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Cooperative Allosteric Transitions01:58

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Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
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Allosteric regulation of enzymes occurs when the binding of an effector molecule to a site that is different from the active site causes a change in the enzymatic activity. This alternate site is called an allosteric site, and an enzyme can contain more than one of these sites. Allosteric regulation can either be positive or negative, resulting in an increase or decrease in enzyme activity. Most enzymes that display allosteric regulation are metabolic enzymes involved in the degradation or...
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トリプトファン合成エボリューションにおけるアロステリック・ドリブン・コンフォーマショナル・アンサンブルを解読する

Miguel A Maria-Solano1, Javier Iglesias-Fernández1, Sílvia Osuna1,2

  • 1CompBioLab group, Institut de Química Computacional i Catàlisi (IQCC) and Departament de Química , Universitat de Girona , Girona 17003 , Spain.

Journal of the American Chemical Society
|July 30, 2019
PubMed
まとめ
この要約は機械生成です。

研究者は,遠隔変異によって,トリプトファン合成酵素 (TrpS) のアロステリック調節を回復することによって,スタンドアロンベータサブユニットの効率を高めました. このアプローチは,生物合成用途の酵素機能の改善を可能にする.

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科学分野:

  • 酵素学
  • 構造生物学
  • 生物触媒

背景:

  • トリプトファン合成酵素 (TrpS) のようなマルチメリック酵素複合体は,アロステル結合によって効率的な触媒作用を示すが,単独では非効率である.
  • TrpSはαββ複合体であり,L-トリプトファンを合成し,その触媒的活動はサブユニット間のアロステル調節に依存する.

研究 の 目的:

  • *Pyrococcus furiosus* (PfTrpS) から TrpSのアロステリック調節を調査する.
  • 実験室で進化した独立したベータサブユニットの変種が,加熱効率を高めるために,アロステリックコンフォーマーションアンサンブルを回復する方法を理解する.

主な方法:

  • PfTrpSコンフォームアンサンブルの計算分析
  • 独立したベータサブユニットの実験室での進化.
  • 構成状態と触媒効率に影響を与える変異の特徴づけ.

主要な成果:

  • TrpSサブドメインの構成アンサンブルを復元することは,スタンドアロンベータサブユニット活動を強化するために不可欠です.
  • アロステル調節を回復し,形状動態を変更する遠隔変異が特定されました.
  • これらの変異は,基本的構成状態の間の集団と交換率を高めます.

結論:

  • アロステル酵素を独立した機能の改善に向けて進化させるための合理的なアプローチが開発された.
  • この戦略は,生物合成用途の酵素の設計に適用できます.
  • 酵素構成組の理解と操作は,タンパク質工学の鍵です.