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ENZYME entry: EC 2.3.1.257

Accepted Name
N-terminal L-serine N(alpha)-acetyltransferase NatD.
Reaction catalysed
  • Acetyl-CoA + an N-terminal-L-seryl-[histone H4] <=> an N-terminal-N(alpha)-acetyl-L-seryl-[histone H4] + CoA
  • Acetyl-CoA + an N-terminal-L-seryl-[histone H2A] <=> an N-terminal-N(alpha)-acetyl-L-seryl-[histone H2A] + CoA
Comment(s)
  • 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 2.3.1.88.
Cross-references
BRENDA2.3.1.257
EC2PDB2.3.1.257
ExplorEnz2.3.1.257
PRIAM enzyme-specific profiles2.3.1.257
KEGG Ligand Database for Enzyme Nomenclature2.3.1.257
IUBMB Enzyme Nomenclature2.3.1.257
IntEnz2.3.1.257
MEDLINEFind literature relating to 2.3.1.257
MetaCyc2.3.1.257
UniProtKB/Swiss-Prot
Q568K5, NAA40_DANRE;  Q86UY6, NAA40_HUMAN;  Q8VE10, NAA40_MOUSE;  
Q9USH6, NAA40_SCHPO;  Q6NUH2, NAA40_XENLA;  Q04751, NAA40_YEAST;  

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