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首页> 外文期刊>Biochemistry >Pre-steady-state analysis of ATP hydrolysis by Saccharomyces cerevisiae DNA topoisomerase II. 2. Kinetic mechanism for the sequential hydrolysis of two ATP
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Pre-steady-state analysis of ATP hydrolysis by Saccharomyces cerevisiae DNA topoisomerase II. 2. Kinetic mechanism for the sequential hydrolysis of two ATP

机译：酿酒酵母DNA拓扑异构酶II对ATP水解的稳态分析。 2.两种ATP顺序水解的动力学机理

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摘要

In the preceding paper, we showed that DNA topoisomerase II from Saccharomyces cerevisiae binds two ATP and rapidly hydrolyzes at least one of them before encountering a slow step in the reaction mechanism. These data are potentially consistent with two different types of reaction pathways: (1) sequential ATP hydrolysis or (2) simultaneous hydrolysis of both ATP. Here, we present results that are consistent only with topoisomerase II hydrolyzing its two bound ATP sequentially. Additionally, these results indicate that the products of the first hydrolysis are released from the enzyme before the second ATP is hydrolyzed, Release of products from both the first and second hydrolyses contributes to the rate-determining process. The proposed mechanism for ATP hydrolysis by topoisomerase II is complex, having nine rate constants. To calculate values for each of these rate constants, a technique of kinetic parameter estimation was developed. This technique involved using singular perturbation theory in order to estimate rate constants, and consequently identify kinetic steps following the rate-determining step. [References: 38]
机译：在先前的论文中，我们显示了来自酿酒酵母的DNA拓扑异构酶II与两个ATP结合并迅速水解至少其中一个，然后遇到反应机理中的缓慢步骤。这些数据可能与两种不同类型的反应途径一致：（1）连续ATP水解或（2）两种ATP同时水解。在这里，我们提出的结果仅与拓扑异构酶II顺序水解其两个结合的ATP一致。另外，这些结果表明第一次水解的产物在第二ATP被水解之前就已从酶中释放出来。第一次水解和第二次水解中产物的释放都有助于速率的确定过程。拓扑异构酶II提议的ATP水解机理很复杂，具有9个速率常数。为了计算每个这些速率常数的值，开发了一种动力学参数估计技术。该技术涉及使用奇异摄动理论来估计速率常数，并因此确定速率确定步骤之后的动力学步骤。 [参考：38]

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