The kinetic effect of product instability in a Michaelis-Menten mechanism with competitive inhibition.
In most kinetic studies it is assumed that both the reactant and the products are stable. However, under certain conditions spontaneous decomposition or deterioration caused by one of the participating species occurs. Studies, in which a species (the free enzyme, the enzyme-substrate complex, an inhibitor or the product of the reaction) is unstable, have appeared in the literature. However, to our knowledge, the enzymatic systems, in which a competitive inhibition and a decomposition or transformation of the products take place simultaneously, have not been studied so far. In this paper, we present a kinetic analysis of an enzyme reaction that follows a Michaelis-Menten mechanism, in which the free enzyme suffers a competitive inhibition simultaneously with the decomposition of the immediate product. In this study, we have linearised the differential equations that describe the kinetics of the process. Under the assumption of limiting concentration of enzyme, we have obtained and tested the explicit equation describing the time dependence of the product concentration using numerical calculus. With this equation and the experimental progress curve of the product, we constructed an easy procedure for the evaluation of the principal kinetic parameters of the process.
Garrido-del Solo
C
C
Departamento de Química-Física, Escuela Politécnica Superior, Universidad de Castilla-La Mancha, Avda. Espana, s/n. Campus Universitario, E-02071, Albacete, Spain.
Moruno
M A
MA
Havsteen
B H
BH
Castellanos
R V
RV
D000818:Animals; D004798:Enzymes / Q000378:metabolism*; D006801:Humans; D007700:Kinetics; D008954:Models, Biological; D013379:Substrate Specificity
D004798:Enzymes