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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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