Aspartyl aminopeptidase that contributes to peptide degradation both in the cytosol and the vacuole. Cells may respond to environmental conditions by changing the distributions of the cytosolic enzyme to the vacuole when cells need more active vacuolar degradation. Release of an N-terminal aspartate or glutamate from a peptide, with a preference for aspartate. Binds 2 Zn(2+) ions per subunit. The metalloproteases inhibitors EDTA and 1.10-phenanthroline both inhibit the activity, whereas bestatin, an inhibitor of most aminopeptidases, does not affect enzyme activity. Optimum pH is 7.5-7.9. Tetrahedron-shaped homododecamer built from six homodimers. In growing conditions, a small portion localizes in the vacuole, but actively transported to the vacuole under nutrient starvation conditions. Present with 172 molecules/cell in log phase SD medium. Belongs to the peptidase M18 family.