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The Michaelis-Menten paradox: Km is not an equilibrium constant but a steady-state constant.

By Enric I. Canela, Gemma Navarro, Jose Luis Beltran, Rafael Franco

Posted 13 Apr 2019
bioRxiv DOI: 10.1101/608232

The Michaelis-Menten constant (Km), the concentration of substrate ([S]) providing half of enzyme maximal activity, is higher than the ES → E+S dissociation equilibrium constant. Actually, Km should be defined as the constant defining the steady state in the E+S=ES → E+P model and, accordingly, caution is needed when Km is used as a measure of the "affinity" of the enzyme-substrate interaction.

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