Enteropeptidase

Enteropeptidase (also known as enterokinase) is an enzyme produced by cells of the duodenum and involved in human digestion. It is secreted from the duodenal brush border and functions to convert trypsinogen (a zymogen) into its active form trypsin, resulting in the subsequent activation of pancreatic digestive enzymes.

Function

Enteropeptidase is a key enzyme in digestion, as it activates trypsinogen by cleaving it to form trypsin. This reaction takes place in the lumen of the small intestine, specifically the duodenum, where enteropeptidase is secreted. Trypsin then goes on to activate other pancreatic enzymes, such as chymotrypsinogen, proelastase, and procarboxypeptidase, amplifying the digestive process.

Structure

Enteropeptidase is a type of serine protease, a group of enzymes that cleave peptide bonds in proteins. It is a heterodimer composed of two subunits, a heavy chain and a light chain, which are bound together by a disulfide bond. The heavy chain anchors the enzyme to the cell membrane, while the light chain is responsible for its enzymatic activity.

Clinical significance

Deficiency in enteropeptidase can lead to a condition known as enterokinase deficiency, which is characterized by severe protein malnutrition, failure to thrive, and diarrhea. This condition is extremely rare, with only a few cases reported in the medical literature.

See also

• Digestive enzyme
• Duodenum
• Serine protease
• Trypsin

References

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Enteropeptidase

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  Enteropeptidase structure
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  Human enteropeptidase light chain