Karboksipeptidaasi

Karboksipeptidaza, also known as carboxypeptidase, is an enzyme that catalyzes the hydrolysis of peptide bonds at the carboxyl (C) terminus of a polypeptide chain. This process involves the removal of a single amino acid residue from the end of the peptide, releasing a free amino acid and a shorter peptide. Carboxypeptidases are classified into two main groups based on their mechanism of action: metallo-carboxypeptidases, which require a metal ion such as zinc for activity, and serine carboxypeptidases, which use a serine residue in their active site.

These enzymes play crucial roles in various biological processes, including protein degradation, peptide synthesis, 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. Carboxypeptidases are also important in biotechnology and medicine, where they are used in the production of peptides and proteins, and in the treatment of certain diseases.

The structure and function of carboxypeptidases have been extensively studied, and their mechanisms of action are well understood. However, ongoing research continues to uncover new aspects of their biology and potential applications.