Carboxypeptidase A is a metalloenzyme that plays a crucial role in protein digestion by catalyzing the hydrolysis of peptide bonds at the carboxyl-terminal end of proteins and peptides. It is primarily found in the pancreas and is involved in the digestive process by breaking down dietary proteins into smaller peptides and amino acids, which can then be absorbed by the body. This enzyme requires zinc ions for its activity, which are essential for its structural stability and catalytic function. Carboxypeptidase A exhibits specificity for aromatic and aliphatic amino acids, making it an important player in the digestive enzyme cascade. The enzyme is also characterized by its relatively high stability and activity across a range of pH levels, typically functioning optimally in the alkaline environment of the small intestine. Its activity can be influenced by various factors, including the presence of inhibitors or activators, and it has potential applications in biotechnology and medicine, particularly in the study of protein metabolism and the development of therapeutic agents.

Carboxypeptidase A

11075-17-5: Carboxypeptidase A1, Carboxypolypeptidase, Cpa 1, E.C. 3.4.12.2, E.C. 3.4.17.1, E.C. 3.4.2.1, carboxipeptidasa A, carboxypeptidase A from bovine pancreas stab.,  carboxypeptidase A-pmsf from*bovine pancreas type,  carboxypeptidase A type I from*bovine pancreas,  Carboxypeptidase�A, PMSF treated bovine pancreas, Carboxypeptidase A,  Carboxypeptidase A bovine pancreas

Carboxypeptidase A (EC 3.4.17.1) is an exopeptidase enzyme. It hydrolyzes peptide bonds of C-terminal residues with aliphatic or aromatic side-chains. One unit of Carboxypeptidase A will hydrolyze 1.0 μmole of hippuryl-L-phenylalanine per min at pH 7.5 and 25 °C.

CAS 11075-17-5: Carboxypeptidase A

Carboxypeptidase A from bovine pancreas

Ref: 3D-FC49792