Title : CYP3A5 Contributes significantly to CYP3A-mediated drug oxidations in liver microsomes from Japanese subjects.

Pub. Date : 2004 Apr

PMID : 15499178






3 Functional Relationships(s)
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1 In addition, the correlation coefficients of CYP3A5 contents with the rates of diltiazem N-demethylation, midazolam 1"-hydroxylation and testosterone 6beta- hydroxylation were higher than those of CYP3A4, although the value of CYP3A5 with the midazolam 4-hydroxylation rate was similar to that of CYP3A4. Diltiazem cytochrome P450 family 3 subfamily A member 5 Homo sapiens
2 The apparent V(max)/K(m) values for recombinant CYP3A5 indicated the greater contributions to diltiazem N-demethylation and midazolam 1"-hydroxylation as compared with CYP3A4. Diltiazem cytochrome P450 family 3 subfamily A member 5 Homo sapiens
3 These results suggest that polymorphic CYP3A5 contributes markedly to the drug oxidations, particularly diltiazem N-demethylation, midazolam 1"- hydroxylation and testosterone 6beta-hydroxylation by liver microsomes from Japanese subjects. Diltiazem cytochrome P450 family 3 subfamily A member 5 Homo sapiens