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Biochem Biophys Res Commun. 2005 Dec 9;338(1):331-6. Epub 2005 Sep 2.

Structural diversity of human xenobiotic-metabolizing cytochrome P450 monooxygenases.

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  • 1Department of Molecular and Experimental Medicine, The Scripps Research Institute, La Jolla, CA 92037, USA. johnson@scripps.edu

Abstract

Cytochrome P450 monooxygenases provide important pathways for the metabolic clearance of drugs and toxins in humans. These enzymes are expressed from multiple genes and exhibit complex patterns of differential and overlapping substrate selectivity. Recent structures of microsomal P450s determined by X-ray crystallography have provided a structural basis for understanding differences in substrate recognition. This review will describe similarities and differences in the active site structures of four human microsomal cytochrome P450 monooxygenases, 2A6, 2C8, 2C9, and 3A4, that contribute extensively to drug and toxin metabolism.

PMID:
16157296
[PubMed - indexed for MEDLINE]

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