Alpha-chymotrypsin (α-Chymotrypsin)

Alpha-chymotrypsin is a serine protease enzyme produced in the pancreas as an inactive precursor (chymotrypsinogen) and activated in the duodenum by trypsin cleavage. It catalyzes the hydrolysis of peptide bonds on the carboxyl side of large hydrophobic amino acids such as phenylalanine, tryptophan, and tyrosine, playing a critical role in protein digestion. Structurally, it is characterized by three peptide chains held together by disulfide bonds and a catalytic triad (serine, histidine, aspartate) that orchestrates nucleophilic attack on peptide substrates. Besides its digestive role, alpha-chymotrypsin is used therapeutically as an anti-inflammatory and proteolytic agent in surgery, particularly ophthalmic procedures. Loss of enzyme activity can occur due to denaturation from heat or pH changes, and allergic or irritant reactions may rarely limit its clinical use[1][2][3][4][5][7].

Other names

ChymotrypsinChymotrypsin AChymotrypsin BChymarAlpha-chymarChymotestQuimarQuimotraseEnzeonOphthAvazymeα-Chy

Proteolytic cleavage of peptide bonds C-terminal to aromatic amino acids (tyrosine, tryptophan, phenylalanine) in proteins and polypeptides, via a covalent hydrolysis (ping-pong) mechanism involving a catalytic triad (Ser195, His57, Asp102)[1][2][3][5]