Ligand-Induced Conformational Changes near the Active Site Regulating Enzyme Activity of Momorcharins from Seeds of Bitter Gourd

Chie Matsunaga, Yuuki Okada, Etsuko Nishimoto

研究成果: ジャーナルへの寄稿学術誌査読

2 被引用数 (Scopus)

抄録

It is reasonable to consider that Type I-ribosomal inactivation proteins (RIP) retain some specific affinity to harmful pathogens to complete the role as a bio-defense relating protein. In the present studies, it was shown that two Type I-RIPs, α- and β-momorcharins, maintained the abilities to bind with N-acetylglucosamine (NAG) to change the conformation around the active sites and to regulate their N-glycosidase activities. By the binding of NAG, the freedom of internal motion of Trp192 in α-momorcharin was increased 1.5 times near the active site and, on the other hand, the corresponding motion of Trp190 was limited 50% in β-momorcharin. The results in the fluorescence resonance excitation energy transfer experiments demonstrated that Trp-190 of β-momorcharin was kept away from Tyr-70 but Trp192 contrarily approached closer to the nearest neighboring Tyr residue consisting of the active center of α-momorcharin by the binding with NAG. These conformational changes near the active site close correlated with promotion and/or suppression of the N-glucosidase activities of β- and α-momorcharins.

本文言語英語
ページ(範囲)231-240
ページ数10
ジャーナルJournal of Fluorescence
29
1
DOI
出版ステータス出版済み - 1月 15 2019

!!!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

フィンガープリント

「Ligand-Induced Conformational Changes near the Active Site Regulating Enzyme Activity of Momorcharins from Seeds of Bitter Gourd」の研究トピックを掘り下げます。これらがまとまってユニークなフィンガープリントを構成します。

引用スタイル