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ENZYME entry: EC

Accepted Name
N-terminal L-serine N(alpha)-acetyltransferase NatD.
Reaction catalysed
  • acetyl-CoA + N-terminal L-seryl-[histone H4] <=> CoA + H(+) + N-terminal N(alpha)-acetyl-L-seryl-[histone H4]
  • acetyl-CoA + N-terminal L-seryl-[histone H2A] <=> CoA + H(+) + N-terminal N(alpha)-acetyl-L-seryl-[histone H2A]
  • 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.
  • NatD is found in all eukaryotic organisms, and acetylates solely the serine residue at the N-terminus of histones H2A or H4.
  • Efficient recognition and acetylation by NatD requires at least the first 30 to 50 highly conserved amino acid residues of the histone N terminus.
  • Formerly EC
PRIAM enzyme-specific profiles2.3.1.257
KEGG Ligand Database for Enzyme Nomenclature2.3.1.257
IUBMB Enzyme Nomenclature2.3.1.257
MEDLINEFind literature relating to
Rhea expert-curated reactions2.3.1.257
Q568K5, NAA40_DANRE;  Q86UY6, NAA40_HUMAN;  Q8VE10, NAA40_MOUSE;  
Q9USH6, NAA40_SCHPO;  Q6NUH2, NAA40_XENLA;  Q04751, NAA40_YEAST;  

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