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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

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Investigation of the active site of an unclassified glutathione transferase in <i>Bombyx mori</i> by alanine scanning.

Yamamoto Kohji K Yamaguchi Misuzu M Yamada Naotaka N

Journal of pesticide science 20201101 4

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 <i>Bombyx mori</i> (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 residue ...[more]

PMID: 33304193

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