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Glutathione-binding site of a bombyx mori theta-class glutathione transferase.

Authors
  • Hossain, M D Tofazzal1
  • Yamada, Naotaka1
  • Yamamoto, Kohji1
  • 1 Faculty of Agriculture, Kyushu University Graduate School, Fukuoka, Japan. , (Japan)
Type
Published Article
Journal
PLoS ONE
Publisher
Public Library of Science
Publication Date
Jan 01, 2014
Volume
9
Issue
5
Identifiers
DOI: 10.1371/journal.pone.0097740
PMID: 24848539
Source
Medline
License
Unknown

Abstract

The glutathione transferase (GST) superfamily plays key roles in the detoxification of various xenobiotics. Here, we report the isolation and characterization of a silkworm protein belonging to a previously reported theta-class GST family. The enzyme (bmGSTT) catalyzes the reaction of glutathione with 1-chloro-2,4-dinitrobenzene, 1,2-epoxy-3-(4-nitrophenoxy)-propane, and 4-nitrophenethyl bromide. Mutagenesis of highly conserved residues in the catalytic site revealed that Glu66 and Ser67 are important for enzymatic function. These results provide insights into the catalysis of glutathione conjugation in silkworm by bmGSTT and into the metabolism of exogenous chemical agents.

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