enterokináz

Enterokinase, also known as enteropeptidase, is a digestive enzyme produced by cells in the duodenum, the first part of the small intestine. It plays a crucial role in protein digestion by activating trypsinogen, an inactive precursor of the enzyme trypsin. Trypsin itself is a key enzyme in the digestive process, responsible for breaking down proteins into smaller peptides.

The synthesis of enterokinase occurs in the brush border of duodenal enterocytes. It is then released into the intestinal lumen. Upon encountering trypsinogen, enterokinase cleaves a specific peptide bond, converting it into its active form, trypsin. This initial activation is critical because trypsin then goes on to activate other pancreatic proteases, such as chymotrypsinogen, proelastase, and procarboxypeptidase, as well as further molecules of trypsinogen. This cascade amplifies the digestive process, ensuring efficient breakdown of dietary proteins.

A deficiency in enterokinase can lead to severe malabsorption of proteins, resulting in malnutrition, failure to thrive, and other serious health issues. Genetic mutations affecting the enterokinase gene (PRSS12) are the cause of congenital enterokinase deficiency. Treatment for this rare condition typically involves oral enzyme replacement therapy.