Modelling Human Cytochrome P450-Substrate Interactions

  • D. F. V. Lewis
Part of the Ernst Schering Research Foundation Workshop book series (SCHERING FOUND, volume 37)


The cytochromes P450 (CYP) are extremely important and ubiquitous enzymes, being present in virtually all species studied to date and across the five biological kingdoms where they are associated with the phase I oxidative metabolism of a large number of structurally diverse chemicals, both exogenous and endogenous (Ortiz de Montellano 1995; Ioannides 1996; Lewis 1996, 2001; Rendic and DiCarlo 1997). Of the 1,200 or more P450s sequenced thus far, it has been established that a relatively small number (~10) of the human hepatic enzymes metabolize over 90% of the known drugs in current clinical use, with the CYP2C, CYP2D and CYP3A subfamilies constituting the major catalysts of drug metabolism in man (Rendic and DiCarlo 1997).


Lauric Acid Haem Iron Putative Active Site Active Site Amino Acid Residue Nicotinamide Adenine Dinu 
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© Springer-Verlag Berlin Heidelberg 2002

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  • D. F. V. Lewis

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