Karboksüpeptidaas

Karboksüpeptidaas is a type of enzyme that catalyzes the hydrolysis of a peptide bond at the carboxyl-terminal end of a protein or peptide. This means it removes amino acids one by one from the C-terminus of a polypeptide chain. Karboksüpeptidaases are exopeptidases, a subclass of peptidases that cleave amino acids from the end of a peptide rather than from within the chain, which is characteristic of endopeptidases.

These enzymes play crucial roles in various biological processes, including protein degradation, peptide processing, and the activation or inactivation of peptide hormones and signaling molecules. For example, some karboksüpeptidaases are involved in the maturation of prohormones, cleaving off precursor fragments to release active peptide hormones. Others contribute to cellular housekeeping by breaking down damaged or unwanted proteins.

The activity of karboksüpeptidaases is often regulated to ensure precise control over peptide and protein turnover. Their substrate specificity can vary, with some enzymes acting on a broad range of peptides, while others are highly specific for particular amino acid sequences or types of peptides.

In research and biotechnology, karboksüpeptidaases can be utilized for protein sequencing, purification of peptides, and the synthesis of specific peptide fragments. Understanding the function and regulation of karboksüpeptidaases is important for comprehending cellular metabolism and for developing therapeutic strategies targeting proteolytic pathways.