Trypsin cleaves
Activation of zymogens: Enteropeptidase (formerly called enterokinase), an enzyme synthesized by and present on the luminal surface of intestinal mucosal cells of the brush border membrane, conves the pancreatic zymogen trypsinogen to trypsin by removal of a hexapeptide from the N-terminus of trypsinogen. Trypsin subsequently conves other trypsinogen molecules to trypsin by cleaving a limited number of specific peptide bonds in the zymogen. Enteropeptidase, thus, unleashesa cascade of proteolytic activity because trypsin is the common activator of all thepancreatic zymogens .
Arginine
Glutamate
Lysine
Proline
Structure and function of protein