Inhibitory effects of UDP-glucuronosyltransferase (UGT) typical ligands against E. coli beta-glucuronidase (GUS).

ABSTRACT: UDP-glucuronosyltransferases (UGTs) and β-glucuronidase (GUS) catalyze entirely distinct metabolism reactions. UGTs are responsible for the glucuronidation of a variety of drugs, endogenous and environmental chemicals, whereas GUS hydrolyzes glucuronides and liberates the parent substrates. Information on the overlap of ligand selectivity between UGT and GUS is essential for exploring the pharmacological or toxicological effects of the inhibitors of these two metabolic enzymes. This study is conducted to test whether UGTs and GUS share common ligands, by investigating the inhibitory effects towards E. coli GUS by a series of UGT typical substrates and inhibitors. Results showed that three typical ligands of UGTs, including two specific substrates (estradiol and trifluoperazine, E2 a

SUBMITTER: Xiao L 

PROVIDER: S-EPMC9054634 | biostudies-literature | 2020 Jun

REPOSITORIES: biostudies-literature