EC Number   |
Inhibitors |
Structure  |
|---|
    4.1.1.11 | more |
not inhibited by (2R,3R)-3-fluoroaspartic acid and (2R,3S)-3-fluoroaspartic acid |
 |
| 4.1.1.11 | more |
potential inhibitor molecule docking using the enzyme's crystal structure, overview |
|
| 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 | CoA |
the CoA-dependent interaction inhibits catalysis by the activated enzyme. Binding of acetyl-CoA to PanZ is required to form the PanZ/PanD interface. PanZ.AcCoA inhibits the activated enzyme regulating pantothenate biosynthesis. The binding site for AcCoA is very close to the protein-protein interface. Structure of the complex of PanD and its activating factor PanZ with bound CoA, overview |
  |
| 4.1.1.11 | acetyl-CoA |
CoA-dependent interaction of PanZ and PanD. Growth inhibition is due to the CoA-dependent PanD-PanZ interaction and the inhibition occurs at native concentrations of PanD and PanZ in the cell. The production of beta-alanine is feedback-regulated by the PanZ-AcCoA complex |
|
| 4.1.1.11 | L-glutamate |
strong inhibition |
|
| 4.1.1.11 | oxaloacetate |
- |
|
| 4.1.1.11 | oxaloacetate |
very strong inhibition |
|
| 4.1.1.11 | succinate |
- |
|
