ENZYME entry: EC 2.3.1.256

Accepted Name

N-terminal methionine N(alpha)-acetyltransferase NatC

Reaction catalysed

N-terminal L-methionyl-L-leucyl-[protein] + acetyl-CoA = N-terminal N(alpha)-acetyl-L-methionyl-L-leucyl-[protein] + CoA + H(+)
N-terminal L-methionyl-L-isoleucyl-[protein] + acetyl-CoA = N-terminal N(alpha)-acetyl-L-methionyl-L-isoleucyl-[protein] + CoA + H(+)
N-terminal L-methionyl-L-phenylalanyl-[protein] + acetyl-CoA = N-terminal N(alpha)-acetyl-L-methionyl-L-phenylalanyl-[protein] + CoA + H(+)
N-terminal L-methionyl-L-tryptophyl-[protein] + acetyl-CoA = N-terminal N(alpha)-acetyl-L-methionyl-L-tryptophyl-[protein] + CoA + H(+)
N-terminal L-methionyl-L-tyrosyl-[protein] + acetyl-CoA = N-terminal N(alpha)-acetyl-L-methionyl-L-tyrosyl-[protein] + CoA + H(+)

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 NatC complex is found in all eukaryotic organisms, and specifically targets N-terminal L-methionine residues attached to bulky hydrophobic residues at the second position, including Leu, Ile, Phe, Trp, and Tyr residues.
Formerly EC 2.3.1.88.

Cross-references

BRENDA

EC2PDB

ExplorEnz

KEGG Ligand Database for Enzyme Nomenclature

IUBMB Enzyme Nomenclature

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.-.-.-