Trypsin cleaves the peptide bond on the carboxyl side of basic amino acids such as arginine and lysine.
Enteropeptidase is produced by the mucosa of duodenum and it cleaves the peptide bond of trypsinogen after residue 15, which is a lysine.
Trypsin is produced, stored and released as the inactive trypsinogen to ensure that the protein is only activated in the appropriate location.
Premature trypsin activation can be destructive and may trigger a series of events that lead to pancreatic self-digestion.
Trypsinogen is stored in intracellular vesicles in the pancreas called zymogen granules whose membranous walls are thought to be resistant to enzymatic degradation.
A mutation at Arg 117, a trypsin-sensitive site, in cationic trypsinogen has been implicated in hereditary pancreatitis, a rare form of early-onset genetic disorder.