EC 2.3.1.258 - N-terminal methionine Nα-acetyltransferase NatE

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IntEnz Enzyme Nomenclature
EC 2.3.1.258

Names

Accepted name:
N-terminal methionine Nα-acetyltransferase NatE
Other names:
NAA50 (gene name)
NAT5
SAN
Systematic name:
acetyl-CoA:N-terminal-Met-Ala/Ser/Val/Thr/Lys/Leu/Phe/Tyr-[protein] Met-Nα-acetyltransferase

Reactions

Comments:

N-terminal-acetylases (NATs) catalyse the covalent attachment of an acetyl moiety from acetyl-CoA to the free α-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, N-terminal methionine Nα-acetyltransferase NatC. 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, methionyl aminopeptidase. The enzyme also has the activity of EC 2.3.1.48, histone acetyltransferase, and autoacetylates several of its own lysine residues. Formerly EC 2.3.1.88.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
UniProtKB/Swiss-Prot: (13) [show] [UniProt]

References

  1. Hou, F., Chu, C. W., Kong, X., Yokomori, K., Zou, H.
    The acetyltransferase activity of San stabilizes the mitotic cohesin at the centromeres in a shugoshin-independent manner.
    J. Cell Biol. 177: 587-597 (2007). [PMID: 17502424]
  2. Pimenta-Marques, A., Tostoes, R., Marty, T., Barbosa, V., Lehmann, R., Martinho, R. G.
    Differential requirements of a mitotic acetyltransferase in somatic and germ line cells.
    Dev. Biol. 323: 197-206 (2008). [PMID: 18801358]
  3. Evjenth, R., Hole, K., Karlsen, O. A., Ziegler, M., Arnesen, T., Lillehaug, J. R.
    Human Naa50p (Nat5/San) displays both protein N alpha- and N epsilon-acetyltransferase activity.
    J. Biol. Chem. 284: 31122-31129 (2009). [PMID: 19744929]
  4. Van Damme, P., Hole, K., Gevaert, K., Arnesen, T.
    N-terminal acetylome analysis reveals the specificity of Naa50 (Nat5) and suggests a kinetic competition between N-terminal acetyltransferases and methionine aminopeptidases.
    Proteomics 15: 2436-2446 (2015). [PMID: 25886145]

[created 1989 as EC 2.3.1.88, part-transferred 2016 to EC 2.3.1.258]