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ENZYME

ENZYME entry: EC 2.3.1.254

Accepted Name
N-terminal methionine N(alpha)-acetyltransferase NatB
Reaction catalysed
  • acetyl-CoA + N-terminal L-methionyl-L-asparaginyl-[protein] <=> CoA + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-asparaginyl-[protein]
  • acetyl-CoA + N-terminal L-methionyl-L-glutaminyl-[protein] <=> CoA + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-glutaminyl-[protein]
  • acetyl-CoA + N-terminal L-methionyl-L-aspartyl-[protein] <=> CoA + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-aspartyl-[protein]
  • acetyl-CoA + N-terminal L-methionyl-L-glutamyl-[protein] <=> CoA + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-glutamyl-[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, and may also play a role in membrane targeting and gene silencing.
  • The NatB complex is found in all eukaryotic organisms, and specifically targets N-terminal L-methionine residues attached to Asn, Asp, Gln, or Glu residues at the second position.
  • Formerly EC 2.3.1.88.
Cross-references
BRENDA2.3.1.254
EC2PDB2.3.1.254
ExplorEnz2.3.1.254
PRIAM enzyme-specific profiles2.3.1.254
KEGG Ligand Database for Enzyme Nomenclature2.3.1.254
IUBMB Enzyme Nomenclature2.3.1.254
IntEnz2.3.1.254
MEDLINEFind literature relating to 2.3.1.254
MetaCyc2.3.1.254
Rhea expert-curated reactions2.3.1.254
UniProtKB/Swiss-Prot
Q8LGI8, NAA20_ARATHQ58ED9, NAA20_DANREP61599, NAA20_HUMAN
Q2PFM2, NAA20_MACFAP61600, NAA20_MOUSEQ7ZXR3, NAA20_XENLA
Q6P632, NAA20_XENTRO74457, NAT3_SCHPOQ06504, NAT3_YEAST

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