ENZYME entry: EC 2.3.1.258

Accepted Name

N-terminal methionine N(alpha)-acetyltransferase NatE

Reaction catalysed

acetyl-CoA + N-terminal L-methionyl-L-alanyl-[protein] <=> CoA + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-alanyl-[protein]
acetyl-CoA + N-terminal L-methionyl-L-seryl-[protein] <=> CoA + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-seryl-[protein]
acetyl-CoA + N-terminal L-methionyl-L-valyl-[protein] <=> CoA + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-valyl-[protein]
acetyl-CoA + N-terminal L-methionyl-L-threonyl-[protein] <=> CoA + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-threonyl-[protein]
acetyl-CoA + N-terminal L-methionyl-L-lysyl-[protein] <=> CoA + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-lysyl-[protein]
acetyl-CoA + N-terminal L-methionyl-L-leucyl-[protein] <=> CoA + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-leucyl-[protein]
acetyl-CoA + N-terminal L-methionyl-L-phenylalanyl-[protein] <=> CoA + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-phenylalanyl-[protein]
acetyl-CoA + N-terminal L-methionyl-L-tyrosyl-[protein] <=> CoA + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-tyrosyl-[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, 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

BRENDA

EC2PDB

ExplorEnz

PRIAM enzyme-specific profiles

KEGG Ligand Database for Enzyme Nomenclature

IUBMB Enzyme Nomenclature

IntEnz

MEDLINE

MetaCyc

Rhea expert-curated reactions

UniProtKB/Swiss-Prot

All UniProtKB/Swiss-Prot entries referenced in this entry, with possibility to download in different formats, align etc.

All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 2.3.1.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 2.3.-.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 2.-.-.-