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• W2398530554 endingPage "338" @default.
• W2398530554 startingPage "301" @default.
• W2398530554 abstract "Glucuronidation, catalyzed by uridine diphosphate glucuronosyltransferases (UGTs), is an important process for the metabolism and clearance of many lipophilic chemicals, including drugs, environmental chemicals, and endogenous compounds. Glucuronidation is a bisubstrate reaction that requires the aglycone and the cofactor, UDP-GlcUA. Accumulating evidence suggests that the bisubstrate reaction follows a compulsory-order ternary mechanism. To simplify the kinetic modeling of glucuronidation reactions in vitro, UDP-GlcUA is usually added to incubations in large excess. Many factors have been shown to influence UGT activity and kinetics in vitro, and these must be accounted for during experimental design and data interpretation. While the assessment of drug–drug interactions resulting from UGT inhibition has been challenging in the past, the increasing availability of UGT enzyme-selective substrate and inhibitor “probes” provides the prospect for more reliable reaction phenotyping and assessment of drug–drug interaction potential. Although extrapolation of the in vitro intrinsic clearance of a glucuronidated drug often underpredicts in vivo clearance, careful selection of in vitro experimental conditions and inclusion of extrahepatic glucuronidation may improve the predictivity of in vitro–in vivo extrapolation. Physiologically based pharmacokinetic (PBPK) modeling has also shown to be of value for predicting PK of drugs eliminated by glucuronidation." @default.
• W2398530554 created "2016-06-24" @default.
• W2398530554 creator A5008901409 @default.
• W2398530554 creator A5013378515 @default.
• W2398530554 creator A5033218102 @default.
• W2398530554 date "2021-01-01" @default.
• W2398530554 modified "2023-10-09" @default.
• W2398530554 title "Enzyme Kinetics of Uridine Diphosphate Glucuronosyltransferases (UGTs)" @default.
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