Karboxypeptidaasi

Karboxypeptidase is an enzyme that catalyzes the hydrolysis of the carboxyl-terminal amino acid from a peptide or protein chain. This process involves the cleavage of the peptide bond between the carboxyl-terminal amino acid and the preceding amino acid, releasing the terminal amino acid as a free amino acid. Karboxypeptidases are classified into two main types based on their mechanism of action: metallo- and serine karboxypeptidases. Metallo-karboxypeptidases require a metal ion, typically zinc, for their catalytic activity, while serine karboxypeptidases use a serine residue in their active site.

These enzymes play crucial roles in various biological processes, including protein degradation, signal transduction, and the regulation of peptide hormones. They are found in a wide range of organisms, from bacteria to humans, and are involved in both intracellular and extracellular environments. Karboxypeptidases are also of significant interest in the field of drug design, as they can be targeted to inhibit specific biological processes.

The study of karboxypeptidases has contributed to our understanding of protein structure, function, and degradation. Their role in the hydrolysis of peptide bonds makes them valuable tools in biochemistry and molecular biology research. Additionally, the inhibition of karboxypeptidases has potential applications in the treatment of various diseases, including cancer and neurodegenerative disorders.