RRC ID 56901
Author Yamamoto K, Yamada N.
Title Identification of a diazinon-metabolizing glutathione S-transferase in the silkworm, Bombyx mori.
Journal Sci Rep
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.
Volume 6
Pages 30073
Published 2016-7-21
DOI 10.1038/srep30073
PII srep30073
PMID 27440377
PMC PMC4954967
MeSH Animals Binding Sites Biotransformation Bombyx / enzymology* DNA Mutational Analysis Diazinon / metabolism* Dinitrochlorobenzene / metabolism Gene Expression Profiling Glutathione / metabolism Glutathione Transferase / genetics Glutathione Transferase / metabolism* Insecticides / metabolism*
IF 4.011
Times Cited 15
Resource
Silkworms