Carboxypeptidase A

Carboxypeptidase A (EC 3.4.2.1), a zinc-containing metalloprotease, catalyzes the hydrolysis of peptide bonds near the C-terminal end of polypeptides and is frequently utilized in biochemical research. As a prototypical enzyme for metalloproteases, it is essential in biological systems [1].

Bz-Ala-Arg, a dipeptide, serves as a spectrophotometric substrate (0.4 M pyridine formate, pH 4.25) for human pancreatic carboxypeptidase B and plasma carboxypeptidase N. It is utilized to screen for competitive inhibitors of these enzymes [1].

FA-Ala-Arg is a dipeptide featuring a furylacryloyl group that degrades to yield arginine. It augments nitric oxide (NO) synthesis in MCF-7 cells through a mechanism in which cell-surface Carboxypeptidase-D (CPD) elevates intracellular arginine levels. Furthermore, FA-Ala-Arg promotes cell survival in prolactin (PRL)-treated cells wherein PRL modulates CPD mRNA levels [1].

Glycylglycylcysteine is an inhibitor of Thrombin Activatable Fibrinolysis Inhibitor (TAFI), exhibiting a K_i value of 0.99 µM and an IC_50 of 9.4 µM in TAFI substrate assays. TAFI, a basic carboxypeptidase, hinders fibrinolysis by cleaving C-terminal lysine residues on partially degraded fibrin [1].

Bradykinin (1-6) is an amino-truncated Bradykinin peptide and a stable metabolite of Bradykinin, cleaved by carboxypeptidase Y (CPY). This fragment of Bradykinin activates pain receptors and induces smooth muscle contraction.

Selective bradykinin B2 receptor agonist that is resistant to carboxypeptidase cleavage. 5-fold more potent and exhibits a more prolonged duration of action than bradykinin in vivo.