Two steps in the reaction of chymotrypsin with acetyl-l-phenylalanine ethyl ester

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Abstract
The effect of pH on kg, the first-order rate constant for the decomposition of the enzyme-substrate complex, and on Km, the Michaelis constant, was studied for the chymotrypsin-catalyzed hydrolysis of acetyl-L-phenyl-alanine ethyl ester. The results presented are consistent with previous findings that Km is the true dissociation constant E + S [image] ES and that this initial rapid enzyme substrate combination is independent of the subsequent catalytic step. Evidence that the imidazole group of histidine is the catalytic site of chymotrypsin is presented.