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Updated: Jun 4, 2026
09:42
Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes
Published on: January 16, 2016
Enzyme kinetics and the maximum entropy production principle
Andrej Dobovišek1, Paško Zupanović, Milan Brumen
1University of Maribor, Faculty of Natural Sciences and Mathematics, Slovenia. andrej.dobovisek@uni-mb.si
Biophysical Chemistry
|February 23, 2011
Summary
Biological evolution of enzymes may be quantified by entropy production. Maximum entropy production indicates a fully evolved enzyme, with rate constants aligning with physical principles.
Area of Science:
- Biophysics
- Biochemistry
- Enzyme kinetics
Background:
- Biological evolution of enzymes is often linked to changes in their internal transitions.
- Quantifying the progress of enzyme evolution requires robust theoretical frameworks.
Purpose of the Study:
- To derive a general proof for maximum entropy production with respect to rate constants in enzymatic transitions.
- To test if increased entropy production quantifies enzyme evolution progress.
- To establish maximum entropy production as a marker for fully evolved enzymes.
Main Methods:
- Derivation of a general proof for entropy production maximization.
- Analysis of the ES↔EP transition in a generalized reversible Michaelis-Menten three-state scheme.
- Comparison of predicted optimal rate constants with experimentally determined values for β-Lactamase enzymes.
Main Results:
- A general principle for optimizing enzymatic rate constants via maximum entropy production is established.
- Experimental data for β-Lactamase enzymes show good agreement with predicted optimal values.
- This principle offers a novel way to quantify enzyme evolution.
Conclusions:
- Maximum entropy production serves as a valid metric for enzyme evolution.
- Enzyme rate constants are optimized according to fundamental physical principles.
- This approach is distinct from metabolic flux maximization or entropy production minimization.
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The experimenter can then plot the initial reaction rate or velocity (Vo) of a given trial against the substrate concentration ([S]) to obtain a graph of the reaction properties. For many enzymatic reactions involving a...
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