Representation of the reversible enzymatic inhibition effect for the kinetic model of Michelis-Menten in transient state

Summary

Enzymatic processes that follow the kinetic model of Micahelis-Merten had been studied taking as reference different proposals to describe the reversible inhibition phase. Inhibition proposals were compared based on a generic process. In this process, the kinetic constants received unitary values and the numeric value of the substrate concentration was ten (10) times higher than the numeric value of enzyme concentration. Numeric solutions based on a non-linear system of ordinary differential equations were obtained for each proposal of the inhibition model, resulting in a graphic representing, separately, the variation of enzyme concentrations, enzymatic complexes, substrate and product reaction. One model was obtained, among the evaluated proposals, with performance indicating behavior similar to the classical Michaelis-Menten model, where the reaction complex is rapidly formed and, along the process, decay tending to zero. However, differently from the classic model, in the proposed new model the inhibition process starts at zero and, during the process, tends to the nominal value of the initial enzymatic concentration. Such responses were shown to be valid for different values of enzyme concentration and processing time, showing robustness and indicating that the sum of the substrate and the product tends to reach the nominal value of the initial concentration of the substrate along the processing time.

Key words:
Enzymatic catalysis; Kinetic model; Michaelis-Menten model