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Information on EC 2.3.1.255 - N-terminal amino-acid Nalpha-acetyltransferase NatA

for references in articles please use BRENDA:EC2.3.1.255
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EC Tree
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. The NatA complex is found in all eukaryotic organisms, and specifically targets N-terminal Ala, Gly, Cys, Ser, Thr, and Val residues, that became available after removal of the initiator methionine.
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UNIPROT: Q9BXJ9
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Word Map
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The enzyme appears in viruses and cellular organisms
Reaction Schemes
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acetyl-CoA
+
an N-terminal-glycyl-[protein]
=
an N-terminal-Nalpha-acetyl-glycyl-[protein]
+
CoA
+
an N-terminal-glycyl-[protein]
=
an N-terminal-Nalpha-acetyl-glycyl-[protein]
+
acetyl-CoA
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an N-terminal-L-alanyl-[protein]
=
an N-terminal-Nalpha-acetyl-L-alanyl-[protein]
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CoA
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an N-terminal-L-alanyl-[protein]
=
an N-terminal-Nalpha-acetyl-L-alanyl-[protein]
+
acetyl-CoA
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an N-terminal-L-seryl-[protein]
=
an N-terminal-Nalpha-acetyl-L-seryl-[protein]
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CoA
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an N-terminal-L-seryl-[protein]
=
an N-terminal-Nalpha-acetyl-L-seryl-[protein]
+
Synonyms
naa15, ard1b, hnaa10, daf-31, naa11, n-terminal acetyltransferase a, ta0058, arrest-defective protein 1, mtrimi, n-alpha-acetyltransferase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ARD1
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NAA10
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NAA15
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
acetyl-CoA:N-terminal-Gly/Ala/Ser/Val/Cys/Thr-[protein] Nalpha-acetyltransferase
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. The NatA complex is found in all eukaryotic organisms, and specifically targets N-terminal Ala, Gly, Cys, Ser, Thr, and Val residues, that became available after removal of the initiator methionine.