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ENZYME

ENZYME entry: EC 2.3.1.255

Accepted Name
N-terminal amino-acid N(alpha)-acetyltransferase NatA
Reaction catalysed
  • acetyl-CoA + N-terminal glycyl-[protein] <=> CoA + H(+) + N-terminal N(alpha)-acetylglycyl-[protein]
  • acetyl-CoA + N-terminal L-alanyl-[protein] <=> CoA + H(+) + N-terminal N(alpha)-acetyl-L-alanyl-[protein]
  • acetyl-CoA + N-terminal L-seryl-[protein] <=> CoA + H(+) + N-terminal N(alpha)-acetyl-L-seryl-[protein]
  • acetyl-CoA + N-terminal L-valyl-[protein] <=> CoA + H(+) + N-terminal N(alpha)-acetyl-L-valyl-[protein]
  • acetyl-CoA + N-terminal L-cysteinyl-[protein] <=> CoA + H(+) + N-terminal N(alpha)-acetyl-L-cysteinyl-[protein]
  • acetyl-CoA + N-terminal L-threonyl-[protein] <=> CoA + H(+) + N-terminal N(alpha)-acetyl-L-threonyl-[protein]
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.
  • 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.
  • Formerly EC 2.3.1.88.
Cross-references
BRENDA2.3.1.255
EC2PDB2.3.1.255
ExplorEnz2.3.1.255
PRIAM enzyme-specific profiles2.3.1.255
KEGG Ligand Database for Enzyme Nomenclature2.3.1.255
IUBMB Enzyme Nomenclature2.3.1.255
IntEnz2.3.1.255
MEDLINEFind literature relating to 2.3.1.255
MetaCyc2.3.1.255
Rhea expert-curated reactions2.3.1.255
UniProtKB/Swiss-Prot
Q9UTI3, ARD1_SCHPOP07347, ARD1_YEASTO61219, DAF31_CAEEL
Q7X9V3, GNAT2_ARATHQ9ZV08, GNAT4_ARATHQ9LR91, GNAT5_ARATH
Q8GUT5, GNAT6_ARATHQ94AC8, GNAT7_ARATHQ9C7G6, GNT10_ARATH
Q9FKI4, NAA10_ARATHQ2KI14, NAA10_BOVINP41227, NAA10_HUMAN
Q9QY36, NAA10_MOUSEQ9BSU3, NAA11_HUMANQ3UX61, NAA11_MOUSE
Q4V8K3, NAA11_RATQ980R9, NAT_SACS2Q4JBG0, NAT_SULAC
Q976C3, NAT_SULTOI6YG32, RIMI_MYCTU

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