Investigation of the active site of an unclassified glutathione transferase in Bombyx mori by alanine scanning

Abstract

Glutathione transferase (GST) is an important class of detoxification enzymes that are vital for defense against various xenobiotics and cellular oxidative stress. Previously, we had reported an unclassified glutathione transferase 2 in Bombyx mori (bmGSTu2) to be responsible for detoxifying diazinon. In this study, we aimed to identify the amino acid residues that constitute a hydrogen-bonding network important for GST activity. Site-directed mutagenesis of bmGSTu2 suggested that residues Asn102, Pro162, and Ser166 contribute to its catalytic activity.