EC Number   |
Inhibitors |
Structure  |
|---|
   2.3.1.B41 | more |
splitomicin and sirtinol fail to inhibit PfSir2 |
 |
| 2.3.1.B41 | more |
nicotinamide insensitivity, IC50: 2.1 mM |
|
| 2.3.1.B41 | more |
not inhibited by linoleic acid, oleic acid, oleoylethanolamide, and myristoylethanolamide |
|
| 2.3.1.B41 | more |
preparation of the 4-substituited-4,5-dihydropyrrolo[1,2-a]quinoxalines and 4-substituited-pyrrolo[1,2-a]quinoxalines |
|
| 2.3.1.B41 | more |
identification of SIRT6 inhibitors that decrease SIRT6 deacetylase activity and evoke coherent biological effects in cells. These inhibitors include a family of compounds with a quinazolinedione-based structure and a family of compounds with salicylate-based structure, with an IC50 for the SIRT6-catalyzed deacetylase activity in the low micromolar range. Relative enzyme activity in presencee of inhibitors compared to control, overview. No inhibition by (9H-fluoren-9-yl)methyl [(2S)-6-[(tert-butoxycarbonyl)amino]-1-(dodecylamino)-1-oxohexan-2-yl]carbamate and tert-butyl [(5S)-5-acetamido-6-(dodecylamino)-6-oxohexyl]carbamate |
|
| 2.3.1.B41 | quercetin |
0.2 mM, 52% inhibition, substrate: Ac-RYQ(N6-acetyl)K-7-amido-4-methylcoumarin |
  |
| 2.3.1.B41 | quercetin |
38% inhibition at 0.1 mM |
|
| 2.3.1.B41 | nicotinamide |
inhibits the deacetylation of native histones much more effectively than deacetylation of a synthetic substrate |
|
| 2.3.1.B41 | luteolin |
30% inhibition at 0.1 mM |
|
| 2.3.1.B41 | trichostatin A |
TSA, a potent, zinc-chelating hydroxamate inhibitors of zinc-dependent deacylases, which potently and isoform-specifically inhibits Sirt6. Sirtuin 6 inhibition mechanism, structural basis and interaction analysis, detailed overview. The binding site are nicotinamide pocket and acyl channel, binding kinetics |
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