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Rapid-equilibrium rate equations for enzyme-catalyzed reactions are especially useful when the mechanism involves a number of pKs, but they are also useful when some reactants have stoichiometric numbers greater than one or hydrogen ions are produced or consumed in the rate-determining step. The pH dependencies of limiting velocities, Michaelis constants, and reaction velocities for the forward reaction...
This article shows how pKs for the enzymatic site and enzyme-substrate complexes can be obtained from kinetic experiments on the reaction A+B=P+Q, with and without the consumption of hydrogen ions. The rapid-equilibrium rate equation makes it possible to obtain the pKs and chemical equilibrium constants involved in the mechanism, the apparent equilibrium constant K′ for the catalyzed reaction, and...
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