Accepted Name |
N-terminal methionine N(alpha)-acetyltransferase NatC
|
Reaction catalysed |
- 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-isoleucyl-[protein] <=> CoA + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-isoleucyl-[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-tryptophyl-[protein] <=> CoA + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-tryptophyl-[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 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 | 2.3.1.256 |
EC2PDB | 2.3.1.256 |
ExplorEnz | 2.3.1.256 |
PRIAM enzyme-specific profiles | 2.3.1.256 |
KEGG Ligand Database for Enzyme Nomenclature | 2.3.1.256 |
IUBMB Enzyme Nomenclature | 2.3.1.256 |
IntEnz | 2.3.1.256 |
MEDLINE | Find literature relating to 2.3.1.256 |
MetaCyc | 2.3.1.256 |
Rhea expert-curated reactions | 2.3.1.256 |
UniProtKB/Swiss-Prot |
|
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