Exact and approximate solutions for a century-old problem: A general treatment of Henri-Michaelis-Menten enzyme kinetics
Mario N. Berberan-Santos

TL;DR
This paper offers a new unified approach to Henri-Michaelis-Menten enzyme kinetics, providing exact solutions and systematic approximations through a simplified one-dimensional differential equation, enhancing understanding and computational methods.
Contribution
It introduces a novel one-variable differential equation formulation of HMM kinetics, enabling exact solutions and systematic approximations without quasi-steady-state assumptions.
Findings
Exact solutions as Maclaurin series for HMM kinetics
Systematic derivation of approximate solutions with validity conditions
Numerical computation method for concentration evolution over time
Abstract
A different view of Henri-Michaelis-Menten (HMM) enzyme kinetics is presented. In the first part of the paper, a simplified but useful description that stresses the cyclic nature of the catalytic process is introduced. The time-dependence of the substrate concentration after the initial transient phase is derived in a simple way that dispenses the mathematical technique known as quasi-steady-state approximation. In the second part of the paper an exact one-dimensional formulation of HMM kinetics is obtained. The whole problem is condensed in a single one-variable evolution equation that is a second-order non-linear differential equation, and the control parameters are reduced to three dimensionless quantities: enzyme efficiency, substrate reduced initial concentration, and enzyme reduced initial concentration. The exact solution of HMM kinetics is obtained as a set of Maclaurin series.…
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Taxonomy
TopicsProtein Structure and Dynamics
