Enteropeptidase
Enteropeptidase — A serine protease in the duodenum that activates trypsinogen by cleaving a specific peptide bond, initiating the digestive enzyme cascade.
What Is Enteropeptidase?
Enteropeptidase (enterokinase) is a serine protease in the duodenal brush border that cleaves the activation peptide from trypsinogen, generating active trypsin. The enteropeptidase recognition sequence (DDDDK↓) is used as a fusion protein cleavage site to release recombinant peptides from fusion tags after purification.
Applications
- Tag removal: Cleave His-tag or other fusion partners at DDDDK↓ site. Leaves native N-terminus
- Specificity: Highly specific for DDDDK sequence. Minimal non-specific cleavage
- Cost: More expensive than TEV or thrombin proteases but leaves no extra residues
Frequently Asked Questions
What is Enteropeptidase?
A serine protease in the duodenum that activates trypsinogen by cleaving a specific peptide bond, initiating the digestive enzyme cascade.
Why is Enteropeptidase important in peptide research?
Enteropeptidase is a fundamental concept in biochemistry as it relates to peptide science. It directly influences experimental design, compound characterization, and the reliability of research outcomes across biochemistry and molecular biology disciplines.
Authority Sources
- Enteropeptidase on Wikipedia
- Search Enteropeptidase on PubChem (NIH)
- Research articles on ScienceDirect