[Kinetics of alpha-chymotrypsin catalyzed hydrolysis in equilibrium. III. Rate constants for individual stages and thermodynamic parameters at different pH's].

The rate constants of the individual steps of the reversible chymotryptic hydrolysis of N-acetyl-L-phenylalanylglycinamide and methyl N-acetyl-L-phenylalaninate have been calculated on the basis of data on the velocity of the exchange between these substrates and products of their hydrolysis at equilibrium and also on the basis of steady-state kinetics of their cleavage. This was done for peptide substrate at pH 5.5, 7.3 and 8.2 and for ester substrate at pH 5.5. The free energy of the formation of intermediate complexes and free energy of activation were calculated. Thus a complete kinetic and thermodynamic description of chymotryptic catalysis of various pH is performed.