Enteropeptidase
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| Enteropeptidase | |
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 Crystal structure of Enteropeptidase with an inhibitor |
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| Structure: | |
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| protein type: | Serine protease |
| Functions: | digestion |
| Domains: | serine protease domain |
| Diseases: | |
Enteropeptidase (previously also enterokinase) is a serine protease enzyme (EC 3.4.21.9) secreted by intestinal gland cells in the crypts of Lieberkühn in the small intestine. Enteropeptidase is a part of the Chymotrypsin-clan of serine proteases, and is structurally similar to these proteins. Enteropeptidase activates trypsinogen, a zymogen, to trypsin, indirectly activating a number of pancreatic digestive enzymes.
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[edit] Reaction
The reaction catalysed by Enteropeptidase:
trypsinogen → trypsin + octapeptide
[edit] Nomenclature
Despite its older name of enterokinase, the enzyme is not a kinase, since it activates its substrate by cleavage and not phosphorylation.
[edit] Genetics
Enteropeptidase is encoded by the PRSS7 (serine protease-7 gene) or ENTK gene on the 21st chromosome (21q21).
Isolated cases of enterokinase deficiency have been reported (OMIM).
[edit] External link
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