EC Number |
Substrates |
Organism |
Products |
Reversibility |
---|
2.3.1.286 | more |
Nepsilon-lysine acetyltransferase PhnO specifically transfer an acetyl group from AcCoA to Nepsilon-lysine residues on proteins. The enzyme shows a high degree of substrate specificity |
Escherichia coli |
? |
- |
- |
2.3.1.286 | more |
determination of substrate specificity, method, detailed overview. Structural analysis of KAT and AcP-dependent acetylation sites |
Escherichia coli |
? |
- |
- |
2.3.1.286 | more |
the enzyme also acts as an aminoalkylphosphonate N-acetyltransferase, EC 2.3.1.380. Determination of substrate specificity, method, detailed overview. Structural analysis of KAT and AcP-dependent acetylation sites |
Escherichia coli |
? |
- |
- |
2.3.1.286 | 2 KKGQSTSRHKKAcLMFKTEG + 2 NAD+ + 2 H2O |
- |
Thermotoga maritima |
KKGQSTSRHKKLMFKTEG + 2''-O-acetyl-ADP-D-ribose + 3''-O-acetyl-ADP-D-ribose + nicotinamide |
- |
? |
2.3.1.286 | acetyl-CoA + [protein]-L-lysine |
- |
Escherichia coli |
CoA + [protein]-N6-acetyl-L-lysine |
- |
? |
2.3.1.286 | acetyl-cytochrome c + NAD+ + H2O |
the enzyme does not deacetylate native acetyl-cytochrome c but does deacetylate the heat-denatured substrate |
Saccharomyces cerevisiae |
? |
- |
? |
2.3.1.286 | acetyl-poly-L-lysine + NAD+ + H2O |
- |
Saccharomyces cerevisiae |
? |
- |
? |
2.3.1.286 | AGG(AcK)GG(AcK)GMG(AcK)VGA(AcK)RHSC + NAD+ + H2O |
tetraacetylated histone-H4 N-terminal tail peptide |
Saccharomyces cerevisiae |
AGG(AcK)GG(AcK)GMG(AcK)VGAKRHSC + 2''-O-acetyl-ADP-D-ribose + nicotinamide |
- |
? |
2.3.1.286 | ARTKQTAR(AcK)STGG(AcK)APRKQLC + NAD+ + H2O |
diacetyl ated histone-H3 N-terminal tail peptide |
Saccharomyces cerevisiae |
ARTKQTARKSTGGKAPRKQLC + 2''-O-acetyl-ADP-D-ribose + nicotinamide |
- |
? |
2.3.1.286 | fluorogenic acetyl-L-lysine + NAD+ + H2O |
- |
Saccharomyces cerevisiae |
? |
- |
? |