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METAP1 Protein, Antibody, ELISA Kit, cDNA Clone

METAP1 Related Areas

METAP1 Related Pathways

METAP1 Related Product

    METAP1 Background

    Catalytic activity: Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides.
    Cofactor: 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, m
    Subunit structure: Associates with the 60S ribosomal subunit of the 80S translational complex (By similarity).
    Subcellular location: Cytoplasm (By similarity).
    Sequence similarities: Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily.
    General information above from UniProt

    Processing of the N-terminal initiator methionine or formylated methionine is an essential cellular process conserved from prokaryotes to eukaryotes. The proteolytic removal of N-terminal methionine from nascent peptides is catalyzed by a family of enzymes known as methionine aminopeptidases (MetAPs) and is essential for cell growth. METAP1 and METAP2 have different substrate specificity due to the differences in both size and shape of the active sites. As a member of the M24 family of metalloproteases, METAP1 plays an important role in G(2)/M phase regulation of the cell cycle and may serve as a promising target for the discovery and development of new anticancer agents.

    METAP1 Altermative Names

    METAP1 Related Studies

    1. Lowther, W.T. and B.W. Matthews, 2000, Biochim. Biophys. Acta. 1477: 157 – 167.

    2. Addlaqatta, A. et al., 2005, Biochemistry. 44: 14741-14749.

    3. Hu, X. et al., 2006, Proc. Natl. Acad. Sci. U.S.A. 103:18148-18153.

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