Macrokinetic Michaelis–Menten models based on thermodynamic activity provide insights into enzyme kinetics because they separate substrate–enzyme from substrate–solvent interactions. Kinetic parameters are estimated from experimental progress curves of enzyme-catalyzed reactions. Three pitfalls are discussed: deviations between thermodynamic and concentration-based models, product effects on the substrate activity coefficient, and product inhibition.

中文翻译：

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基于热力学活性的酶动力学进展曲线分析

基于热力学活动的宏观动力学Michaelis-Menten模型提供了酶动力学的见解，因为它们将底物-酶与底物-溶剂的相互作用分开了。动力学参数是根据酶催化反应的实验进度曲线估算的。讨论了三个陷阱：热力学模型和基于浓度的模型之间的偏差，产物对底物活性系数的影响以及产物的抑制作用。