ID   2.3.1.256
DE   N-terminal methionine N(alpha)-acetyltransferase NatC.
CA   (1) acetyl-CoA + N-terminal L-methionyl-L-leucyl-[protein] = CoA + H(+) +
CA   N-terminal N(alpha)-acetyl-L-methionyl-L-leucyl-[protein].
CA   (2) acetyl-CoA + N-terminal L-methionyl-L-isoleucyl-[protein] = CoA +
CA   H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-isoleucyl-[protein].
CA   (3) acetyl-CoA + N-terminal L-methionyl-L-phenylalanyl-[protein] = CoA +
CA   H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-phenylalanyl-[protein].
CA   (4) acetyl-CoA + N-terminal L-methionyl-L-tryptophyl-[protein] = CoA +
CA   H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-tryptophyl-[protein].
CA   (5) acetyl-CoA + N-terminal L-methionyl-L-tyrosyl-[protein] = CoA + H(+)
CA   + N-terminal N(alpha)-acetyl-L-methionyl-L-tyrosyl-[protein].
CC   -!- N-terminal-acetylases (NATs) catalyze the covalent attachment of an
CC       acetyl moiety from acetyl-CoA to the free alpha-amino group at the
CC       N-terminus of a protein.
CC   -!- This irreversible modification neutralizes the positive charge at the
CC       N-terminus and makes the N-terminal residue larger and more
CC       hydrophobic, and may also play a role in membrane targeting and gene
CC       silencing.
CC   -!- The NatC complex is found in all eukaryotic organisms,
CC       and specifically targets N-terminal L-methionine residues attached to
CC       bulky hydrophobic residues at the second position, including Leu,
CC       Ile, Phe, Trp, and Tyr residues.
CC   -!- Formerly EC 2.3.1.88.
DR   O80438, MAK3_ARATH ;  Q147X3, NAA30_HUMAN;  Q8CES0, NAA30_MOUSE;
DR   O74311, NAA30_SCHPO;  Q0IHH1, NAA30_XENLA;  Q03503, NAA30_YEAST;
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