KINETIC-STUDY OF AN ENZYME-CATALYZED 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 Mic haelis-Menten enzyme-catalysed reaction in the presence of irreversibl e inhibitors rendered unstable in the medium by their reaction with th e product of enzymatic catalysis. A general mechanism involving compet itive, non-competitive, uncompetitive and mixed irreversible inhibitio n with one or two steps has been analysed. The differential equation t hat describes the kinetics of the reaction is non-linear and computer simulations of its dynamic behaviour are presented. The results obtain ed show that the systems studied here present kinetic co-operativity f or 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.