Where Does Chymotrypsin Cleave in a Peptide Sequence

It uses an active serine residue to perform hydrolysis on the C-terminus of the aromatic amino acids of other proteins. Chymotrypsin is a protease enzyme that cleaves on the C-terminal phenylalanine (F), tryptophan (W), and tyrosine (Y) on peptide chains.

Does chymotrypsin break peptide bonds?

Chymotrypsin cleaves peptide bonds by attacking the unreactive carbonyl group with a powerful nucleophile, the serine 195 residue located in the active site of the enzyme, which briefly becomes covalently bonded to the substrate, forming an enzyme-substrate intermediate.

Where does peptide cleavage occur?

The cleavage mediated by the signal peptidase occurs on the carboxyl terminal side of small, uncharged amino acids like Ala, Gly and Ser.