Chymotrypsin catalyzes the hydrolysis of peptide bonds. It employs a catalytic triad consisting of serine, histidine, and aspartate residues. The mechanism involves a nucleophilic attack by the serine residue on the carbonyl carbon of the peptide bond, forming a tetrahedral intermediate. This intermediate is stabilized by a structure known as the oxyanion hole, facilitating the breakdown of the peptide bond.
