Enterokinase

Enterokinase, also known as enteroprotease (E.C. 3.4.21.9), is a key enzyme in the digestion of dietary proteins in the small intestine. It catalyzes the activation of trypsinogen by removing six amino acids from the amino terminus of the 229-residue protein and does so with extremely high specificity. The resulting trypsin then activates all the other pancreatic proenzymes, as part of a two-step proteolytic cascade that is essential for proper digestion.

Enterokinase is a serine proteinase of the trypsin family and with trypsin-like specificity (1). It is synthesized in the epithelial cells of the duodenum and appears to be an intrinsic membrane protein located on the outer surface of the intestinal brush border. In fact, it is generated from a 1019-residue precursor that is proteolytically cleaved to a 235-residue light chain, which resembles trypsin and has the serine proteinase catalytic triad, plus a 784-residue heavy chain (2); the two chains are linked by a disulfide bond (3). In this regard, its properties are like those of the blood-clotting enzymes (4).

It should be noted that the term kinase is normally used to denote an enzyme that catalyzes the transfer of a phosphate group from a donor, such as ATP, to a receptor, such as glucose. In this regard, enterokinase has been misnamed. It does not catalyze phosphate transfer at all and, hence, is more appropriately called enteropeptidase .

References

1. A. Light and H. Janska (1989) Trends Biochem. Sci. 14, 110–112. 

2. Y. Kitamoto, R. A. Viele, H. Donis-Keller, and J. E. Sadler (1995) Biochemsitry 34, 4562–4568.

3. A. Light and P. Fonseca (1984) J. Biol. Chem. 259, 13195–13198. 

4. L. E. Anderson, K. A. Walsh, and H. Neurath (1977) Biochemistry 16, 3354–3360.