Enteropeptidáz

Enteropeptidase, also known as enterokinase, is a digestive enzyme produced by cells of the duodenum. Its primary role is to activate trypsinogen, an inactive precursor of the enzyme trypsin, which is crucial for protein digestion. Enteropeptidase cleaves a specific peptide bond in trypsinogen, converting it into its active form, trypsin. Trypsin then plays a central role in the digestive cascade, activating other pancreatic zymogens like chymotrypsinogen, procarboxypeptidase, and proelastase, all of which are essential for breaking down dietary proteins into absorbable amino acids and small peptides.

The synthesis of enteropeptidase occurs in the duodenal enterocytes, the cells lining the small intestine. It is secreted into the lumen of the duodenum, where it encounters trypsinogen secreted by the pancreas. This activation is a vital step, as trypsinogen itself cannot activate other pancreatic proteases. Once trypsin is formed, it can autocatalytically activate more trypsinogen, amplifying the digestive process. Deficiencies in enteropeptidase can lead to severe malabsorption and protein malnutrition, highlighting its critical importance in nutrient processing. Therapeutic applications are being explored for conditions involving insufficient digestive enzyme activity.