Methionine aminopeptidase 2 (METAP2)

Cotranslationally eliminates the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the main 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 always two orders of magnitude greater than that of METAP1, suggesting it is responsible for processing proteins containing N- terminal Met-Val and Met-Thr sequences in vivo. .