ArticleScientific reports2018
Characterisation of a diazinon-metabolising glutathione S-transferase in the silkworm Bombyx mori by X-ray crystallography and genome editing analysis.
Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 15 citations in OpenAlex.
- Characterization of a glutamate-cysteine ligase in Bombyx mori.Molecular biology reports · 2023Article
- Role of Insect and Mammal Glutathione Transferases in Chemoperception.Biomolecules · 2023Review
- Structural and Functional Characterization of One Unclassified Glutathione S-Transferase in Xenobiotic Adaptation ofInternational journal of molecular sciences · 2021Article
- Investigation of the Substrate-Binding Site of a Prostaglandin E Synthase in Bombyx mori.The protein journal · 2021Article
- Investigation of the active site of an unclassified glutathione transferase inJournal of pesticide science · 2020Article
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Authors and funding
7 authors at 3 institutions in 1 country.
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Abstract
Previously, we found an unclassified glutathione S-transferase 2 (bmGSTu2) in the silkworm Bombyx mori that conjugates glutathione to 1-chloro-2,4-dinitrobenzene and also metabolises diazinon, an organophosphate insecticide. Here, we provide a structural and genome-editing characterisation of the diazinon-metabolising glutathione S-transferase in B. mori. The structure of bmGSTu2 was determined at 1.68 Å by X-ray crystallography. Mutation of putative amino acid residues in the substrate-binding site showed that Pro13, Tyr107, Ile118, Phe119, and Phe211 are crucial for enzymatic function. bmGSTu2 gene disruption resulted in a decrease in median lethal dose values to an organophosphate insecticide and a decrease in acetylcholine levels in silkworms. Taken together, these results indicate that bmGSTu2 could metabolise an organophosphate insecticide. Thus, this study provides insights into the physiological role of bmGSTu2 in silkworms, detoxification of organophosphate insecticides, and drug targets for the development of a novel insecticide.
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