Cotranslationally removes the N-terminal methionine from nascent proteins (PubMed:16983082, PubMed:27023914). The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val) (By similarity). May play an important role in parasite growth during the blood asexual stage (PubMed:16983082). Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides. Highest activity with zinc and cobalt ions, and low activity with manganese or divalent iron ions (PubMed:27023914). Binds 2 divalent metal cations per subunit. Has a high-affinity and a low affinity metal-binding site. The true nature of the physiological cofactor is under debate. The enzyme is active with cobalt, zinc, manganese or divalent iron ions. Most likely, methionine aminopeptidases function as mononuclear Fe(2+)-metalloproteases under physiological conditions, and the catalytically relevant metal-binding site has been assigned to the histidine-containing high-affinity site (By similarity). Inhibited by pyrimidine derivative XC11. kcat is 13.9 min(-1) with methionine containing-oligopeptide as substrate (PubMed:16983082). kcat is 552.49 min(-1) in presence of 1 uM Zn(2+), 442.48 min(-1) in presence of 10 uM Zn(2+) and 364.30 min(-1) in presence of 100 uM Zn(2+), with Met-Gly-Met-Met peptide as substrate (PubMed:27023914). kcat is 1005 min(-1) in presence of 1 uM Co(2+), 583.09 min(-1) in presence of 10 uM Co(2+) and 547.95 min(-1) in presence of 100 uM Co(2+), with Met-Gly-Met-Met peptide as substrate (PubMed:27023914). Optimum pH is 7.5. Optimum temperature is 37 degrees Celsius (PubMed:27023914). However, has substantial activity at 25 degrees Celsius (PubMed:27023914). Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily.