EC Number   |
Inhibitors |
Structure |
|---|
    4.1.1.11 | more |
no inhibition by D-serine, (4S)-1,3-thiazolidin-3-ium-4-carboxylate, alpha-D-arabinopyranose, and 1,2-dihydropyrazolo[3,4-d]pyrimidin-4-one |
 |
| 4.1.1.11 | more |
enzyme ADC is also subject to mechanism-based inactivation, which has been reported for many other pyruvoyl-dependent. Mechanism-based inactivation only occurs during catalysis |
|
| 4.1.1.11 | NaBH4 |
- |
  |
| 4.1.1.11 | oxaloacetate |
- |
|
| 4.1.1.11 | oxaloacetate |
very strong inhibition |
|
| 4.1.1.11 | PanZ |
structure of the complex of PanD and its activating factor PanZ, overview. Binding of acetyl-CoA to PanZ is required to form the PanZ/PanD interface. PanZ-AcCoA activates PanD via selection of a reactive conformation of PanD. PanZ is essential for activation of the zymogen PanD to form the mature enzyme in vivo, and its deletion leads to beta-alanine auxotrophy. NMR spectroscopy dmonstrates that CoA is an absolute requirement for PanD-PanZ complex formation. PanZ inhibits catalytic activity by activated PanD |
|
| 4.1.1.11 | pentyl pantothenamide |
high-potency growth inhibition by pentyl pantothenamide is dependent upon the PanD-PanZ interaction. Substitution of the Escherichia coli panD for the noninteracting Bacillus panD leads to resistance against the inhibitor |
|
| 4.1.1.11 | phenylhydrazine |
- |
|
| 4.1.1.11 | succinate |
- |
|
| 4.1.1.11 | succinate |
moderate inhibition |
|
