Abstract
For single intermediate enzyme kinetic systems, a relationship between a defined dimensionless parameter alpha (α) and the rate constants and initial enzyme concentration of the system was derived to describe the stationary-state trajectory of d(P)/dt versus (S) between the upper and lower bounds of the Michaelis-Menten and Briggs-Haldane systems. It was found that α is a function of E o /k m and the parameter Ω, which is a function of k 2 and k 3. The development of the α parameter provides a new method for directly estimating all the rate constants in the enzyme kinetic model, given (S) and (P) data as a function of time. This method for estimating the three rate constants and initial enzyme concentration is tested on four sets of simulated discrete (isothermal) data covering a range of different trajectories and on experimental data for the horseradish-peroxidase enzyme system.
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