Zinc-dependent metalloproteinase (PubMed:16750535). Proteolytically removes the C-terminal three residues of farnesylated proteins (By similarity). The peptide bond hydrolyzed can be designated -C-|-A-A-X in which C is an S-isoprenylated cysteine residue, A is usually aliphatic and X is the C-terminal residue of the substrate protein, and may be any of several amino acids. Binds 1 zinc ion per subunit. Inhibited by ethylenediaminetetraacetic acid (EDTA) but not by serine, aspartic or cysteine protease inhibitors. Inhibited by high concentration of Zn(2+) (> 0.1 mM). Optimum pH is 7.5. Optimum temperature is 37 degrees Celsius. Loss of catalytic activity at temperatures above 50 degrees Celsius. Homodimer; disulfide-linked. Expressed in scolex and bladder wall of metacestode larval stage. Expressed in adults. Belongs to the peptidase M48A family.