<Tr> <Th> PMC </Th> <Td> articles </Td> </Tr> <Tr> <Th> PubMed </Th> <Td> articles </Td> </Tr> <Tr> <Th> NCBI </Th> <Td> proteins </Td> </Tr> <P> Chymotrypsin (EC 3.4. 21.1, 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 side chain of the amino acid N - terminal to the scissile amide bond (the P position) is a large hydrophobic amino acid (tyrosine, tryptophan, and phenylalanine). These amino acids contain an aromatic ring in their side chain 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 side chain 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 . </P>

Using enzyme catalysis explain the action of chemotrypsin