chymotrypsinë

Chymotrypsin is a digestive enzyme that breaks down proteins. It is produced in the pancreas as an inactive precursor called chymotrypsinogen, which is then activated in the small intestine. Chymotrypsin functions by cleaving peptide bonds, specifically at the carboxyl side of aromatic amino acids like tyrosine, tryptophan, and phenylalanine. This enzymatic activity is crucial for the digestion and absorption of dietary proteins.

The structure of chymotrypsin is a globular protein composed of two polypeptide chains linked by disulfide bonds. Its active site contains a catalytic triad, consisting of serine, histidine, and aspartate residues, which are essential for its enzymatic function. Chymotrypsin plays a significant role in the breakdown of proteins into smaller peptides, which can then be further processed by other proteases or absorbed by the intestinal lining.

In addition to its digestive role, chymotrypsin is also used therapeutically. It is sometimes administered to help break down inflammatory debris or to aid in wound healing. Research has also explored its potential in various medical applications, including the treatment of certain eye conditions. The study of chymotrypsin has provided valuable insights into enzyme mechanisms and protein structure.