title: Substrate specificity of human hepatic udp-glucuronosyltransferases.
abstract: Five human hepatic UDP-glucuronosyltransferases (UGTs) catalyze the facilitated excretion of more than 90% of drugs eliminated by glucuronidation. The substrate specificity of these UGTs has been examined using cloned expressed enzymes and liquid chromatography-mass spectrometry assays to determine the intrinsic clearance of drug glucuronidation in vitro. Specific substrates for the five individual UGTs have been identified. These five probe substrates could be used to predict the drug clearance catalyzed by individual UGTs in vivo.
authors.affiliation: Department of Molecular and Cellular Pathology, Ninewells Hospital and Medical School, University of Dundee, Scotland, United Kingdom.
authors.forename: Brian
authors.initials: B
authors.lastname: Burchell
authors.forename: David J
authors.initials: DJ
authors.lastname: Lockley
authors.forename: Adam
authors.initials: A
authors.lastname: Staines
authors.forename: Yoshihiro
authors.initials: Y
authors.lastname: Uesawa
authors.forename: Michael W H
authors.initials: MW
authors.lastname: Coughtrie
mesh_terms: D008401:Gas Chromatography-Mass Spectrometry; D020719:Glucuronides / Q000737:chemistry* / Q000378:metabolism; D014453:Glucuronosyltransferase / Q000737:chemistry* / Q000145:classification / Q000235:genetics; D006801:Humans; D008099:Liver / Q000201:enzymology*; D015394:Molecular Structure; D013379:Substrate Specificity
chemical_list: D020719:Glucuronides; D014453:Glucuronosyltransferase