ID   2.3.1.256
DE   N-terminal methionine N(alpha)-acetyltransferase NatC.
CA   (1) N-terminal L-methionyl-L-leucyl-[protein] + acetyl-CoA = N-terminal
CA   N(alpha)-acetyl-L-methionyl-L-leucyl-[protein] + CoA + H(+).
CA   (2) N-terminal L-methionyl-L-isoleucyl-[protein] + acetyl-CoA =
CA   N-terminal N(alpha)-acetyl-L-methionyl-L-isoleucyl-[protein] + CoA +
CA   H(+).
CA   (3) N-terminal L-methionyl-L-phenylalanyl-[protein] + acetyl-CoA =
CA   N-terminal N(alpha)-acetyl-L-methionyl-L-phenylalanyl-[protein] + CoA +
CA   H(+).
CA   (4) N-terminal L-methionyl-L-tryptophyl-[protein] + acetyl-CoA =
CA   N-terminal N(alpha)-acetyl-L-methionyl-L-tryptophyl-[protein] + CoA +
CA   H(+).
CA   (5) N-terminal L-methionyl-L-tyrosyl-[protein] + acetyl-CoA = N-terminal
CA   N(alpha)-acetyl-L-methionyl-L-tyrosyl-[protein] + CoA + H(+).
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 ;  Q95RC0, NA30A_DROME;  Q147X3, NAA30_HUMAN;
DR   Q8CES0, NAA30_MOUSE;  O74311, NAA30_SCHPO;  Q0IHH1, NAA30_XENLA;
DR   Q03503, NAA30_YEAST;
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