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 | 2.3.1.258 |
EC2PDB | 2.3.1.258 |
ExplorEnz | 2.3.1.258 |
PRIAM enzyme-specific profiles | 2.3.1.258 |
KEGG Ligand Database for Enzyme Nomenclature | 2.3.1.258 |
IUBMB Enzyme Nomenclature | 2.3.1.258 |
IntEnz | 2.3.1.258 |
MEDLINE | Find literature relating to 2.3.1.258 |
MetaCyc | 2.3.1.258 |
Rhea expert-curated reactions | 2.3.1.258 |
UniProtKB/Swiss-Prot |
Q0IIJ0, NAA50_BOVIN | Q6DBY2, NAA50_DANRE | Q9GZZ1, NAA50_HUMAN |
Q6PGB6, NAA50_MOUSE | Q5RF28, NAA50_PONAB | Q6GP53, NAA50_XENLA |
Q5XGA9, NAA50_XENTR | Q08689, NAT5_YEAST | Q980R9, NAT_SACS2 |
Q4JBG0, NAT_SULAC | Q976C3, NAT_SULTO | I6YG32, RIMI_MYCTU |
Q9NHD5, SAN_DROME |
|
View entry in original ENZYME format
View entry in raw text format (no links)
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.-.-.-