Structural insight into the active site of a Bombyx mori unclassified glutathione transferase

Tofazzal Hossain, Kohji Yamamoto

Research output: Contribution to journalArticle

Abstract

Glutathione transferases (GSTs) are major detoxification enzymes that play central roles in the defense against various environmental toxicants as well as oxidative stress. Here, we identify amino acid residues of an unclassified GST from Bombyx mori, bmGSTu-interacting glutathione (GSH). Site-directed mutagenesis of bmGSTu mutants indicated that amino acid residues Asp103, Ser162, and Ser166 contribute to catalytic activity.

Original languageEnglish
Pages (from-to)989-991
Number of pages3
JournalBioscience, Biotechnology and Biochemistry
Volume79
Issue number6
DOIs
Publication statusPublished - Jan 1 2015

Fingerprint

Bombyx
Glutathione Transferase
Catalytic Domain
Amino Acids
Detoxification
Mutagenesis
Oxidative stress
Site-Directed Mutagenesis
Glutathione
Catalyst activity
Oxidative Stress
Enzymes

All Science Journal Classification (ASJC) codes

  • Biotechnology
  • Analytical Chemistry
  • Biochemistry
  • Applied Microbiology and Biotechnology
  • Molecular Biology
  • Organic Chemistry

Cite this

Structural insight into the active site of a Bombyx mori unclassified glutathione transferase. / Hossain, Tofazzal; Yamamoto, Kohji.

In: Bioscience, Biotechnology and Biochemistry, Vol. 79, No. 6, 01.01.2015, p. 989-991.

Research output: Contribution to journalArticle

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