KINETIC-ANALYSIS OF A MICHAELIS-MENTEN MECHANISM IN WHICH THE ENZYME IS UNSTABLE

A kinetic analysis of the Michaelis-Menten mechanism is made for the c ases in which the free enzyme, or the enzyme-substrate complex, or bot h, are unstable, either spontaneously or as a result of the addition o f a reagent. The explicit time-course equations of all of the species involved has been derived under conditions of limiting enzyme concentr ation. The validity of these equations has been checked by using numer ical simulations. An experimental design and a kinetic data analysis a llowing the evaluation of the parameters and kinetic constants are rec ommended.