Enterokinase

Enterokinase (pronounced: en-ter-o-ki-nase), also known as Enteropeptidase, is an enzyme that plays a crucial role in the human digestive system. Its primary function is to activate trypsinogen by cleaving it to form trypsin, which in turn activates other pancreatic enzymes.

Etymology

The term "Enterokinase" is derived from the Greek words "enteron" meaning intestine, and "kinase" meaning to move. This is reflective of the enzyme's role in the digestive process, which primarily takes place in the small intestine.

Function

Enterokinase is secreted by the cells of the duodenum, the first section of the small intestine. It is responsible for the conversion of trypsinogen, an inactive enzyme, into its active form, trypsin. This process is vital for the digestion of proteins in the diet. Trypsin then activates other pancreatic enzymes, such as chymotrypsinogen, procarboxypeptidase, and proelastase, which further aid in protein digestion.

Clinical Significance

Deficiency or malfunction of enterokinase can lead to protein malnutrition and malabsorption syndrome, due to the inability to properly digest proteins. In the medical field, enterokinase is used in the laboratory for the cleavage of fusion proteins.

Related Terms

• Trypsinogen
• Trypsin
• Duodenum
• Protein malnutrition
• Malabsorption syndrome

External links

• Medical encyclopedia article on Enterokinase
• Wikipedia's article - Enterokinase

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