Aminopeptidase
Aminopeptidase — An exopeptidase that cleaves amino acid residues from the N-terminus of a peptide chain, a major pathway of peptide degradation in vivo.
What Is an Aminopeptidase?
An aminopeptidase is an exopeptidase that removes amino acid residues sequentially from the N-terminus of a peptide. Aminopeptidases are a major cause of peptide degradation in vivo and in biological samples. N-terminal protection strategies (acetylation, D-amino acids, pyroglutamate) block aminopeptidase activity.
Key Aminopeptidases
- Aminopeptidase N (CD13): Broad-specificity membrane-bound enzyme. Tumor marker and drug target
- DPP-IV: Cleaves X-Pro/X-Ala dipeptides from N-terminus. Degrades GLP-1, GIP
- Leucine aminopeptidase: Prefers hydrophobic N-terminal residues
Frequently Asked Questions
What is Aminopeptidase?
An exopeptidase that cleaves amino acid residues from the N-terminus of a peptide chain, a major pathway of peptide degradation in vivo.
Why is Aminopeptidase important in peptide research?
Aminopeptidase 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
- Aminopeptidase on Wikipedia
- Search Aminopeptidase on PubChem (NIH)
- Research articles on ScienceDirect