Is Activated by Enterokinase?

Enterokinase is produced by the duodenal mucosa. It activates trypsin, a pancreatic proteolytic enzyme, which in turn activates the remainder of the enzymes facilitating protein digestion. The pancreas releases other proteolytic enzymes into the intestine that continue the digestive process.

Which enzyme activates enterokinase?

The amino acid sequence surrounding the amino terminus of the enterokinase light chain is ITPK-IVGG (human) or VSPK-IVGG (bovine), suggesting that single-chain enterokinase is activated by an unidentified trypsin-like protease that cleaves the indicated Lys-Ile bond.

Is trypsinogen activated by enterokinase?

Trypsinogen is activated by enterokinase, which cleaves an amino-terminal activation peptide (TAP). Active trypsin then cleaves and activates all of the other pancreatic proteases, a phospholipase, and colipase, which is necessary for the physiological action of pancreatic triglyceride lipase.