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Updated: Jun 22, 2026
X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050
Published on: May 13, 2020
Enteropeptidase, a type II transmembrane serine protease.
X Long Zheng1, Yasunori Kitamoto, J Evan Sadler
1Department of Pathology and Laboratory Medicine, The Children's Hospital of Philadelphia and The University of Pennsylvania School of Medicine, Philadelphia, PA 19104, USA. zheng@email.chop.edu
Enteropeptidase initiates digestion by activating trypsinogen. Its deficiency causes severe digestive issues, while its reflux can lead to pancreatitis, underscoring its critical role in gut health.
Area of Science:
- Gastroenterology
- Biochemistry
- Molecular Biology
Background:
- Enteropeptidase is a serine protease found in the small intestine's brush border.
- It is synthesized as an inactive zymogen, proenteropeptidase, requiring activation by other proteases.
- Enteropeptidase plays a crucial role in activating digestive enzymes.
Purpose of the Study:
- To elucidate the function and clinical significance of enteropeptidase.
- To understand the consequences of enteropeptidase deficiency and reflux.
Main Methods:
- The abstract does not specify methods, focusing on biological function and clinical manifestations.
- Information is based on established knowledge of enzyme activation cascades and disease pathology.
Main Results:
- Enteropeptidase activates trypsinogen to trypsin, which then activates other pancreatic zymogens.
- Congenital enteropeptidase deficiency leads to severe maldigestion, including diarrhea, failure to thrive, hypoproteinemia, and edema.
- Duodenopancreatic reflux of active enteropeptidase is implicated in acute and chronic pancreatitis.
Conclusions:
- Enteropeptidase is essential for initiating intestinal digestion and maintaining protein homeostasis.
- Disruptions in enteropeptidase activity have significant clinical consequences, ranging from malabsorptive disorders to pancreatic inflammation.
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