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Chymotrypsin is an enzyme that breaks down proteins and is used to make medicine for various conditions. Learn about its effectiveness, safety, dosage, and interactions from WebMD. Chymotrypsin, a protease, is an enzyme that cleaves the carbonyl side of certain peptide bonds by both general acid-base catalysis, but primarily covalent catalysis. In this mechanism, a nucleophile becomes covalently attached to a substrate in a transition state with an acyl-enzyme. The protease cleaves proteins by a hydrolysis reaction, an addition of a water molecule. The double bond between the carbon and nitrogen strengthens its bond. Chymotrypsin is site specific and will only cleave ... Chymotrypsin is an enzyme that degrades human trypsin enzymes and trypsinogen isoforms with high specificity, and mutations in the chymotrypsin C gene (CTRC) can lead to impaired enzyme activity, contributing to conditions such as chronic pancreatitis. Consider the mechanism of catalysis of the enzyme known as chymotrypsin. Found in our digestive system, chymotrypsin’s catalytic action is cleaving peptide bonds in proteins and it uses the …