Kinetic and structural analysis of enzyme intermediates: Lessons from EPSP synthase
Kinetic and structural analysis of enzyme intermediates: Lessons from EPSP synthase
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酶中间体的动力学和结构分析：EPSP 合酶的经验教训
DOI：
10.1021/cr00105a004
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发表时间：
1990
期刊：
影响因子：
62.1
通讯作者：
K. Johnson
中科院分区：
文献类型：
--
作者：
K. Anderson;K. Johnson
在催化过程中中间体的鉴定为特定的反应途径提供了积极的“证据”，因此，许多解决酶促机理的尝试都集中在分离或提供给定中间体的证据上。然而，中间体的鉴定只是建立反应顺序和提供催化途径的完整动力学和热力学描述的更大目标的一部分。此外，在没有完整的动力学表征的情况下，人们不能证明光谱上观察到的或分离和化学鉴定的新物质对应于真正的反应中间体。在这篇综述中，我们将研究用于建立反应路径和识别中间体的标准，重点是
The identificationof intermediates during catalysis provides positive “proof” for a particular reaction pathway and, accordingly, many attempts to solve an enzymatic mechanism have centered on efforts to iso-late or provide evidence for a given intermediate. However, the identification of an intermediate is only one part of a larger goal to establish a reaction sequence and to provide a complete kinetic and thermodynamic description of the catalytic pathway. Moreover, in the absence of a complete kinetic characterization, one cannot prove that a new species observed spectroscop-ically or isolated and identified chemicallycorresponds to a true reaction intermediate. In this review, we will examine the criteria used to establish a reaction path-way and to identify intermediates with a focus on the