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In vivo, chymotrypsin is a proteolytic enzyme (Serine protease) acting in the digestive systems of many organisms. It facilitates the cleavage of peptide bonds by a hydrolysis reaction, which despite being thermodynamically favorable occurs extremely slowly in the absence of a catalyst.
Chymotrypsin catalyzes the reaction rate by a factor of 10 9. The reaction has two steps, an acylation phase and a deacylation phase. In the former phase, the peptide bond is cleaved and an ester is formed between substrate and enzyme.In the latter phase, this ester is hydrolyzed and the enzyme is regenerated. This illustrates the covalent catalysis of chymotrypsin.The first step is the acylation, which forms the acyl-enzyme intermediate. Then the acyl-enzyme intermediate goes through deacylation converting back to its original free enzyme form.he reaction has two steps, an acylation phase and a deacylation phase. In the former phase, the peptide bond is cleaved and an ester is formed between substrate and enzyme. In the latter phase, this ester is hydrolyzed and the enzyme is regenerated. This illustrates the covalent catalysis of chymotrypsin.