Title : Involvement of human cytochrome P450 2B6 in the omega- and 4-hydroxylation of the anesthetic agent propofol.

Pub. Date : 2007 Jul

PMID : 17620218






3 Functional Relationships(s)
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1 Of six cDNA-expressed human P450 enzymes tested, CYP2B6 and CYP1A2, followed by CYP3A4, had high catalytic activities at a 20 microM propofol concentration, corresponding to clinical plasma levels. Propofol cytochrome P450 family 3 subfamily A member 4 Homo sapiens
2 In a panel of individual human liver microsomes, propofol omega- and 4-hydroxylation activities (at the substrate concentration of 20 microM) were highly correlated with CYP2B6 contents, and moderately with CYP3A4 contents. Propofol cytochrome P450 family 3 subfamily A member 4 Homo sapiens
3 These results suggest that CYP2B6 has an important role in propofol omega- and 4-hydroxylation in human livers and that the hepatic contents of CYP2B6, CYP3A4, and CYP1A2 determine which P450 enzymes play major roles in propofol oxidation in individual humans. Propofol cytochrome P450 family 3 subfamily A member 4 Homo sapiens