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

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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.

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

Document Type: Review Article

DOI: https://doi.org/10.2174/0929866033478654

Affiliations: Institute Of Molecular Biology And Genetics, Mahidol University Salaya Campus, Salaya, Nakhon Pathom 73170, Thailand.

Publication date: 2003-10-01

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  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.
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