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Updated: Aug 13, 2026

Spectrophotometric Screening for Potential Inhibitors of Cytosolic Glutathione S-Transferases
Published on: October 10, 2020
Activation of alkyl halides by glutathione transferases
1Department of Biochemistry and Center in Molecular Toxicology, Vanderbilt University School of Medicine, Nashville, Tennessee, USA.
Abstract:
Glutathione (GSH) transferases catalyze the conjugation of the tripeptide GSH with alkyl halides and related compounds. If a second leaving group is present, the substrate is at least a potential bis-electrophile and the initial conjugate may be susceptible to further attack by the sulfur atom. This process can yield potent electrophiles that modify DNA and are genotoxic. Much of the chemistry is understood in the context of the halide order and size of rings generated in reactive sulfonium ions. Similar chemistry has been demonstrated with the active site cysteine residue in the DNA repair protein O(6)-alkylguanine DNA-alkyltransferase.
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