An alternative analysis of enzyme systems based on the whole reaction time: evaluation of the kinetic parameters and initial enzyme concentration

Abstract

This work presents an alternative analysis of the integrated rate equations corresponding to the simple Michaelis-Menten mechanism without product inhibition. The suggested new results are reached under a minimal set of assumptions and include, as a particular case, the classical integrated Michaelis–Menten equation. Experimental designs and a kinetic data analysis are suggested to the estimation of the maximum steady-state rate, Vmax, the Michaelis–Menten constant, Km, the initial enzyme concentration, [E]0, and the catalytic constant, k2. The goodness of the analysis is tested with simulated time progress curves obtained by numerical integration.