ENZYME entry: EC 2.3.1.255

Accepted Name

N-terminal amino-acid N(alpha)-acetyltransferase NatA

Reaction catalysed

acetyl-CoA + N-terminal glycyl-[protein] <=> CoA + H(+) + N-terminal N(alpha)-acetylglycyl-[protein]
acetyl-CoA + N-terminal L-alanyl-[protein] <=> CoA + H(+) + N-terminal N(alpha)-acetyl-L-alanyl-[protein]
acetyl-CoA + N-terminal L-seryl-[protein] <=> CoA + H(+) + N-terminal N(alpha)-acetyl-L-seryl-[protein]
acetyl-CoA + N-terminal L-valyl-[protein] <=> CoA + H(+) + N-terminal N(alpha)-acetyl-L-valyl-[protein]
acetyl-CoA + N-terminal L-cysteinyl-[protein] <=> CoA + H(+) + N-terminal N(alpha)-acetyl-L-cysteinyl-[protein]
acetyl-CoA + N-terminal L-threonyl-[protein] <=> CoA + H(+) + N-terminal N(alpha)-acetyl-L-threonyl-[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.
The NatA complex is found in all eukaryotic organisms, and specifically targets N-terminal Ala, Gly, Cys, Ser, Thr, and Val residues, that became available after removal of the initiator methionine.
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.-.-.-