karboksipeptidaasia

Karboksipeptidaasi is an enzyme that catalyzes the hydrolysis of a peptide bond at the carboxyl end of a protein or peptide. This means it cleaves amino acids one by one from the C-terminus of a polypeptide chain. These enzymes are classified as hydrolases, specifically peptidases, and are further categorized as carboxypeptidases.

Carboxypeptidases play a vital role in protein digestion and metabolism in many organisms. In humans, for example, pancreatic carboxypeptidase A and B are secreted into the small intestine to break down dietary proteins into smaller peptides and free amino acids, which can then be absorbed. Carboxypeptidase A primarily cleaves aromatic and aliphatic amino acids, while carboxypeptidase B is specific for basic amino acids like lysine and arginine.

Beyond digestion, carboxypeptidases are involved in various cellular processes. They can participate in protein turnover, modifying or inactivating specific proteins, and are also important in the synthesis of certain hormones and neuropeptides. Some carboxypeptidases are membrane-bound and have roles in cell signaling and adhesion. The activity of these enzymes is often regulated to ensure proper protein processing and homeostasis.