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Updated: Mar 7, 2026

Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes
Published on: January 16, 2016
Thermodynamic Activity-Based Interpretation of Enzyme Kinetics
1Institute of Technical Biochemistry, University of Stuttgart, Allmandring 31, 70569 Stuttgart, Germany.
Abstract:
The experimentally determined Michaelis constant Km results from a combination of two effects: the recognition of the substrate by the enzyme and the interactions between substrate and solvent. For a solvent-independent analysis of substrate specificity, the thermodynamic activity of the substrate, rather than its concentration, must be considered.
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