ENZYME entry: EC 2.3.1.255
Accepted Name |
N-terminal amino-acid N(alpha)-acetyltransferase NatA.
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Reaction catalysed |
- Acetyl-CoA + an N-terminal-glycyl-[protein] <=> an N-terminal-N(alpha)-acetyl-glycyl-[protein] + CoA
- Acetyl-CoA + an N-terminal-L-alanyl-[protein] <=> an N-terminal-N(alpha)-acetyl-L-alanyl-[protein] + CoA
- Acetyl-CoA + an N-terminal-L-seryl-[protein] <=> an N-terminal-N(alpha)-acetyl-L-seryl-[protein] + CoA
- Acetyl-CoA + an N-terminal-L-valyl-[protein] <=> an N-terminal-N(alpha)-acetyl-L-valyl-[protein] + CoA
- Acetyl-CoA + an N-terminal-L-cysteinyl-[protein] <=> an N-terminal-N(alpha)-acetyl-L-cysteinyl-[protein] + CoA
- Acetyl-CoA + an N-terminal-L-threonyl-[protein] <=> an N-terminal-N(alpha)-acetyl-L-threonyl-[protein] + CoA
|
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.
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Cross-references |
BRENDA | 2.3.1.255 |
EC2PDB | 2.3.1.255 |
ExplorEnz | 2.3.1.255 |
PRIAM enzyme-specific profiles | 2.3.1.255 |
KEGG Ligand Database for Enzyme Nomenclature | 2.3.1.255 |
IUBMB Enzyme Nomenclature | 2.3.1.255 |
IntEnz | 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; |
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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