Carboxypeptidase
Carboxypeptidase — An exopeptidase that cleaves amino acids from the C-terminus of a peptide chain, used in C-terminal sequencing and peptide processing studies.
What Is a Carboxypeptidase?
A carboxypeptidase is an exopeptidase that removes amino acid residues sequentially from the C-terminus of a peptide. Carboxypeptidases are classified as metalloenzymes (CPA, CPB) or serine proteases (CPDS). C-terminal amidation and D-amino acid substitution block carboxypeptidase activity.
Key Carboxypeptidases
- Carboxypeptidase E: Removes C-terminal basic residues during prohormone processing
- CPA: Prefers hydrophobic C-terminal residues. Used for C-terminal sequencing
- CPB: Prefers basic C-terminal residues (Arg, Lys)
Frequently Asked Questions
What is Carboxypeptidase?
An exopeptidase that cleaves amino acids from the C-terminus of a peptide chain, used in C-terminal sequencing and peptide processing studies.
Why is Carboxypeptidase important in peptide research?
Carboxypeptidase 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
- Carboxypeptidase on Wikipedia
- Search Carboxypeptidase on PubChem (NIH)
- Research articles on ScienceDirect