Structural characteristics of human P450s involved in drug metabolism: QSARs and lipophilicity profiles.
The factors with human P450 substrate selectivity are reviewed, together with extensive tabulation of quantitative relationships between structure and activity for many species of P450 substrates, inducers and inhibitors. In addition, the physicochemical characteristics (logP and pK(a) values) of heptic microsomal P450 substrates are collated, such that comparisons can be made on the grounds of compound lipophilicities.
Lewis
D F
DF
Molecular Toxicology Group, School of Biological Sciences, University of Surrey, Guildford, UK. d.lewis@surrey.ac.uk
D000818:Animals; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D003577:Cytochrome P-450 Enzyme System / Q000737:chemistry / Q000378:metabolism*; D006801:Humans; D007527:Isoenzymes / Q000737:chemistry / Q000378:metabolism; D008055:Lipids / Q000737:chemistry*; D004364:Pharmaceutical Preparations / Q000378:metabolism*; D013329:Structure-Activity Relationship
D007527:Isoenzymes; D008055:Lipids; D004364:Pharmaceutical Preparations; D003577:Cytochrome P-450 Enzyme System