Energy landscape along an enzymatic reaction trajectory: hinges or cracks?
Energy landscape along an enzymatic reaction trajectory: hinges or cracks?
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DOI：
10.2976/1.2894846
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发表时间：
2008-04-01
期刊：
影响因子：
--
通讯作者：
Wolynes, Peter Guy
中科院分区：
文献类型：
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作者：
Whitford, Paul Charles;Onuchic, Jose Nelson;Wolynes, Peter Guy
酶平衡结构周围的最具动态柔性的区域是否与酶促反应中限速过程的过渡态所涉及的区域相同？克恩及其同事，Wolf-Watz等人，2004; Henzler-Wildman等人，2007 a，2007 b）已经表明，通过研究腺苷酸激酶平衡盆周围的构象动力学，可以获得关于决定总酶周转率的功能相关运动的见解。蛋白质结构的变构变化被证明是控制过程。在这篇评论中，我们比较了这项研究的结果与早期的预测的路线，酶经历其构象变化。这些预测是基于这样的想法，即蛋白质的能量表面由构象变化的末端结构决定。一个关键问题是蛋白质是否通过特定的铰链移动，或者它是否在结构变化期间“破裂”并进入部分未折叠状态。
Are the most dynamically flexible regions around the equilibrium structure of an enzyme the same regions involved in the transition state for rate limiting processes involved in the enzymatic reaction? Kern and-coworkers, Wolf-Watz et al., 2004; Henzler-Wildman et al., 2007a, 2007b) have shown that insights about functionally relevant motions that determine the overall enzyme turnover rate can be obtained by investigating conformational dynamics around the equilibrium basin of the enzyme adenylate kinase. An allosteric change in protein structure turns out to be the controlling process. In this commentary we compare results of this study with earlier predictions of the route by which the enzyme undergoes its conformational change. These predictions are based on the idea that the energy surface for the protein is determined by the end structures of the conformational change. A key issue is whether the protein moves by specific hinges or whether it "cracks" and accesses partially unfolded states during its structural change.