Accepted Name |
N-terminal amino-acid N(alpha)-acetyltransferase NatA
|
Reaction catalysed |
- N-terminal glycyl-[protein] + acetyl-CoA = N-terminal N(alpha)-acetylglycyl-[protein] + CoA + H(+)
- N-terminal L-alanyl-[protein] + acetyl-CoA = N-terminal N(alpha)-acetyl-L-alanyl-[protein] + CoA + H(+)
- N-terminal L-seryl-[protein] + acetyl-CoA = N-terminal N(alpha)-acetyl-L-seryl-[protein] + CoA + H(+)
- N-terminal L-valyl-[protein] + acetyl-CoA = N-terminal N(alpha)-acetyl-L-valyl-[protein] + CoA + H(+)
- N-terminal L-cysteinyl-[protein] + acetyl-CoA = N-terminal N(alpha)-acetyl-L-cysteinyl-[protein] + CoA + H(+)
- N-terminal L-threonyl-[protein] + acetyl-CoA = N-terminal N(alpha)-acetyl-L-threonyl-[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.
- 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 | 2.3.1.255 |
EC2PDB | 2.3.1.255 |
ExplorEnz | 2.3.1.255 |
KEGG Ligand Database for Enzyme Nomenclature | 2.3.1.255 |
IUBMB Enzyme Nomenclature | 2.3.1.255 |
MEDLINE | Find literature relating to 2.3.1.255 |
MetaCyc | 2.3.1.255 |
Rhea expert-curated reactions | 2.3.1.255 |
UniProtKB/Swiss-Prot |
Q9UTI3, ARD1_SCHPO | P07347, ARD1_YEAST | O61219, DAF31_CAEEL |
Q7X9V3, GNAT2_ARATH | Q9ZV08, GNAT4_ARATH | Q9LR91, GNAT5_ARATH |
Q8GUT5, GNAT6_ARATH | Q94AC8, GNAT7_ARATH | Q9C7G6, GNT10_ARATH |
Q9FKI4, NAA10_ARATH | Q2KI14, NAA10_BOVIN | P41227, NAA10_HUMAN |
Q9QY36, NAA10_MOUSE | Q9BSU3, NAA11_HUMAN | Q3UX61, NAA11_MOUSE |
Q4V8K3, NAA11_RAT | Q980R9, NAT_SACS2 | Q4JBG0, NAT_SULAC |
Q976C3, NAT_SULTO | I6YG32, RIMI_MYCTU |
|
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