Open AccessCytochrome P450 (version 2019.4) in the IUPHAR/BPS Guide to Pharmacology Database
Author(s) -
Kathryn Burns,
Nuala A. Helsby
Publication year - 2019
Publication title -
iuphar/bps guide to pharmacology cite
Language(s) - English
Resource type - Journals
ISSN - 2633-1020
DOI - 10.2218/gtopdb/f242/2019.4
Subject(s) - cytochrome p450 , enzyme , monooxygenase , pharmacology , drug metabolism , cytochrome , biochemistry , chemistry , biology , database , computer science
The cytochrome P450 enzyme family (CYP450), E.C. 1.14.-.-, were originally defined by their strong absorbance at 450 nm due to the reduced carbon monoxide-complexed haem component of the cytochromes. They are an extensive family of haem-containing monooxygenases with a huge range of both endogenous and exogenous substrates. These include sterols, fat-soluble vitamins, pesticides and carcinogens as well as drugs. The substrates of some orphan CYP are not known. Listed below are the human enzymes; their relationship with rodent CYP450 enzyme activities is obscure in that the species orthologue may not catalyse the metabolism of the same substrates. Although the majority of CYP450 enzyme activities are concentrated in the liver, the extrahepatic enzyme activities also contribute to patho/physiological processes. Genetic variation of CYP450 isoforms is widespread and likely underlies a significant proportion of the individual variation to drug administration.