429-33 (1993)
DOI:10.1042/bj2910429
Reference
3  [PMID:9547277]
  Authors
Subramanian A, Wang J, Gil G.
  Title
STAT 5 and NF-Y are involved in expression and growth hormone-mediated sexually dimorphic regulation of cytochrome P450 3A10/lithocholic acid 6beta-hydroxylase.
  Journal
Nucleic Acids Res 26:2173-8 (1998)
DOI:10.1093/nar/26.9.2173
Reference
4  [PMID:12543708]
  Authors
Russell DW
  Title
The enzymes, regulation, and genetics of bile acid synthesis.
  Journal
Annu Rev Biochem 72:137-74 (2003)
DOI:10.1146/annurev.biochem.72.121801.161712
Other DBs
ExplorEnz - The Enzyme Database: 1.14.14.138
IUBMB Enzyme Nomenclature: 1.14.14.138
ExPASy - ENZYME nomenclature database: 1.14.14.138
BRENDA, the Enzyme Database: 1.14.14.138
CAS: 9075-83-6

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