Molecular structure of a prostaglandin D synthase requiring glutathione from the brown planthopper, Nilaparvata lugens

Kohji Yamamoto, Akifumi Higashiura, Mamoru Suzuki, Kosuke Aritake, Yoshihiro Urade, Atsushi Nakagawa

研究成果: ジャーナルへの寄稿学術誌査読

5 被引用数 (Scopus)

抄録

Prostaglandins are involved in many physiological processes, and prostaglandin synthases facilitate the detoxification of xenobiotics as well as endogenous compounds, such as through glutathione conjugation. Specifically, prostaglandin D synthase (PGDS) catalyzes the isomerization of PGH2 to PGD2. Here we report the identification and structural analysis of PGDS from the brown planthopper rice pest Nilaparvata lugens (nlPGDS), which belongs to the sigma-class glutathione transferases. The structure of nlPGDS in complex with glutathione was determined at a resolution of 2.0 Å by X-ray crystallography. Bound glutathione was localized to the glutathione-binding site (G-site). Enzyme activity measurements following site-directed mutagenesis of nlPGDS indicated that amino acid residues Tyr8, Leu14, Trp39, Lys43, Gln50, Val51, Gln63, and Ser64 in the G-site contribute to its catalytic activity. To our knowledge, this represents the first report of a PGDS in insects. Our findings provide insights into the mechanism of nlPGDS activity and potentially that of other insects and therefore may facilitate the development of more effective and safe insecticides.

本文言語英語
ページ(範囲)166-171
ページ数6
ジャーナルBiochemical and Biophysical Research Communications
492
2
DOI
出版ステータス出版済み - 10月 14 2017

!!!All Science Journal Classification (ASJC) codes

  • 生物理学
  • 生化学
  • 分子生物学
  • 細胞生物学

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