Wiktionary
n. An endopeptidase enzyme that cleaves peptides at the carboxyl side of tyrosine, tryptophan, and phenylalanine amino acids.
Wikipedia
Chymotrypsin (, chymotrypsins A and B, alpha-chymar ophth, avazyme, chymar, chymotest, enzeon, quimar, quimotrase, alpha-chymar, alpha-chymotrypsin A, alpha-chymotrypsin) is a digestive enzyme component of pancreatic juice acting in the duodenum where it performs proteolysis, the breakdown of proteins and polypeptides. Chymotrypsin preferentially cleaves peptide amide bonds where the carboxyl side of the amide bond (the P position) is a large hydrophobic amino acid ( tyrosine, tryptophan, and phenylalanine). These amino acids contain an aromatic ring in their sidechain that fits into a ' hydrophobic pocket' (the S position) of the enzyme. It is activated in the presence of trypsin. The hydrophobic and shape complementarity between the peptide substrate P sidechain and the enzyme S binding cavity accounts for the substrate specificity of this enzyme. Chymotrypsin also hydrolyzes other amide bonds in peptides at slower rates, particularly those containing leucine and methionine at the P position.
Structurally, it is the archetypal structure for its superfamily, the PA clan of proteases.
Usage examples of "chymotrypsin".
Unstable molecular structure that breaks down in secondsjust time enough to make the human body go wild activating chymotrypsin enzymes.
Unstable molecular structure that breaks down in seconds—just time enough to make the human body go wild activating chymotrypsin enzymes.