Roles of NADPH-P450 reductase and apo- and holo-cytochrome b5 on xenobiotic oxidations catalyzed by 12 recombinant human cytochrome P450s expressed in membranes of Escherichia coli.
作者： Hiroshi Yamazaki , Mami Nakamura , Tomoko Komatsu , Katsuhiro Ohyama , Naoya Hatanaka
关键词:
摘要: Drug oxidation activities of 12 recombinant human cytochrome P450s (P450) coexpressed with NADPH-P450 reductase (NPR) in bacterial membranes (P450/NPR membranes) were determined and compared those other systems liver microsomes. Addition exogenous membrane-bound NPR to the P450/NPR enhanced catalytic CYP2C8, CYP2C9, CYP2C19, CYP3A4, CYP3A5. Enhancement CYP1A1, CYP1A2, CYP1B1, CYP2A6, CYP2B6, CYP2D6, CYP2E1 was not observed after addition (4 molar excess each P450). Exogenous purified b5 (b5) further CYP2E1, CYP3A5/NPR membranes. Catalytic CYP2C9 CYP2C19 by reconstituted but Apo (devoid heme) when added both membrane systems, except for CYP2E1/NPR system containing NPR. fortified roughly similar measured microsomes insect cells coexpressing P450 (and b5) and/or microsomes, based on equivalent contents. These results suggest that interactions or mixed appear be different some CYP2 family enzymes, possibly due a conformational role b5. are useful models prediction rates microsomal P450-dependent drug oxidations.
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