Abstract
A computer-based method is employed for the reformulation of rate equations for enzyme-catalyzed reactions from the coefficient form to the kinetic form. This method is applied to equations for the initial rate of enzyme-catalyzed isotope exchange. In the reformulated equations, the coefficients of each rate equation term are expressed as maximum velocity of the initial rate of the net reaction, Michaelis constants, inhibition constants, and exchange constants. The definition of the exchange constant for a given reactant may be identical to one of the inhibition constants for that reactant.
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