karboxypeptidaasigeenejä

Carboxypeptidase is a type of exopeptidase enzyme that catalyzes the hydrolysis of peptide bonds at the carboxyl-terminal end of a protein or peptide. This means it cleaves amino acids one by one from the C-terminus. Carboxypeptidases are crucial in various biological processes, including protein digestion, protein turnover, and the regulation of peptide hormone activity.

There are two main classes of carboxypeptidases: metallocarboxypeptidases and serine carboxypeptidases. Metallocarboxypeptidases require a metal ion, typically zinc, for their catalytic activity. Examples include carboxypeptidase A and carboxypeptidase B, which are important digestive enzymes found in the pancreas. Carboxypeptidase A primarily cleaves aromatic and aliphatic amino acids from the C-terminus, while carboxypeptidase B preferentially cleaves basic amino acids like arginine and lysine.

Serine carboxypeptidases, on the other hand, utilize a catalytic triad involving a serine residue for their enzymatic action. These are less common than their metallocarboxypeptidase counterparts. Carboxypeptidases play significant roles in maintaining homeostasis by breaking down excess or inactivated peptides. Their activity is tightly regulated to prevent premature degradation of essential proteins. Dysfunctions in carboxypeptidase activity can lead to various medical conditions.