Kinetic analysis of enzyme systems with suicide substrate in the presence of a reversible, uncompetitive inhibitor.
We present a general kinetic analysis of enzyme catalyzed reactions evolving according to a Michaelis-Menten mechanism, in which an uncompetitive, reversible inhibitor acts. Simultaneously, enzyme inactivation is induced by an unstable suicide substrate, i.e. it is a Michaelis-Menten mechanism with double inhibition: one originating from the substrate and another originating from the reversible inhibitor. Rapid equilibrium of the reversible reaction steps involved is assumed and the time course equations for the reaction product have been derived under the assumption of limiting enzyme. The goodness of the analytical solutions has been tested by comparison with simulated curves obtained by numerical integration. A kinetic data analysis to determine the corresponding kinetic parameters from the time progress curve of the product is suggested.
Moruno-Dávila
M A
MA
Departamento de Química-Física, Escuela Politécnica Superior, Universidad de Castilla-La Mancha, Avda. España, s/n, Campus Universitario, E-02071 Albacete, Spain.
Solo
C G
CG
García-Moreno
M
M
García-Cánovas
F
F
Varón
R
R
D004791:Enzyme Inhibitors / Q000494:pharmacology*; D004798:Enzymes / Q000378:metabolism*; D007700:Kinetics; D013379:Substrate Specificity
D004791:Enzyme Inhibitors; D004798:Enzymes