Carboxypeptidase that catalyzes the release of hydrophobic and acidic C-terminal amino acids. Binds 1 zinc ion per subunit. Completely inhibited by the A-type carboxypeptidase inhibitor benzylsuccinic acid. Inhibited by the leech carboxypeptidase inhibitor and the potato carboxydase inhibitor. Inhibited by the chelating agent 1,10-phenanthroline. Partial inhibition by preincubation with the chelating agent EDTA is reversed by addition of Zn(2+). Not inhibited by the cysteine protease inhibitors L-carboxy-trans-2,3-epoxypropyl-leycylamido (4-guanidino) butane, E-64 and cystatin, the aspartic protease inhibitor pepstatin, or the serine protease inhibitors Pefabloc, soybean trypsin-chymotrypsin inhibitor, soybean trypsin inhibitor and aprotinin. Optimum pH is 7.0-7.5 with AAFP as substrate. Detected in the body but not in the tentacle crown (at protein level). Belongs to the peptidase M14 family.