| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 2603956 | Toxicology in Vitro | 2006 | 9 Pages |
Abstract
The oxidative metabolism of coumarin via several human cytochrome P450 (CYP) enzymes from families CYP1, CYP2 and CYP3 is rationalized in terms of molecular modelling studies carried out on the key interactions with various amino acid residues in the relevant active sites. The findings from modelling by homology with the CYP2C5 crystallographic template are in agreement with the known metabolism of coumarin in human P450s from the CYP1, CYP2 and CYP3 families, which has been published recently, and with independently reported information from site-directed mutagenesis studies.
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Authors
David F.V. Lewis, Yuko Ito, Brian G. Lake,