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Information on EC 2.3.1.257 - N-terminal L-serine Nalpha-acetyltransferase NatD

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IUBMB Comments
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.
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The expected taxonomic range for this enzyme is: Eukaryota, Archaea, Bacteria
Synonyms
hNAA40, hNaa40p/hNatD, N(alpha)-acetyltransferase 40, N-acetyltransferase 11, N-alpha-acetyltransferase 40, Naa40, Naa40p, Nat11, NAT4, NatD, more
REACTION
REACTION DIAGRAM
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ORGANISM
UNIPROT
LITERATURE
acetyl-CoA + an N-terminal-L-seryl-[histone H2A] = an N-terminal-Nalpha-acetyl-L-seryl-[histone H2A] + CoA
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acetyl-CoA + an N-terminal-L-seryl-[histone H4] = an N-terminal-Nalpha-acetyl-L-seryl-[histone H4] + CoA
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(1)
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