Enzyme dynamics during catalysis
Enzyme dynamics during catalysis
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DOI：
10.1126/science.1066176
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发表时间：
2002-02-22
期刊：
影响因子：
56.9
通讯作者：
Kern, D
中科院分区：
文献类型：
--
作者：
Eisenmesser, EZ;Bosco, DA;Kern, D
内部蛋白质动力学与酶催化密切相关。然而，与底物周转有关的酶运动在很大程度上仍然未知。我们已经研究了动力学的酶在催化过程中的原子分辨率使用核磁共振弛豫方法。在亲环素A酶的催化作用期间，我们检测到在数百微秒的时间尺度上发生的活性位点的构象波动。酶的构象动力学速率与底物周转的微观速率密切相关。目前的结果，连同可用的结构数据，允许预测的反应轨迹。
Internal protein dynamics are intimately connected to enzymatic catalysis. However, enzyme motions linked to substrate turnover remain largely unknown. We have studied dynamics of an enzyme during catalysis at atomic resolution using nuclear magnetic resonance relaxation methods. During catalytic action of the enzyme cyclophilin A, we detect conformational fluctuations of the active site that occur on a time scale of hundreds of microseconds. The rates of conformational dynamics of the enzyme strongly correlate with the microscopic rates of substrate turnover. The present results, together with available structural data, allow a prediction of the reaction trajectory.