Functional Analysis of an Epsilon-Class Glutathione S-Transferase From Nilaparvata lugens (Hemiptera: Delphacidae)

研究成果: ジャーナルへの寄稿記事

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.

元の言語英語
ジャーナルJournal of insect science (Online)
19
発行部数5
DOI
出版物ステータス出版済み - 9 1 2019

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Delphacidae
Nilaparvata lugens
glutathione transferase
Hemiptera
insecticides
xenobiotics
glutathione
binding sites
amino acid sequences
mutation

All Science Journal Classification (ASJC) codes

  • Insect Science

これを引用

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