Carboxypeptidase

Carboxypeptidase refers to a family of enzymes that catalyze the hydrolysis of peptide bonds at the carboxyl-terminal (C-terminal) end of proteins and peptides, removing single amino acids and playing essential roles in protein digestion, maturation, and regulation of hormones and neuropeptides[1][4][6]. These enzymes are classified mainly as metallocarboxypeptidases, typically requiring a zinc ion for activity, and occur in numerous forms including carboxypeptidase A, B, E, and O, among others[2][3]. Their functions span digestion (especially pancreatic isoforms), post-translational modification of proteins, blood clotting regulation, neuropeptide biosynthesis, and extracellular matrix remodeling[1][2][6]. Mutations or dysregulation of specific carboxypeptidases are implicated in diseases such as obesity (carboxypeptidase E), epilepsy (carboxypeptidase A6), neurodegeneration, and certain cancers[6]. Carboxypeptidase enzymes are exploited as drug targets, most notably in the development of ACE inhibitors for hypertension, demonstrating the therapeutic relevance of this enzyme family[2]. Note: "Carboxypeptidases" is a plural and family-level designation, not a single, specific molecular entity. For structured informatics or pharmacological purposes, further specification to a unique isoenzyme (e.g., "Carboxypeptidase A1," "Carboxypeptidase E") is recommended for accuracy and actionable data[1][2].

Other names

CarboxypeptidasesCPCarboxypeptidase A (CPA)Carboxypeptidase B (CPB)Carboxypeptidase E (CPE)Carboxypeptidase O (CPO)Cytosolic carboxypeptidase (CCP)Mast cell carboxypeptidase (MCCPA)Plasma carboxypeptidase B2

Inhibition of C-terminal amino acid cleavage, Modulation of neuropeptide and hormone maturation, Antagonism of digestive function