An existing model for the rate coefficients of enzyme-catalyzed processes involves the regularized gamma function of Euler replacing the exponential dependence of the rate coefficient from the reaction barrier. The application of this model to experimental data, on one hand, validates the model by correctly describing the negative curvature of Eyring plots. On the other hand, this analysis evidences that enzymes never reach the maximum theoretical efficiency, a counterintuitive fact that requires an explanation. This work interprets this evolutionary limit in terms of the necessity of living systems to achieve and maintain homeostasis. Further validation of the expression for the rate coefficients comes from the analysis of the discrepancy between the theoretically predicted energy difference between reactants and products in a chemical equilibrium and the corresponding value obtained by regression to the classical expression for the equilibrium constant. The discrepancy is resolved by making use of the proposed model.

中文翻译：

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关于酶催化反应速率的物理和进化极限

酶催化过程的速率系数的现有模型涉及欧拉的正则化伽马函数，以取代反应势垒中速率系数的指数依赖性。将该模型应用于实验数据，一方面通过正确描述 Eyring 图的负曲率来验证模型。另一方面，该分析证明酶从未达到最大理论效率，这是一个需要解释的违反直觉的事实。这项工作根据生命系统实现和维持稳态的必要性来解释这种进化极限。速率系数表达式的进一步验证来自对化学平衡中反应物和产物之间的理论预测能量差异与通过回归到平衡常数经典表达式获得的相应值之间的差异的分析。通过使用所提出的模型来解决差异。