Faraj S E, Montes M R, Peluffo R D, González-Lebrero R M, Rossi R C
Facultad de Farmacia y Bioquímica, Departamento de Química Biológica, Universidad de Buenos Aires, Buenos Aires, Argentina.
Consejo Nacional de Investigaciones Científicas y Técnicas (CONICET), Universidad de Buenos Aires, Instituto de Química y Fisicoquímica Biológicas "Prof. Alejandro C. Paladini" (IQUIFIB), Buenos Aires, Argentina.
Biophys Rev. 2025 Feb 11;17(2):479-490. doi: 10.1007/s12551-025-01277-y. eCollection 2025 Apr.
Many enzymes operate through mechanisms that comply with the Michaelis-Menten equation (hyperbolic kinetics). The theoretical framework for analyzing these enzymes, widely developed in the literature, is largely based on the ability to linearize the equation and apply linear regression to experimental data. However, certain systems, such as P-type ATPases, present mechanisms that do not fit into hyperbolic models, requiring the development of more complex equations. This study explores the underlying causes of the non-hyperbolic behavior observed for P-type ATPases and reviews some methodologies used for their analysis. Here, we propose to employ rational equations, whose form limits the range of possible kinetic models applicable to the system, offering a structured approach to its analysis.
许多酶通过符合米氏方程(双曲线动力学)的机制发挥作用。文献中广泛发展的用于分析这些酶的理论框架,在很大程度上基于将该方程线性化并将线性回归应用于实验数据的能力。然而,某些系统,如P型ATP酶,呈现出不符合双曲线模型的机制,这就需要开发更复杂的方程。本研究探讨了P型ATP酶观察到的非双曲线行为的潜在原因,并回顾了一些用于其分析的方法。在此,我们建议采用有理方程,其形式限制了适用于该系统的可能动力学模型的范围,为其分析提供了一种结构化方法。