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ENZYME entry: EC

Accepted Name
N-terminal methionine N(alpha)-acetyltransferase NatE
Reaction catalysed
  • acetyl-CoA + N-terminal L-methionyl-L-alanyl-[protein] = CoA + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-alanyl-[protein]
  • acetyl-CoA + N-terminal L-methionyl-L-seryl-[protein] = CoA + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-seryl-[protein]
  • acetyl-CoA + N-terminal L-methionyl-L-valyl-[protein] = CoA + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-valyl-[protein]
  • acetyl-CoA + N-terminal L-methionyl-L-threonyl-[protein] = CoA + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-threonyl-[protein]
  • acetyl-CoA + N-terminal L-methionyl-L-lysyl-[protein] = CoA + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-lysyl-[protein]
  • acetyl-CoA + N-terminal L-methionyl-L-leucyl-[protein] = CoA + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-leucyl-[protein]
  • acetyl-CoA + N-terminal L-methionyl-L-phenylalanyl-[protein] = CoA + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-phenylalanyl-[protein]
  • acetyl-CoA + N-terminal L-methionyl-L-tyrosyl-[protein] = CoA + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-tyrosyl-[protein]
  • 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, makes the N-terminal residue larger and more hydrophobic, and prevents its removal by hydrolysis.
  • It may also play a role in membrane targeting and gene silencing.
  • NatE is found in all eukaryotic organisms and plays an important role in chromosome resolution and segregation.
  • It specifically targets N-terminal L-methionine residues attached to Lys, Val, Ala, Tyr, Phe, Leu, Ser, and Thr.
  • There is some substrate overlap with EC
  • In addition, the acetylation of Met followed by small residues such as Ser, Thr, Ala, or Val suggests a kinetic competition between NatE and EC
  • The enzyme also has the activity of EC and autoacetylates several of its own lysine residues.
  • Formerly EC
PRIAM enzyme-specific profiles2.3.1.258
KEGG Ligand Database for Enzyme Nomenclature2.3.1.258
IUBMB Enzyme Nomenclature2.3.1.258
MEDLINEFind literature relating to
Rhea expert-curated reactions2.3.1.258

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