exopeptidase
Sign in to saveAlso known as exopeptidases
An exopeptidase is any peptidase that catalyzes the cleavage of the terminal (or the penultimate) peptide bond; the process releases a single amino acid, dipeptide or a tripeptide from the peptide chain. Depending on whether the amino acid is released from the amino or the carboxy terminal (N-terminus or C-terminus), an exopeptidase is further classified as an aminopeptidase or a carboxypeptidase, respectively. Thus, an aminopeptidase, an enzyme in the brush border of the small intestine, will cleave a single amino acid from the amino terminal, whereas carboxypeptidase, which is a digestive en
Research
54,748 papers- Engineered nanopores for exopeptidase protein sequencing.Nature methods · 2024
- Exopeptidase Assisted N- and C-Terminal Proteome Sequencing.Analytical chemistry · 2020
- Exopeptidase combination enhances the degradation of isotopically labelled gluten immunogenic peptides in humans.Frontiers in immunology · 2024
- Review Article: Novel Enzyme Therapy Design for Gluten Peptide Digestion Through Exopeptidase Supplementation.Alimentary pharmacology & therapeutics · 2025
- Exopeptidase treatment combined with Maillard reaction modification of protein hydrolysates derived from porcine muscle and plasma: Structure-taste relationship.Food chemistry · 2020
via PubMed
~1 min read
Encyclopedic overview
3 sectionsContents
- See also
- External links
- References
An exopeptidase is any peptidase that catalyzes the cleavage of the terminal (or the penultimate) peptide bond; the process releases a single amino acid, dipeptide or a tripeptide from the peptide chain. Depending on whether the amino acid is released from the amino or the carboxy terminal (N-terminus or C-terminus), an exopeptidase is further classified as an aminopeptidase or a carboxypeptidase, respectively. Thus, an aminopeptidase, an enzyme in the brush border of the small intestine, will cleave a single amino acid from the amino terminal, whereas carboxypeptidase, which is a digestive enzyme present in pancreatic juice, will cleave a single amino acid from the carboxylic end of the peptide.
Some examples of exopeptidases include: Carboxypeptidase A - cleaves C-terminal Phe, Tyr, Trp, or Leu Carboxypeptidase B - cleaves C-terminal Lys or Arg Aminopeptidase - cleaves any N-terminal amino acid Prolinase - cleaves N-terminal Pro from dipeptides Prolidase - cleaves C-terminal Pro from dipeptides
Excerpted from Wikipedia’s “exopeptidase” article, available under the CC BY-SA 4.0 licence.