Chymotrypsinin

Chymotrypsin is a digestive enzyme that functions by cleaving peptide bonds in proteins. It is synthesized in the pancreas as an inactive precursor called chymotrypsinogen A. Upon activation by the enzyme trypsin in the small intestine, chymotrypsinogen A undergoes a conformational change and becomes active chymotrypsin. This enzyme is a serine protease, meaning it has a serine residue in its active site that is crucial for its catalytic activity.

Chymotrypsin plays a vital role in protein digestion by breaking down dietary proteins into smaller peptides, which can then be further processed by other proteases or absorbed. Its specificity lies in its ability to hydrolyze peptide bonds on the carboxyl side of aromatic amino acids such as tyrosine, tryptophan, and phenylalanine. This targeted cleavage contributes to the efficient breakdown of complex protein structures.

Beyond its digestive function, chymotrypsin has found applications in various medical and biotechnological fields. It is used therapeutically to help break down abnormal protein deposits, such as in wound debridement and the treatment of certain inflammatory conditions. In research and industry, chymotrypsin is employed in protein purification, peptide synthesis, and as a reagent in biochemical assays. The precise mechanism and broad utility of chymotrypsin highlight its significance in both biological processes and scientific applications.