[6] The inert function of digestive enzymes within the pancreas was known, as compared to their potent activity within the intestine, but the basis of this difference was unknown.

In 1899, Pavlov's student, N. P. Schepowalnikov, demonstrated that canine duodenal secretions dramatically stimulated the digestive activity of pancreatic enzymes, especially trypsinogen.

[8] Enteropeptidase is a type II transmembrane serine protease (TTSP) localized to the brush border of the duodenal and jejunal mucosa and synthesized as a zymogen, proenteropeptidase, which requires activation by duodenase or trypsin.

Once activated, TTSPs are predicted to remain membrane-bound through a conserved disulfide bond linking the pro- and catalytic domains.

[11] The detected apparent mass of about 160 kDa is consistent with the specified carbohydrate content of 30 - 40%, with equal amounts of neutral and amino sugars.

However, the isolated light chain is subtle whether prepared by limited reduction of the natural protein[16] or by mutagenesis and expression in COS cells.

Despite its alternative name (enterokinase), enteropeptidase is a serine protease that catalyses the hydrolysis of peptide bonds in proteins and, unlike other kinases, does not catalyze transfer of phosphate groups.

Some nonsense and frameshift mutations in this gene lead to a rare recessive disorder characterised by severe failure to thrive in affected infants, due to enteropeptidase deficiency.