Enterokinase

Enterokinase (also known as Enteropeptidase) is an enzyme produced by cells of the duodenum and involved in human digestion. It plays a crucial role in the digestive process by converting trypsinogen, a zymogen, into its active form trypsin.

Function

Enterokinase is secreted from the duodenal mucosa into the lumen of the small intestine, where it activates trypsinogen by cleaving it to form trypsin. This reaction is the key step in the activation of the pancreatic digestive enzymes.

Structure

Enterokinase is a type of serine protease, which is a group of enzymes that cleave peptide bonds in proteins. It is composed of two subunits, a heavy chain and a light chain, which are bound together by a disulfide bond.

Clinical significance

Deficiency in enterokinase can lead to a condition known as enterokinase deficiency, which is characterized by severe protein malnutrition. This condition is extremely rare and is usually diagnosed in infancy.

See also

• Digestive enzyme
• Duodenum
• Serine protease
• Trypsin
• Trypsinogen

References

Enterokinase Resources
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