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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >How an enzyme surmounts the activation energy barrier
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How an enzyme surmounts the activation energy barrier

机译：酶如何克服激活能垒

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摘要

The action of chorismate mutase is a paradigm of enzyme catalysis, because the enzyme is a structurally simple protein that accelerates a straightforward unimolecu-lar reaction: a concerted, intramolecular rearrangement of chorismate to pre-phenate in which one carbon-carbon bond is formed and one carbon-oxygen bond is broken (Fig. 1). The reaction itself is a vital step in the biosynthesis of aromatic amino acids, lending the enzyme a biological importance equal to its importance in understanding mechanisms of catalysis. In this issue of PNAS, Hur and Bruice (1) have applied the near-attack conformation (NAC) concept, which Bruice and coworkers have been developing for several years (2, 3), to the accelerations produced by several different chorismate mutases, developing thereby what might be called a mi-crohistory of the catalytic process for these enzymes, tracing events between reactant state and transition state. The findings are illuminating and likely to generate considerable surprise.
机译：分支酸突变酶的作用是酶催化的范例，因为该酶是一种结构简单的蛋白质，可加速简单的单分子反应：将分支酸分子协调一致地分子内重排至形成一个碳-碳键的酚之前体。一个碳-氧键断裂（图1）。该反应本身是芳香族氨基酸生物合成中至关重要的一步，使该酶具有与理解催化机理相同的生物学重要性。在本期PNAS中，Hur和Bruice（1）将Bruice和他的同事们开发了几年（2、3）的近似攻击构象（NAC）应用于几种不同的分支酸突变产生的加速作用，从而发展出可能被称为这些酶催化过程的微观历史，追踪反应物状态和过渡状态之间的事件。研究结果具有启发性，并可能会引起相当大的惊奇。

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