A Much better replacement of the Michaelis-Menten equation and its application
Banghe Li, Bo Li, Yuefeng Shen

TL;DR
This paper introduces a quartic equation as a more accurate and informative replacement for the Michaelis-Menten equation in enzyme kinetics, improving approximation during reaction and near completion.
Contribution
It proposes a new quartic equation A(S,E)=0 that surpasses Michaelis-Menten in accuracy and information content, with potential applications in enzyme reaction analysis.
Findings
Quartic equation A(S,E)=0 offers better approximation during the quasi-steady state.
The new equation approaches reaction end with matching tangent lines.
It differs from Michaelis-Menten less than 1/S^3 as substrate concentration increases.
Abstract
Michaelis-Menten equation is a basic equation of enzyme kinetics and gives an acceptable approximation of real chemical reaction processes. Analyzing the derivation of this equation yields the fact that its good performance of approximating real reaction processes is due to Michaelis-Menten curve (15). This curve is derived from Quasi-Steady-State Assumption(QSSA), which has been proved always true and called Quasi-Steady-State Law by Banghe Li et al [19]. Here, we found a quartic equation A(S,E)=0 (22), which gives more accurate approximation of the reaction process in two aspects: during the quasi-steady state of a reaction, Michaelis-Menten curve approximates the reaction well, while our quartic equation gives better approximation; near the end of the reaction, our equation approaches the end of the reaction with a tangent line same to that of the reaction, while…
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Taxonomy
TopicsProtein Structure and Dynamics · Quantum Computing Algorithms and Architecture · Advanced Thermodynamics and Statistical Mechanics
