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Catalytic function of an E psilon‐class glutathione S‐transferase of the silkworm
Author(s) -
Yamamoto K.,
Aso Y.,
Yamada N.
Publication year - 2013
Publication title -
insect molecular biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.955
H-Index - 93
eISSN - 1365-2583
pISSN - 0962-1075
DOI - 10.1111/imb.12041
Subject(s) - glutathione s transferase , glutathione , biochemistry , mutagenesis , enzyme , biology , transferase , site directed mutagenesis , mutant , function (biology) , peroxidase , amino acid , microbiology and biotechnology , gene , genetics
The glutathione S ‐transferase ( GST ) superfamily is involved in the detoxification of various xenobiotics. A silkworm GST, belonging to a previously reported E psilon‐class GST family, was identified, named bmGSTE , cloned, and produced in E scherichia coli . Investigation of this enzyme's properties showed that it was able to catalyse glutathione (GSH) with 1‐chloro‐2,4‐dinitrobenzene and ethacrynic acid, and also that it possessed GSH‐dependent peroxidase activity. The enzyme's highly conserved amino acid residues, including S er11, H is53, V al55, S er68 and A rg112, were of interest regarding their possible involvement in its catalytic activity. These residues were replaced with alanine by site‐directed mutagenesis and subsequent kinetic analysis of bmGSTE mutants indicated that H is53, V al55, and S er68 were important for enzyme function.