Enteropeptidase was first discovered by Ivan Pavlov, a renowned physiologist who was awarded the Nobel Prize in Physiology or Medicine in 1904 for his studies on gastrointestinal physiology . Pavlov’s student, N. P. Schepowalnikov, demonstrated that duodenal secretions could activate pancreatic proteolytic enzymes, leading to the identification of enteropeptidase as a key activator of these enzymes .
Enteropeptidase is a type II transmembrane serine protease localized to the brush border of the duodenal and jejunal mucosa . It is synthesized as a zymogen (proenteropeptidase) that requires activation by another protease, such as trypsin or duodenase . The enzyme consists of a disulfide-linked heavy chain (82-140 kDa) that anchors it to the intestinal brush border membrane and a light chain (35-62 kDa) that contains the catalytic subunit .
The primary function of enteropeptidase is to convert trypsinogen, an inactive zymogen, into its active form, trypsin . This activation is crucial because trypsin, in turn, activates other pancreatic digestive enzymes, facilitating the breakdown of proteins in the small intestine .
Enteropeptidase is essential for proper digestion and nutrient absorption. In the absence of this enzyme, the activation of trypsinogen is impaired, leading to significant digestive issues . The enzyme’s activity ensures that digestive enzymes are activated only in the intestine, preventing premature activation that could damage the pancreas and other tissues .
Extensive research has been conducted on enteropeptidase, focusing on its structure, function, and role in various physiological processes . Studies have also explored the enzyme’s involvement in certain disorders and potential inhibitors that could modulate its activity . Understanding enteropeptidase’s mechanisms and interactions can provide insights into developing therapeutic interventions for digestive disorders and other related conditions .