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ENZYME entry: EC 2.3.1.258

Accepted Name
N-terminal methionine N(alpha)-acetyltransferase NatE.
Reaction catalysed
  • Acetyl-CoA + an N-terminal-L-methionyl-L-alanyl-[protein] <=> an N-terminal-N(alpha)-acetyl-L-methionyl-L-alanyl-[protein] + CoA
  • Acetyl-CoA + an N-terminal-L-methionyl-L-seryl-[protein] <=> an N-terminal-N(alpha)-acetyl-L-methionyl-L-seryl-[protein] + CoA
  • Acetyl-CoA + an N-terminal-L-methionyl-L-valyl-[protein] <=> an N-terminal-N(alpha)-acetyl-L-methionyl-L-valyl-[protein] + CoA
  • Acetyl-CoA + an N-terminal-L-methionyl-L-threonyl-[protein] <=> an N-terminal-N(alpha)-acetyl-L-methionyl-L-threonyl-[protein] + CoA
  • Acetyl-CoA + an N-terminal-L-methionyl-L-lysyl-[protein] <=> an N-terminal-N(alpha)-acetyl-L-methionyl-L-lysyl-[protein] + CoA
  • Acetyl-CoA + an N-terminal-L-methionyl-L-leucyl-[protein] <=> an N-terminal-N(alpha)-acetyl-L-methionyl-L-leucyl-[protein] + CoA
  • Acetyl-CoA + an N-terminal-L-methionyl-L-phenylalanyl-[protein] <=> an N-terminal-N(alpha)-acetyl-L-methionyl-L-phenylalanyl-[protein] + CoA
  • Acetyl-CoA + an N-terminal-L-methionyl-L-tyrosyl-[protein] <=> an N-terminal-N(alpha)-acetyl-L-methionyl-L-tyrosyl-[protein] + CoA
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, makes the N-terminal residue larger and more hydrophobic, and prevents its removal by hydrolysis.
  • It may also play a role in membrane targeting and gene silencing.
  • NatE is found in all eukaryotic organisms and plays an important role in chromosome resolution and segregation.
  • It specifically targets N-terminal L-methionine residues attached to Lys, Val, Ala, Tyr, Phe, Leu, Ser, and Thr.
  • There is some substrate overlap with EC 2.3.1.256.
  • In addition, the acetylation of Met followed by small residues such as Ser, Thr, Ala, or Val suggests a kinetic competition between NatE and EC 3.4.11.18.
  • The enzyme also has the activity of EC 2.3.1.48 and autoacetylates several of its own lysine residues.
  • Formerly EC 2.3.1.88.
Cross-references
BRENDA2.3.1.258
EC2PDB2.3.1.258
ExplorEnz2.3.1.258
PRIAM enzyme-specific profiles2.3.1.258
KEGG Ligand Database for Enzyme Nomenclature2.3.1.258
IUBMB Enzyme Nomenclature2.3.1.258
IntEnz2.3.1.258
MEDLINEFind literature relating to 2.3.1.258
MetaCyc2.3.1.258
UniProtKB/Swiss-Prot
Q0IIJ0, NAA50_BOVIN;  Q6DBY2, NAA50_DANRE;  Q9GZZ1, NAA50_HUMAN;  
Q6PGB6, NAA50_MOUSE;  Q5RF28, NAA50_PONAB;  Q6GP53, NAA50_XENLA;  
Q5XGA9, NAA50_XENTR;  Q08689, NAT5_YEAST;  Q980R9, NAT_SACS2;  
Q4JBG0, NAT_SULAC;  Q976C3, NAT_SULTO;  I6YG32, RIMI_MYCTU;  
Q9NHD5, SAN_DROME;  

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