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• W2766465725 abstract "Glutathione S-transferases (GSTs) comprise a diverse family of phase II drug metabolizing enzymes whose shared function is the conjugation of reduced glutathione (GSH) to endo- and xenobiotics. Although the conglomerate activity of these enzymes can be measured, the isoform-specific contribution to the metabolism of xenobiotics in complex biological samples has not been possible. We have developed two activity-based probes (ABPs) that characterize active GSTs in mammalian tissues. The GST active site is composed of a GSH binding G site and a substrate binding H site. Therefore, we developed (1) a GSH-based photoaffinity probe (GSTABP-G) to target the G site, and (2) an ABP designed to mimic a substrate molecule and have H site activity (GSTABP-H). The GSTABP-G features a photoreactive moiety for UV-induced covalent binding to GSTs and GSH-binding enzymes. The GSTABP-H is a derivative of a known mechanism-based GST inhibitor that binds within the active site and inhibits GST activity. Validation of probe targets and G and H site specificity was carried out using a series of competition experiments in the liver. Herein, we present robust tools for the characterization of enzyme- and active site-specific GST activity in mammalian model systems." @default.
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• W2766465725 date "2017-11-01" @default.
• W2766465725 modified "2023-09-26" @default.
• W2766465725 title "Activity-Based Probes for Isoenzyme- and Site-Specific Functional Characterization of Glutathione <i>S</i>-Transferases" @default.
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• W2766465725 doi "https://doi.org/10.1021/jacs.7b07378" @default.
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