Multiple roles of glutathione binding-site residues of glutathione s-transferase.
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.
Vararattanavech
Ardcharaporn
A
Institute Of Molecular Biology And Genetics, Mahidol University Salaya Campus, Salaya, Nakhon Pathom 73170, Thailand.
Ketterman
Albert J
AJ
D000818:Animals; D000852:Anopheles / Q000235:genetics; D001665:Binding Sites; D005978:Glutathione / Q000737:chemistry / Q000378:metabolism*; D005982:Glutathione Transferase / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D006639:Histidine / Q000737:chemistry / Q000378:metabolism; D007700:Kinetics; D007930:Leucine / Q000737:chemistry / Q000378:metabolism; D016297:Mutagenesis, Site-Directed; D011487:Protein Conformation; D013329:Structure-Activity Relationship; D013379:Substrate Specificity
D006639:Histidine; D005982:Glutathione Transferase; D005978:Glutathione; D007930:Leucine