57 varieties: the human cytochromes P450.
The human cytochrome P450 (CYP) complement of heme-thiolate enzymes is reviewed. Of the 57 individual P450s characterized in Homo sapiens thus far, it is apparent that approximately one-half are associated with the metabolism of drugs and other xenobiotics, whereas the other half have endogenous functions in steroid, prostanoid, eicosanoid and fatty acid metabolism. This review covers the extent of enzyme functionality for the known human P450s, focusing primarily on their role in the Phase I metabolism of foreign compounds, which involves the CYP1, CYP2 and CYP3 families.
Lewis
David F V
DF
School of Biomedical and Molecular Sciences, University of Surrey, UK. d.lewis@surrey.ac.uk
D003577:Cytochrome P-450 Enzyme System / Q000235:genetics* / Q000378:metabolism / Q000502:physiology; D006801:Humans; D007527:Isoenzymes / Q000235:genetics; D008958:Models, Molecular; D004364:Pharmaceutical Preparations / Q000378:metabolism; D015262:Xenobiotics / Q000378:metabolism
D007527:Isoenzymes; D004364:Pharmaceutical Preparations; D015262:Xenobiotics; D003577:Cytochrome P-450 Enzyme System