EC Number   |
Inhibitors |
Structure |
|---|
   3.5.1.15 | aspartic acid |
0.002 M, 20-25% inhibition |
   |
| 3.5.1.15 | diisopropyl fluorophosphate |
- |
|
| 3.5.1.15 | glutamic acid |
0.002 M, 20-25% inhibition |
|
| 3.5.1.15 | Glycyl-L-aspartate |
- |
|
| 3.5.1.15 | methylphosphonamidate |
- |
|
| 3.5.1.15 | N-acetyl-aspartate |
decrease of the reaction rate at high substrate concentrations. Binding of N-acetyl-aspartate to the allosteric site induces significant rigidity to the protein loops with the amino acid side chains forming gates to the enzyme active site |
|
| 3.5.1.15 | N-acetyl-L-aspartate |
at low N-acetyl-L-aspartate concentrations, sigmoidal shape of kinetic curve is observed, followed by typicalrate growth of the enzyme-catalyzed reaction, whereas at high concentrations of N-acetyl-L-aspartate self-inhibition takes place. N-Acetylaspartate acts as activator at low concentrations, substrate at moderate concentrations, and inhibitor at high concentrations |
|
| 3.5.1.15 | N-acetyl-L-aspartate |
substrate inhibition at high concentration |
|
| 3.5.1.15 | N-acetylaspartic acid |
substrate inhibition at concentration above 0.2 mM |
|
| 3.5.1.15 | N-carbobenzoxy-D-aspartic acid |
- |
|
