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• W2476302008 abstract "The glutathione S-transferase superfamily play key roles in the metabolism of numerous xenobiotics. We report herein the identification and characterization of a novel glutathione S-transferase in the silkworm, Bombyx mori. The enzyme (bmGSTu2) conjugates glutathione to 1-chloro-2,4-dinitrobenzene, as well as metabolizing diazinon, one of the organophosphate insecticides. Quantitative reverse transcription-polymerase chain reaction analysis of transcripts demonstrated that bmGSTu2 expression was induced 1.7-fold in a resistant strain of B. mori. Mutagenesis of putative amino acid residues in the glutathione-binding site revealed that Ile54, Glu66, Ser67, and Asn68 are crucial for enzymatic function. These results provide insights into the catalysis of glutathione conjugation in silkworm by bmGSTu2 and into the detoxification of organophosphate insecticides." @default.
• W2476302008 created "2016-08-23" @default.
• W2476302008 creator A5007687858 @default.
• W2476302008 creator A5015953030 @default.
• W2476302008 date "2016-07-21" @default.
• W2476302008 modified "2023-10-10" @default.
• W2476302008 title "Identification of a diazinon-metabolizing glutathione S-transferase in the silkworm, Bombyx mori" @default.
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• W2476302008 doi "https://doi.org/10.1038/srep30073" @default.
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