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) |
| 巻 | 19 |
| 発行部数 | 5 |
| DOI | |
| 出版物ステータス | 出版済み - 9 1 2019 |
Fingerprint
All Science Journal Classification (ASJC) codes
- Insect Science
これを引用
Functional Analysis of an Epsilon-Class Glutathione S-Transferase From Nilaparvata lugens (Hemiptera : Delphacidae). / Saruta, Fumiko; Yamada, Naotaka; Yamamoto, Kohji.
：: Journal of insect science (Online), 巻 19, 番号 5, 01.09.2019.研究成果: ジャーナルへの寄稿 › 記事
}
TY - JOUR
T1 - Functional Analysis of an Epsilon-Class Glutathione S-Transferase From Nilaparvata lugens (Hemiptera
T2 - Delphacidae)
AU - Saruta, Fumiko
AU - Yamada, Naotaka
AU - Yamamoto, Kohji
PY - 2019/9/1
Y1 - 2019/9/1
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=85073148656&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=85073148656&partnerID=8YFLogxK
U2 - 10.1093/jisesa/iez096
DO - 10.1093/jisesa/iez096
M3 - Article
C2 - 31606747
AN - SCOPUS:85073148656
VL - 19
JO - Journal of Insect Science
JF - Journal of Insect Science
SN - 1536-2442
IS - 5
ER -