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<p>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.</p>

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Non-hyperbolic enzyme kinetics: the case of P-type ATPases

  • 期刊论文

  • 发表日期：

    2025年2月11日

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  • S. E. Faraj,
  • M. R. Montes,
  • R. D. Peluffo,
  • R. M. González-Lebrero,
  • R. C. Rossi

摘要

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.