ANALYSIS OF MICHAELIS-MENTEN KINETICS IN THE PRESENCE OF IRREVERSIBLE INHIBITORS THAT REACT WITH THE SUBSTRATE

This paper presents a kinetic analysis of a Michaelis-Menten enzyme-catalyzed reaction in the presence of irreversible inhibitors that are rendered unstable by their reaction with the substrate. A general mechanism involving competitive, non-competitive, uncompetitive and mixed irreversible inhibition with one or two steps has been analyzed, and analytical expressions for the evolution of all the species involved in the scheme have been obtained. By assigning arbitrary values to the kinetic constants of these equations, simulated cases of this type of enzymatic inhibition are presented. The results obtained show that the enzymatic systems of the type studied here present positive kinetic co-operativity for a Michaelian enzyme in its action on the substrate.