kimotripsinë

Kimotripsinë is a serine protease that plays a significant role in protein digestion. It is synthesized in the pancreas as an inactive precursor called chymotrypsinogen. This zymogen is then activated in the small intestine by trypsin, another digestive enzyme. Once activated, chymotrypsinë is a key enzyme responsible for breaking down proteins into smaller peptides. It specifically cleaves peptide bonds on the carboxyl side of aromatic amino acid residues, such as tyrosine, phenylalanine, and tryptophan. This enzymatic activity is crucial for the absorption of amino acids and small peptides by the body. Besides its digestive function, chymotrypsinë is also involved in other physiological processes, including blood clotting and the breakdown of certain proteins in the immune system. Its activity is regulated to prevent damage to the digestive tract. The enzyme's structure and catalytic mechanism are well-studied, making it a model enzyme in biochemistry. Understanding kimotripsinë's function is essential for comprehending protein metabolism and related digestive disorders.