Dynamic Model of Protein Behavior and Mechanism of Enzymatic Function

Abstract

The functional model of enzymatic activity which will be presented is really a development of the association and dissociation mechanisms of specific complexes, such as the mechanism described in the preceding chapter. Kaivarainen (1979c) derived expressions interconnecting the rate of enzymatic reaction and the Michaelis constant KM with the free activation energies of fluctuation of the active site and of the auxiliary cavity of the enzyme between ‘closed’ and ‘open’ states during relaxational changes. These expressions yield a simple physical interpretation of the effects of competing and non-competing inhibitors, temperature and other nonspecific agents on the kinetics of the enzymatic process. The corollaries of the model have been confirmed by a large number of experimental results.