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ENZYME entry: EC

Accepted Name
N-terminal amino-acid N(alpha)-acetyltransferase NatA.
Reaction catalysed
  • Acetyl-CoA + an N-terminal-glycyl-[protein] <=> an N-terminal-N(alpha)-acetyl-glycyl-[protein] + CoA
  • Acetyl-CoA + an N-terminal-L-alanyl-[protein] <=> an N-terminal-N(alpha)-acetyl-L-alanyl-[protein] + CoA
  • Acetyl-CoA + an N-terminal-L-seryl-[protein] <=> an N-terminal-N(alpha)-acetyl-L-seryl-[protein] + CoA
  • Acetyl-CoA + an N-terminal-L-valyl-[protein] <=> an N-terminal-N(alpha)-acetyl-L-valyl-[protein] + CoA
  • Acetyl-CoA + an N-terminal-L-cysteinyl-[protein] <=> an N-terminal-N(alpha)-acetyl-L-cysteinyl-[protein] + CoA
  • Acetyl-CoA + an N-terminal-L-threonyl-[protein] <=> an N-terminal-N(alpha)-acetyl-L-threonyl-[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.
  • The NatA complex is found in all eukaryotic organisms, and specifically targets N-terminal Ala, Gly, Cys, Ser, Thr, and Val residues, that became available after removal of the initiator methionine.
  • Formerly EC
PRIAM enzyme-specific profiles2.3.1.255
KEGG Ligand Database for Enzyme Nomenclature2.3.1.255
IUBMB Enzyme Nomenclature2.3.1.255
MEDLINEFind literature relating to
Rhea expert-curated reactions2.3.1.255
Q9UTI3, ARD1_SCHPO;  P07347, ARD1_YEAST;  O61219, DAF31_CAEEL;  
Q9FKI4, NAA10_ARATH;  Q2KI14, NAA10_BOVIN;  P41227, NAA10_HUMAN;  
Q4V8K3, NAA11_RAT;  Q980R9, NAT_SACS2;  Q4JBG0, NAT_SULAC;  

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