N-terminal-acetylases (NATs) catalyse the covalent attachment of an acetyl moiety from acetyl-CoA to the free ¦Á-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.
Cofactor
History
Reactions
(1) Acetyl-CoA + an N-terminal-L-seryl-[histone H4] = an N-terminal- N(alpha)-acetyl-L-seryl-[histone H4] + CoA. (2) Acetyl-CoA + an N-terminal-L-seryl-[histone H2A] = an N-terminal- N(alpha)-acetyl-L-seryl-[histone H2A] + CoA.
