Name=protease, serine, 7 (enteropeptidase)
caption=Crystal structure of Enteropeptidase with an inhibitor


Enteropeptidase (also called enterokinase) is an enzyme involved in human digestion. It is produced by cells in the duodenum wall, and is secreted from duodenum's glands, the crypts of Lieberkühn, whenever ingested food enters the duodenum from the stomach. Enteropeptidase has the critical job of turning trypsinogen (a zymogen) to trypsin, indirectly activating a number of pancreatic digestive enzymes.

Enteropeptidase is a serine protease enzyme (EC number| Enteropeptidase is a part of the Chymotrypsin-clan of serine proteases, and is structurally similar to these proteins.


The reaction catalysed by Enteropeptidase:

trypsinogen → trypsin + octapeptide

Enteropeptidase cleaves after Lysine if the Lys is preceded by four Asp and not followed by a Pro. [cite web|url=http://www.neb.com/nebecomm/products/productP8070.asp|title=Enterokinase, light chain (P8070), Proteases, NEB|accessdate=2007-10-04]


Despite its older name of "enterokinase", the enzyme is not a kinase. This is because enteropeptidase alters the degree of enzymatic activity its substrate expresses though a proteolytic cleavage reaction. A kinase would do the same by phosphorylation reaction.


Enteropeptidase is encoded by the "PRSS7" (serine protease-7 gene) or "ENTK" gene on the 21st chromosome (21q21).

Isolated cases of enteropeptidase deficiency have been reported. [cite journal |author=Holzinger A, Maier EM, Bück C, "et al" |title=Mutations in the proenteropeptidase gene are the molecular cause of congenital enteropeptidase deficiency |journal=Am. J. Hum. Genet. |volume=70 |issue=1 |pages=20–5 |year=2002 |pmid=11719902 |doi=]


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