Structure-activity relationship for human cytochrome P450 substrates and inhibitors.
Article Details
- CitationCopy to clipboard
Lewis DF, Modi S, Dickins M
Structure-activity relationship for human cytochrome P450 substrates and inhibitors.
Drug Metab Rev. 2002 Feb-May;34(1-2):69-82.
- PubMed ID
- 11996013 [ View in PubMed]
- Abstract
Criteria governing the avidity of substrate binding to human hepatic cytochromes P450 (CYP) associated with Phase 1 metabolism of drugs are described. The results of extensive quantitative structure-activity relationship (QSAR) analyses are reported for substrates of human P450s: CYPIA2, CYP2A6, CYP2B6, CYP2C9, CYP2C19, CYP2D6, CYP2E1, and CYP3A4, representing the enzymes exhibiting major involvement in the metabolism of drug substrates in Homo sapiens. In particular, it is shown that hydrogen bond properties in each class of enzyme-substrate complex are especially important factors in determining substrate binding affinity towards those human P450s which are involved in drug metabolism.
DrugBank Data that Cites this Article
- Drug Enzymes
Drug Enzyme Kind Organism Pharmacological Action Actions Bupropion Cytochrome P450 2B6 Protein Humans UnknownSubstrateDetails Desipramine Cytochrome P450 2D6 Protein Humans UnknownSubstrateInhibitorDetails Ethanol Cytochrome P450 2E1 Protein Humans UnknownSubstrateInducerDetails Hexobarbital Cytochrome P450 2C19 Protein Humans UnknownSubstrateDetails Mephenytoin Cytochrome P450 2B6 Protein Humans UnknownSubstrateDetails Propranolol Cytochrome P450 2D6 Protein Humans UnknownSubstrateInhibitorDetails