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Updated: Aug 16, 2026

Formation of Covalent DNA Adducts by Enzymatically Activated Carcinogens and Drugs In Vitro and Their Determination by 32P-postlabeling
Published on: March 20, 2018
Structural diversity of human xenobiotic-metabolizing cytochrome P450 monooxygenases
Eric F Johnson1, C David Stout
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.
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