Venom protein that cleaves N-terminal acidic residues from peptides with high potency in presence of calcium (PubMed:18384831). It may have several roles in venom including alteration of blood pressure by cleaving circulating angiotensin-2, general degradation of host tissue, increase of permeability to other venom components, and/or processing of other toxins in the venom (By similarity) (PubMed:18384831). Release of N-terminal glutamate (and to a lesser extent aspartate) from a peptide. Binds 1 zinc ion per subunit. Inhibited by the aminopeptidase competitive inhibitors amastatin (Leu and acidic inhibitor), and bestatin (Leu inhibitor), by chelating agents EDTA, and 1,10-Phenanthroline, as well as by Zn(2+) ions. Substrate specificity is modulated by Ca(2+), Ba(2+), and Mn(2+) ions which enhances the enzymatic activity for cleavage of acidic residues. Homodimer; disulfide-linked. Found in the venom as transmembrane proteins in exosome-like vesicles. Belongs to the peptidase M1 family.