Enteropeptidase
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| Crystal structure of Enteropeptidase with an inhibitor | |
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protease, serine, 7 (enteropeptidase)
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| Identifiers | |
| Symbol | PRSS7 |
| Entrez | 5651 |
| HUGO | 9490 |
| OMIM | 606635 |
| RefSeq | NM_002772 |
| UniProt | P98073 |
| Other data | |
| Locus | Chr. 21 q21 |
Enteropeptidase (previously 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 3.4.21.9). Enteropeptidase is a part of the Chymotrypsin-clan of serine proteases, and is structurally similar to these proteins.
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[edit] Reaction
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. [1]
[edit] Nomenclature
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.
[edit] Genetics
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.[2]
[edit] References
- ^ Enterokinase, light chain (P8070), Proteases, NEB. Retrieved on 2007-10-04.
- ^ Holzinger A, Maier EM, Bück C, et al (2002). "Mutations in the proenteropeptidase gene are the molecular cause of congenital enteropeptidase deficiency". Am. J. Hum. Genet. 70 (1): 20–5. PMID 11719902.
[edit] External links
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