Structural highlights
Disease
[ENTK_HUMAN] Congenital enteropathy due to enteropeptidase deficiency. The disease is caused by mutations affecting the gene represented in this entry.
Function
[ENTK_HUMAN] Responsible for initiating activation of pancreatic proteolytic proenzymes (trypsin, chymotrypsin and carboxypeptidase A). It catalyzes the conversion of trypsinogen to trypsin which in turn activates other proenzymes including chymotrypsinogen, procarboxypeptidases, and proelastases.
Publication Abstract from PubMed
The highly specific serine protease human enteropeptidase light chain (hEPl) cleaves the Asp(4) Lys recognition sequence and represents an interesting enzyme for biotechnological applications. The human enzyme shows 10-times faster kinetics compared to other animal sources but low solubility under low salt conditions, which hampers protein production and crystallization. Therefore, a supercharged variant (N6D/G21D/G22D/N142D/K210E/C112S) with increased solubility was used for crystallization. The structure (1.9A resolution) displays a typical alpha/beta trypsin-like serine protease-fold. The mutations introduced for protein supercharging generate larger clusters of negative potential on both sites of the active cleft but do not affect the structural integrity of the protein. Proteins 2012. (c) 2012 Wiley-Liss, Inc.
Crystal structure of a supercharged variant of the human enteropeptidase light chain.,Simeonov P, Zahn M, Strater N, Zuchner T Proteins. 2012 Apr 10. doi: 10.1002/prot.24084. PMID:22488687[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Simeonov P, Zahn M, Strater N, Zuchner T. Crystal structure of a supercharged variant of the human enteropeptidase light chain. Proteins. 2012 Apr 10. doi: 10.1002/prot.24084. PMID:22488687 doi:10.1002/prot.24084
