Kinetic study of an enzyme-catalysed reaction in the presence of novel irreversible-type inhibitors that react with the product of enzymatic catalysis.
In the present paper a kinetic study is made of the behaviour of a Michaelis-Menten enzyme-catalysed reaction in the presence of irreversible inhibitors rendered unstable in the medium by their reaction with the product of enzymatic catalysis. A general mechanism involving competitive, non-competitive, uncompetitive and mixed irreversible inhibition with one or two steps has been analysed. The differential equation that describes the kinetics of the reaction is non-linear and computer simulations of its dynamic behaviour are presented. The results obtained show that the systems studied here present kinetic co-operativity for a target enzyme that follows the simple Michaelis-Menten mechanism in its action on the substrate, except in the case of an uncompetitive-type inhibitor.
Navarro-Lozano
M J
MJ
Departmento de Química-Física, Escuela Universitaria Politécnica de Albacete, Universidad de Castilla-La Mancha, Spain.
Valero
E
E
Varon
R
R
Garcia-Carmona
F
F
D001667:Binding, Competitive; D002384:Catalysis; D004791:Enzyme Inhibitors / Q000494:pharmacology*; D004798:Enzymes / Q000378:metabolism*; D007700:Kinetics; D008433:Mathematics; D011485:Protein Binding
D004791:Enzyme Inhibitors; D004798:Enzymes