Multiple Roles Of Glutathione Binding-Site Residues Of Glutathione S-Transferase

Title: Multiple Roles Of Glutathione Binding-Site Residues Of Glutathione S-Transferase

Volume: 10 Issue: 5

Author(s): Ardcharaporn Vararattanavech and Albert J. Ketterman

Affiliation:

Keywords: active site, anopheles dirus, catalysis, glutathione transferase, mosquito, structure

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.

Cite this article as:

Vararattanavech Ardcharaporn and Ketterman J. Albert, Multiple Roles Of Glutathione Binding-Site Residues Of Glutathione S-Transferase, Protein & Peptide Letters 2003; 10 (5) . https://dx.doi.org/10.2174/0929866033478654

DOI https://dx.doi.org/10.2174/0929866033478654	Print ISSN 0929-8665
Publisher Name Bentham Science Publisher	Online ISSN 1875-5305