Carboxypeptidase that possesses the specificities of both mammalian Cpase A and B. Thus shows broad substrate specificity, being able to cleave Cbz-Gly-Leu, Cbz-Gly-Val, Cbz-Gly-Phe, Cbz-Gly-Lys and Bz-Gly-Arg in vitro. Releases a C-terminal residue, which may be hydrophobic or positively charged. Binds 1 zinc ion per subunit. In vitro, is completely inhibited by l,l0-phenanthroline, and by isocaproic acid and Bz-Arg. Optimum pH is 7-8. Belongs to the peptidase M14 family.