Application | Comment | Organism |
---|---|---|
additional information | has great potential for cofactor regeneration | Pseudomonas stutzeri |
Cloned (Comment) | Organism |
---|---|
His6-tagged PTDH overexpressed in Escherichia coli BL21(DE3) harboring a pET15b vector | Pseudomonas stutzeri |
Protein Variants | Comment | Organism |
---|---|---|
D79A | significant differences in its kinetic constants compared to the wild-type enzyme. 2600fold decrease in catalytic efficiency. Pre-steady-state rates are approximately the same as the steady-state rates | Pseudomonas stutzeri |
D79N | has kinetic parameters more similar to those of wild-type | Pseudomonas stutzeri |
E266Q | higher activity, steady-state and pre-steady-state rates are comparable | Pseudomonas stutzeri |
K76A | pre-steady-state rates are approximately the same as the steady-state rates | Pseudomonas stutzeri |
additional information | thermostable mutant 12X-PTDH with higher solubility than the wild-type. Thermostable mutant with dual cofactor specificity NADP-12X NAD shows pre-steady-state behavior very similar to that observed with 12X-PTDH and the wild-type enzyme. Pre-steady-state traces of thermostable mutant with dual cofactor specificity NADP-12X NADP shows curvature with NADP, particularly with protiated phosphite | Pseudomonas stutzeri |
R237K | low activity, absence of a significant burst in the pre-steady-state | Pseudomonas stutzeri |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
additional information | slow steps after hydride transfer do not significantly limit the rate of reaction for the wild-type enzyme, the active site mutants, or the thermostable mutant | Pseudomonas stutzeri |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.001 | - |
phosphite | mutant R237K | Pseudomonas stutzeri | |
0.012 | - |
NAD+ | mutant D79N | Pseudomonas stutzeri | |
0.035 | - |
NAD+ | wild-type | Pseudomonas stutzeri | |
0.035 | - |
phosphite | mutant D79N | Pseudomonas stutzeri | |
0.055 | - |
phosphite | wild-type | Pseudomonas stutzeri | |
0.062 | - |
NAD+ | mutant D79A | Pseudomonas stutzeri | |
1 | - |
NAD+ | mutant R237K | Pseudomonas stutzeri | |
1.2 | - |
phosphite | mutant D79A | Pseudomonas stutzeri |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Pseudomonas stutzeri | - |
- |
- |
Pseudomonas stutzeri WW88 | - |
- |
- |
Purification (Comment) | Organism |
---|---|
on Ni2+ affinity resin | Pseudomonas stutzeri |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
phosphite + H2O + NAD+ | Asp79 is important in orienting Arg237 for proper interaction with phosphite | Pseudomonas stutzeri | phosphate + NADH + H+ | - |
? | |
phosphite + H2O + NAD+ | Asp79 is important in orienting Arg237 for proper interaction with phosphite | Pseudomonas stutzeri WW88 | phosphate + NADH + H+ | - |
? |
Synonyms | Comment | Organism |
---|---|---|
phosphite dehydrogenase | - |
Pseudomonas stutzeri |
PTDH | - |
Pseudomonas stutzeri |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.0126 | - |
phosphite | mutant R237K | Pseudomonas stutzeri | |
0.0305 | - |
phosphite | mutant D79A | Pseudomonas stutzeri | |
0.23 | - |
phosphite | mutant D79N | Pseudomonas stutzeri | |
0.58 | - |
phosphite | mutant NADP-12X NAD | Pseudomonas stutzeri | |
0.621 | - |
phosphite | mutant K76A | Pseudomonas stutzeri | |
2.04 | - |
phosphite | mutant NADP-12X NAD | Pseudomonas stutzeri | |
2.42 | - |
phosphite | wild-type | Pseudomonas stutzeri | |
3.26 | - |
phosphite | thermostable mutant 12X-PTDH | Pseudomonas stutzeri | |
7.5 | - |
phosphite | mutant E266Q | Pseudomonas stutzeri |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NAD(P)+ | - |
Pseudomonas stutzeri |