Identification of a diazinon-metabolizing glutathione S-transferase in the silkworm, Bombyx mori

Research output: Contribution to journalArticlepeer-review

15 Citations (Scopus)

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.

Original languageEnglish
Article number30073
JournalScientific reports
Volume6
DOIs
Publication statusPublished - Jul 21 2016

All Science Journal Classification (ASJC) codes

  • General

Fingerprint Dive into the research topics of 'Identification of a diazinon-metabolizing glutathione S-transferase in the silkworm, Bombyx mori'. Together they form a unique fingerprint.

Cite this