Human Methionine Aminopeptidase 2, METAP2 ELI

Cotranslationally removes the N-terminal methionine from nascent proteins.

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).

The catalytic activity of human METAP2 toward Met-Val Peptides is consistently two orders of magnitude higher than that of METAP1, suggesting that it is responsible for processing proteins containing N-terminal Met-Val and Met-Thr sequences in vivo.

Protects eukaryotic initiation factor EIF2S1 from translation-inhibiting phosphorylation by inhibitory kinases such as EIF2AK2/PKR and EIF2AK1/HCR.

Plays a critical role in the regulation of protein synthesis.