Displays aminopeptidase activity with a broad substrate specificity. Preferentially hydrolyzes L-Lys-AMC but also shows strong activity against L-Ala-AMC, L-Arg-AMC and L-Leu-AMC. Binds 1 zinc ion per subunit. Inhibited by 1,10-phenanthroline, EDTA and bestatin. Activity is not affected by phosphoramidin, PMSF, leupeptin, iodoacetamide or pepstatin. Optimum pH is 7.4. Active from pH 5.8 to 8.6, with less than 20% of normal activity at pH 6.0. Expressed in all erythrocytic stages. The 120 kDa precursor is cleaved in vitro into 96 kDa and 68 kDa forms. Belongs to the peptidase M1 family.