Title : Cytochrome P450 specificity of metabolism and interactions of oxybutynin in human liver microsomes.

Pub. Date : 1998 Apr

PMID : 9584328






5 Functional Relationships(s)
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1 Recombinant CYP3A5 enzyme had higher activity in oxybutynin N-deethylation than recombinant CYP3A4. oxybutynin n cytochrome P450 family 3 subfamily A member 5 Homo sapiens
2 Ketoconazole inhibited oxybutynin N-deethylation by the recombinant CYP3A4 and CYP3A5 almost completely, whereas itraconazole inhibited the activity of CYP3A4 more potently than that of CYP3A5. Ketoconazole cytochrome P450 family 3 subfamily A member 5 Homo sapiens
3 Ketoconazole inhibited oxybutynin N-deethylation by the recombinant CYP3A4 and CYP3A5 almost completely, whereas itraconazole inhibited the activity of CYP3A4 more potently than that of CYP3A5. Ketoconazole cytochrome P450 family 3 subfamily A member 5 Homo sapiens
4 Ketoconazole inhibited oxybutynin N-deethylation by the recombinant CYP3A4 and CYP3A5 almost completely, whereas itraconazole inhibited the activity of CYP3A4 more potently than that of CYP3A5. oxybutynin cytochrome P450 family 3 subfamily A member 5 Homo sapiens
5 Although the reasons for the weak and variable inhibition by itraconazole remain to be studied, it seems that oxybutynin is predominantly metabolized by CYP3A4 and CYP3A5 but not by CYP2D6. oxybutynin cytochrome P450 family 3 subfamily A member 5 Homo sapiens