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.

SUBMITTER: Yamamoto K 

PROVIDER: S-EPMC7691559 | biostudies-literature | 2020 Nov

REPOSITORIES: biostudies-literature