Aminopeptidase with broad substrate specificity to several peptides. Shows strong preference for leucine but cleaves also next to Arg and lysine in peptide-bond-containing substrates. Release of an N-terminal amino acid, Xaa-|-Yaa- from a peptide, amide or arylamide. Xaa is preferably Ala, but may be most amino acids including Pro (slow action). When a terminal hydrophobic residue is followed by a prolyl residue, the two may be released as an intact Xaa-Pro dipeptide. Binds 1 zinc ion per subunit. Monomer. The N-terminus is blocked. Belongs to the peptidase M1 family.