Abstract
The glutathione S-transferase (GST) superfamily is involved in the detoxification of various xenobiotics. A silkworm GST, belonging to a previously reported Epsilon-class GST family, was identified, named bmGSTE, cloned, and produced in Escherichia 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 Ser11, His53, Val55, Ser68 and Arg112, 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 His53, Val55, and Ser68 were important for enzyme function.
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