Glutathione-binding site of a Bombyx mori theta-class glutathione transferase

M. D.Tofazzal Hossain, Naotaka Yamada, Kohji Yamamoto

Research output: Contribution to journalArticle

7 Citations (Scopus)

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.

Original languageEnglish
Article numbere97740
JournalPloS one
Volume9
Issue number5
DOIs
Publication statusPublished - May 21 2014

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Bombyx
Bombyx mori
silkworms
Glutathione Transferase
glutathione transferase
Glutathione
glutathione
binding sites
Binding Sites
Dinitrochlorobenzene
Propane
Detoxification
Mutagenesis
propane
Xenobiotics
xenobiotics
bromides
Catalysis
epoxides
catalytic activity

All Science Journal Classification (ASJC) codes

  • Biochemistry, Genetics and Molecular Biology(all)
  • Agricultural and Biological Sciences(all)

Cite this

Glutathione-binding site of a Bombyx mori theta-class glutathione transferase. / Hossain, M. D.Tofazzal; Yamada, Naotaka; Yamamoto, Kohji.

In: PloS one, Vol. 9, No. 5, e97740, 21.05.2014.

Research output: Contribution to journalArticle

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