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Induced-fit Model01:13

Induced-fit Model

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Most chemical reactions in cells require enzymes—biological catalysts that speed up the reaction without being consumed or permanently changed. They reduce the activation energy needed to convert the reactants into products. Enzymes are proteins, that usually work by binding to a substrate—a reactant molecule that they act upon.
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Inside living organisms, enzymes act as catalysts for many biochemical reactions involved in cellular metabolism. The role of enzymes is to reduce the activation energies of biochemical reactions by forming complexes with its substrates. The lowering of activation energies favor an increase in the rates of biochemical reactions.
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Binding sites linkages can regulate a protein's function.  For example, enzyme activity is often regulated through a feedback mechanism where the end product of the biochemical process serves as an inhibitor.
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For many years, scientists thought that enzyme-substrate binding took place in a simple "lock-and-key" fashion. This model stated that the enzyme and substrate fit together perfectly in one instantaneous step. However, current research supports a more refined view scientists call induced fit. The induced-fit model expands upon the lock-and-key model by describing a more dynamic interaction between enzyme and substrate. As the enzyme and substrate come together, their interaction causes...
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Defining Substrate Specificities for Lipase and Phospholipase Candidates
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酵素基板の特異性は,異なる形状経路によって与えられる.

Florencia Rago1, Daniel Saltzberg2, Karen N Allen1,3

  • 1Program in Biochemistry and Molecular Biology (BMB), Boston University , Boston, Massachusetts 02215, United States.

Journal of the American Chemical Society
|October 7, 2015
PubMed
まとめ
この要約は機械生成です。

酵素の形状の変化は基質の特異性を決定する. アルドーラゼは,異なる形状を用いて,フルークトーゼ1-リン酸とフルークトーゼ1,6-二リン酸を区別し,形状の変化と触媒を結びつける.

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科学分野:

  • 生物化学
  • 酵素運動
  • タンパク質の構成動態

背景:

  • 酵素触媒は基質の認識に依存しているが,酵素の構造変化と基質の選択性を関連付ける直接的な証拠は限られている.
  • アルドーラーゼは,重要な糖分分解酵素で,フルークトーゼ1-リン酸とフルークトーゼ1,6-リン酸を区別しなければならないので,基板の差別を研究するための理想的なモデルである.
  • 活性部位から遠い同酵素固有残留物 (ISR) は,特に表面アルファヘリックスとカルボキシル末端領域 (CTR) で,運動的区別を媒介することが知られている.

研究 の 目的:

  • 酵素構成の変化がアルドラーゼにおける基質選択性の基礎にあるという仮説を調査する.
  • 表面アルファヘリックスとCTRを含む特定の領域がこれらの構成変化を媒介する役割を調査する.
  • 観察された形状動態と触媒過程の間のリンクを確立する.

主な方法:

  • サイト固有のラベリングのためのアルドラーゼの単一の表面システインの変種を作成します.
  • 環境に敏感なフッ素素でラベルを貼る
  • 光放射スペクトロフォトメトリーと停止フロー光スペクトロフォトメトリーを用いた形状の変化のモニタリング.

主要な成果:

  • 標識されたアルドラーゼ変種の光スペクトルは,フルークトーゼ1-リン酸とフルークトーゼ1,6-リン酸の飽和量に差異があり,異なる形状を示しています.
  • 光スペクトルの基質濃度依存の変化により,結合が確認されました.
  • 止まった流れの光測定は,触媒と同じ時間スケールで形状の変化の割合が起こったことを明らかにした.

結論:

  • アルドーラゼは基板特有の形状の変化を示します.
  • これらの構成動態は,酵素の触媒サイクルと基板認識に関連しています.
  • 構成の変化は,複数の基板を持つ酵素における基板特異性の潜在的な共通のメカニズムを表しています.