(1) acetyl-CoA + an N-terminal-L-seryl-[histone H4] = an N-terminal-Nalpha-acetyl-L-seryl-[histone H4] + CoA;
(2) acetyl-CoA + an N-terminal-L-seryl-[histone H2A] = an N-terminal-Nalpha-acetyl-L-seryl-[histone H2A] + CoA
N-terminal-Nalpha-acetyl-L-seryl-[histone H4];
CoA [CPD:C00010];
N-terminal-Nalpha-acetyl-L-seryl-[histone H2A]
Comment
N-terminal-acetylases (NATs) catalyse 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.
History
EC 2.3.1.257 created 1989 as EC 2.3.1.88, part transferred 2016 to EC 2.3.1.257