A thermal-variation method for analysing the rate constants of the Michaelis-Menten mechanism

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Abstract
By analyzing the variations of saturation velocity and Km with temperature and invoking the mathematical constraint represented by the Arrhenius equation, it becomes possible to estimate k+2 and indistinguishably k+1 and k-1 for the Michaelis-Menten mechanisms of 1-substrate enzyme reactions. Distinction between k+1 and k-1 may be obtained through the determination of isotopic rate effects. This procedure thus provides a basis for evaluating all 3 rate constants of the 1-substrate mechanism, and disproves the suggestion that k+1 and k-1 are intrinsically unobtainable from steady-state kinetic measurements.