Karboxipeptidaasin

Karboxipeptidaasin is a type of enzyme that catalyzes the hydrolysis of peptide bonds. Specifically, it acts by cleaving amino acids from the carboxyl terminus of a peptide chain. This enzymatic activity is crucial in various biological processes, including protein digestion and the regulation of peptide hormone levels.

These enzymes are broadly classified into two main groups: serine carboxypeptidases and metallo-carboxypeptidases. Serine carboxypeptidases utilize a serine residue in their active site for catalysis, while metallo-carboxypeptidases require a metal ion, typically zinc, for their function. The specific amino acid sequence and three-dimensional structure of the enzyme determine its substrate specificity and catalytic efficiency.

In the digestive system, carboxypeptidases play a significant role in breaking down dietary proteins into smaller peptides and amino acids that can be absorbed by the body. For instance, carboxypeptidase A and B are secreted by the pancreas into the small intestine to aid in this process. Beyond digestion, carboxypeptidases are involved in metabolic pathways, cellular signaling, and the processing of neuropeptides. Dysregulation of carboxypeptidase activity has been linked to various diseases, making them targets for therapeutic intervention. Research continues to explore the diverse roles of these enzymes in health and disease.