EC Number   |
Specific Activity Minimum [µmol/min/mg] |
Specific Activity Maximum [µmol/min/mg] |
Reference  |
|---|
    4.3.3.7 | 458 |
- |
- |
33906 |
| 4.3.3.7 | -999 |
- |
- |
33902, 33905, 33907, 33908, 33911, 33915, 664244 |
| 4.3.3.7 | 100 |
- |
- |
33909 |
| 4.3.3.7 | 1.11 |
- |
purified enzyme |
649771 |
| 4.3.3.7 | 0.0034 |
- |
purified mutant T44V |
652939 |
| 4.3.3.7 | 0.008 |
- |
purified mutant Y133F |
652939 |
| 4.3.3.7 | 0.27 |
- |
purified mutant Y107F |
652939 |
| 4.3.3.7 | 1.81 |
- |
purified wild-type enzyme |
652939 |
| 4.3.3.7 | -999 |
- |
attempt to examine the specificity of the active site of DHDPS, co-crystallization with the substrate analogue oxaloacetate, solution of the protein structure indicates that pyruvate rather than oxaloacetic acid bounds in the active site, decarboxylation of oxaloacetate not catalysed by DHDPS, rate of pyruvate production independent of DHDPS concentration, indicating that the decarboxylation of oxaloacetate is occurring by a spontaneous and enzyme-independent mechanism, confirmed by kinetic analysis |
690252 |
| 4.3.3.7 | -999 |
- |
archetypal subunit orientation in the crystal structure of other dihydrodipicolinate synthase enzymes not observed, structure refinement will provide information regarding the structural evolution of dihydrodipicolinate synthase and the design of antibiotics targeting lysine biosynthesis in Staphylococcus aureus |
690266 |
