Sugar binding effects on the enzymatic reaction and conformation near the active site of pokeweed antiviral protein revealed by fluorescence spectroscopy

Hiromichi Nakashima, Yukihiro Fukunaga, Ryosuke Ueno, Etsuko Nishimoto

研究成果: ジャーナルへの寄稿学術誌査読

4 被引用数 (Scopus)

抄録

In various trials for elucidating the physiological function of pokeweed antiviral protein (PAP), studies on the interaction with sugar are essential. The fluorescence titration curves showed that PAP retained the strong affinity against N-acetylglucosamine (NAG) and two sites in one PAP molecule co-operatively participated in the binding. In the complex of PAP with NAG, Trp208 located at the entrance lid site of substrate came closer to Tyr72 about 0.3 Å. Furthermore, the fluorescence anisotropy decay measurement demonstrated that the segmental rotation of Trp208 was enlarged by the binding of PAP with NAG. Such conformational changes around the active site closely correlate with the enzymatic activity of PAP. The N-glycosidase activity of PAP was enhanced more than two times in the presence of NAG. The obtained results consistently suggested the enzymatic activity of PAP would be regulated through the conformation change near the active site induced by the binding with NAG.

本文言語英語
ページ(範囲)951-958
ページ数8
ジャーナルJournal of Fluorescence
24
3
DOI
出版ステータス出版済み - 5月 2014

!!!All Science Journal Classification (ASJC) codes

  • 生化学
  • 臨床心理学
  • 社会科学(その他)
  • 社会学および政治科学
  • 分光学
  • 臨床生化学
  • 法学

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