Functional analysis of an epsilon-class glutathione s-transferase from nilaparvata lugens (Hemiptera: Delphacidae)

研究成果: Contribution to journalArticle査読

2 被引用数 (Scopus)

抄録

Glutathione conjugation is a crucial step in xenobiotic detoxification. In the current study, we have functionally characterized an epsilon-class glutathione S-transferase (GST) from a brown planthopper Nilaparvata lugens (nlGSTE). The amino acid sequence of nlGSTE revealed approximately 36-44% identity with epsilon-class GSTs of other species. The recombinant nlGSTE was prepared in soluble form by bacterial expression and was purified to homogeneity. Mutation experiments revealed that the putative substrate-binding sites, including Phe107, Arg112, Phe118, and Phe119, were important for glutathione transferase activity. Furthermore, inhibition study displayed that nlGSTE activity was affected by insecticides, proposing that, in brown planthopper, nlGSTE could recognize insecticides as substrates.

本文言語英語
論文番号iez096
ジャーナルJournal of Insect Science
19
5
DOI
出版ステータス出版済み - 9 1 2019

All Science Journal Classification (ASJC) codes

  • 昆虫科学

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