Submitted August 6, 1996.
General schemes of unbranched multisubstrate enzymatic reactions associated with enzyme inactivation during the reaction are analyzed. Equations of integral kinetics at constant and decreasing substrate concentrations are presented. Experimental concentration curves characterized by additivity of some enzyme intermediates (optical absorption, fluorescence, EPR, etc. spectra) are theoretically analyzed. Rapid equilibrium at certain steps of the enzymatic reaction is considered. The relationships between the enzyme intermediates is a criterion of the kinetic behavior of the enzymatic reaction mechanism. New coordinates are suggested for the analysis of the integral kinetics of self-inactivating enzymes. Results of the analysis are used for interpretation of data on arachidonic cascade enzymes.
KEY WORDS: integral kinetics, multisubstrate enzymatic reaction, enzyme inactivation, qualitative criteria, prostaglandin H-synthetase.