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

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  • Yamamoto Kohji
    Department of Bioscience and Biotechnology, Kyushu University Graduate School
  • Yamaguchi Misuzu
    Department of Bioscience and Biotechnology, Kyushu University Graduate School
  • Yamada Naotaka
    Department of Bioscience and Biotechnology, Kyushu University Graduate School

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

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<p>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.</p>

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