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ENZYME entry: EC

Accepted Name
N-terminal methionine N(alpha)-acetyltransferase NatC.
Reaction catalysed
  • Acetyl-CoA + an N-terminal-L-methionyl-L-leucyl-[protein] <=> an N-terminal-N(alpha)-acetyl-L-methionyl-L-leucyl-[protein] + CoA
  • Acetyl-CoA + an N-terminal-L-methionyl-L-isoleucyl-[protein] <=> an N-terminal-N(alpha)-acetyl-L-methionyl-L-isoleucyl-[protein] + CoA
  • Acetyl-CoA + an N-terminal-L-methionyl-L-phenylalanyl-[protein] <=> an N-terminal-N(alpha)-acetyl-L-methionyl-L-phenylalanyl-[protein] + CoA
  • Acetyl-CoA + an N-terminal-L-methionyl-L-tryptophyl-[protein] <=> an N-terminal-N(alpha)-acetyl-L-methionyl-L-tryptophyl-[protein] + CoA
  • Acetyl-CoA + an N-terminal-L-methionyl-L-tyrosyl-[protein] <=> an N-terminal-N(alpha)-acetyl-L-methionyl-L-tyrosyl-[protein] + CoA
  • N-terminal-acetylases (NATs) catalyze the covalent attachment of an acetyl moiety from acetyl-CoA to the free alpha-amino group at the N-terminus of a protein.
  • This irreversible modification neutralizes the positive charge at the N-terminus and makes the N-terminal residue larger and more hydrophobic, and may also play a role in membrane targeting and gene silencing.
  • The NatC complex is found in all eukaryotic organisms, and specifically targets N-terminal L-methionine residues attached to bulky hydrophobic residues at the second position, including Leu, Ile, Phe, Trp, and Tyr residues.
  • Formerly EC
PRIAM enzyme-specific profiles2.3.1.256
KEGG Ligand Database for Enzyme Nomenclature2.3.1.256
IUBMB Enzyme Nomenclature2.3.1.256
MEDLINEFind literature relating to
O80438, MAK3_ARATH;  Q147X3, NAA30_HUMAN;  Q8CES0, NAA30_MOUSE;  
O74311, NAA30_SCHPO;  Q0IHH1, NAA30_XENLA;  Q03503, NAA30_YEAST;  

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