Enzymatic characterization of two epsilon‐class glutathione S‐transferases of Spodoptera litura. Issue 3 (13th December 2017)

• Record Type: Journal Article
• Authors: Hirowatari, Aiko; Chen, Zhiwei; Mita, Kazuei; Yamamoto, Kohji
• Is Part Of: Archives of insect biochemistry and physiology. Volume 97:Issue 3(2018)
• Page Start: n/a
• Page End: n/a
• Publication Date: 2017-12-13
• Subjects: glutathione -- glutathione transferase -- Lepidoptera -- Spodoptera litura; Insects -- Physiology -- Periodicals; Insect biochemistry -- Periodicals; 595.701572
• DOI: 10.1002/arch.21443
• Languages: English
• ISSNs: 0739-4462

Abstract

Abstract: Two cDNAs encoding glutathione S ‐transferase (GST) of the tobacco cutworm, Spodoptera litura, were cloned by reverse transcriptase‐polymerase chain reaction. The deduced amino acid sequences of the resulting clones revealed 32–51% identities to the epsilon‐class GSTs from other organisms. The recombinant proteins were functionally overexpressed in Escherichia coli cells in soluble form and were purified to homogeneity. The enzymes were capable of catalyzing the bioconjugation of glutathione with 1‐chloro‐2, 4‐dinitrobenzene, 1, 2‐epoxy‐3‐(4‐nitrophenoxy)‐propane, and ethacrynic acid. A competition assay revealed that the GST activity was inhibited by insecticides, suggesting that it could be conducive to insecticide tolerance in the tobacco cutworm.