METAP2

METAP2, methylthionyl aminopeptidase 2, alias MAP2, MNPEP, p67, Peptidase M, and so on. It is an enzyme present in all living organisms with critical tissue repair and protein degradation functions.The mechanism of action of METAP2 is mainly the co-translational removal of the N-terminal methionine from the nascent polypeptide chain during protein synthesis, a process that is essential for protein maturation and function. In particular, the catalytic activity of METAP2 is significantly increased when the second residue of the polypeptide chain is a small nonpolar amino acid, such as alanine, cysteine, glycine, proline, serine, threonine, or valine.

METAP2 has a wide range of significance in biology, which is not only involved in the regulation of protein synthesis, but also is associated with a wide range of biological processes, including angiogenesis, cell proliferation, and tumor development, etc. Due to its key role in angiogenesis, METAP2 has emerged as a potential target for the treatment of certain diseases such as solid tumor cancers and rheumatoid arthritis. In addition, inhibitors of METAP2, such as Fumagillin and Ovalicin, have been investigated for the development of anticancer drugs, and studies have shown that inhibitors targeting METAP2 are also effective in the treatment of obesity .