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Updated: Aug 30, 2026

Spectrophotometric Screening for Potential Inhibitors of Cytosolic Glutathione S-Transferases
Published on: October 10, 2020
Multiple roles of glutathione binding-site residues of glutathione s-transferase
Ardcharaporn Vararattanavech1, Albert J Ketterman
1Institute Of Molecular Biology And Genetics, Mahidol University Salaya Campus, Salaya, Nakhon Pathom 73170, Thailand.
Abstract:
This study was designed to characterize residues in the glutathione binding site of AdGSTD4-4 from the mosquito malaria vector Anopheles dirus. The data revealed that Leu33, His38 and His50 each play a role in enzyme catalysis and glutathione binding. The mutants of these three residues also displayed differences in hydrophobic substrate specificity, suggesting that changes in the active site conformation occurred. Differences in conformations was also suggested by protein stability changes. These results indicate that residues in the glutathione binding site are not only important in the catalytic function but also play a role in the structural integrity of the enzyme.
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