chymotrypsiin

Chymotrypsin is a digestive enzyme that belongs to the serine protease family. It is produced in the pancreas as an inactive zymogen, chymotrypsinogen, and then activated in the small intestine. Its primary role is to break down proteins into smaller peptides. Chymotrypsin specifically cleaves peptide bonds on the carboxyl side of aromatic amino acids like tyrosine, tryptophan, and phenylalanine. This enzymatic activity is crucial for protein digestion, allowing the body to absorb amino acids and use them for various biological functions. The activation of chymotrypsinogen involves the removal of a small peptide segment by the enzyme trypsin. This activation process ensures that the enzyme is only active within the digestive tract, preventing self-digestion of pancreatic tissues. Chymotrypsin is also used therapeutically, often in formulations for wound healing and to reduce inflammation, due to its protein-degrading properties. Its mechanism involves a catalytic triad of amino acids within its active site, characteristic of serine proteases.