EC Number   |
Inhibitors |
Structure |
|---|
    1.17.1.8 | (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate |
dihydrodipicolinate reductase enzymes from plants are much more prone to substrate inhibition than the bacterial enzymes, which appears to be a consequence of increased flexibility of the substrate-binding loop and higher affinity for the nucleotide substrate |
   |
| 1.17.1.8 | (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate |
when NADPH is employed as the cofactor |
|
| 1.17.1.8 | (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinate |
- |
|
| 1.17.1.8 | 1,10-phenanthroline |
- |
|
| 1.17.1.8 | 2,3-dihydrodipicolinate |
the enzyme is inhibited by high concentrations of 2,3-dihydrodipicolinate |
|
| 1.17.1.8 | 2,6-pyridine dicarboxylate |
stable analog of the dihydrodipicolinate substrate, the binding affinity is not affected by the presence of NADH or NAD+ |
|
| 1.17.1.8 | 2,6-pyridinedicarboxylate |
competitive, binding site structure |
|
| 1.17.1.8 | 2,6-pyridinedicarboxylic acid |
- |
|
| 1.17.1.8 | 2,6-pyridinedicarboxylic acid |
dead-end inhibitor |
|
| 1.17.1.8 | 2-pyridine carboxylic acid |
- |
|
