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An omega‐class glutathione S ‐transferase in the brown planthopper Nilaparvata lugens exhibits glutathione transferase and dehydroascorbate reductase activities
Author(s) -
Saruta Fumiko,
Yamada Naotaka,
Yamamoto Kohji
Publication year - 2019
Publication title -
archives of insect biochemistry and physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.576
H-Index - 66
eISSN - 1520-6327
pISSN - 0739-4462
DOI - 10.1002/arch.21599
Subject(s) - brown planthopper , glutathione , glutathione s transferase , biology , biochemistry , transferase , glutathione reductase , escherichia coli , recombinant dna , reductase , microbiology and biotechnology , enzyme , glutathione peroxidase , gene
A complementary DNA that encodes an omega‐class glutathione S ‐transferase (GST) of the brown planthopper, Nilaparvata lugens (nlGSTO), was isolated by reverse transcriptase polymerase chain reaction. A recombinant protein (nlGSTO) was obtained via overexpression in the Escherichia coli cells and purified. nlGSTO catalyzes the biotransformation of glutathione with 1‐chloro‐2,4‐dinitrobenzene, a general substrate for GST, as well as with dehydroascorbate to synthesize ascorbate. Mutation experiments revealed that putative substrate‐binding sites, including Phe28, Cys29, Phe30, Arg176, and Lue225, were important for glutathione transferase and dehydroascorbate reductase activities. As ascorbate is a reducing agent, nlGSTO may participate in antioxidant resistance.