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Literature summary for 2.7.9.1 extracted from
- Kinetic and molecular characterization of the pyruvate phosphate dikinase from Trypanosoma cruzi (2016), Exp. Parasitol., 165, 81-87.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| ammonium | activates up to 2.6fold | Trypanosoma cruzi |  |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene ppdk2 or ppdk1, recombinant His-tagged enzyme expression in Escherichia coli | Trypanosoma cruzi |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | steady-state kinetics, progress curves of the reaction for both the native and recombinant PPDK show non-linearity with the activity increasing until a steady state is reached after a significant delay | Trypanosoma cruzi | |
| 0.007 | - |
AMP | recombinant enzyme, pH 8.3, temperature not specified in the publication | Trypanosoma cruzi | |
| 0.017 | - |
diphosphate | recombinant enzyme, pH 8.3, temperature not specified in the publication | Trypanosoma cruzi | |
| 0.32 | - |
phosphoenolpyruvate | recombinant enzyme, pH 8.3, temperature not specified in the publication | Trypanosoma cruzi | |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| glycosome | - |
Trypanosoma cruzi | 20015 | - |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Mg2+ | required, activates 1.5fold at 7 mM | Trypanosoma cruzi | |
| additional information | no effect by Ca2+ and Mn2+ at 5-10 mM | Trypanosoma cruzi |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 100000 | - |
monomeric enzyme form, gel filtration | Trypanosoma cruzi |
| 200000 | - |
homdimeric enzyme form, gel filtration | Trypanosoma cruzi |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| AMP + phosphoenolpyruvate + diphosphate | Trypanosoma cruzi | - |
ATP + pyruvate + phosphate | - |
r | |
| ATP + pyruvate + phosphate | Trypanosoma cruzi | - |
AMP + phosphoenolpyruvate + diphosphate | - |
r | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Trypanosoma cruzi | Q9GN79 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant His-tagged enzyme from Escherichia coli by nickel affinityy chromatography, purification of native glycosomes | Trypanosoma cruzi |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| epimastigote | - |
Trypanosoma cruzi | - |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 0.005 | - |
native enzyme in purified glycosomes, pH 8.3, temperature not specified in the publication | Trypanosoma cruzi |
| 0.2 | - |
purified recombinant enzyme, pH 8.3, temperature not specified in the publication | Trypanosoma cruzi |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| AMP + phosphoenolpyruvate + diphosphate | - |
Trypanosoma cruzi | ATP + pyruvate + phosphate | - |
r | |
| ATP + pyruvate + phosphate | - |
Trypanosoma cruzi | AMP + phosphoenolpyruvate + diphosphate | - |
r | |
| additional information | coupled assay method with lactate dehydrogenase | Trypanosoma cruzi | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| monomer or dimer | - |
Trypanosoma cruzi |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| PPDK | - |
Trypanosoma cruzi |
| PPDK1 | - |
Trypanosoma cruzi |
| PPDK2 | - |
Trypanosoma cruzi |
| PPi-dependent pyruvate phosphate dikinase | - |
Trypanosoma cruzi |
| pyruvate phosphate dikinase | - |
Trypanosoma cruzi |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.11 | - |
phosphoenolpyruvate | recombinant enzyme, pH 8.3, temperature not specified in the publication | Trypanosoma cruzi | |
| 0.12 | - |
AMP | recombinant enzyme, pH 8.3, temperature not specified in the publication | Trypanosoma cruzi | |
| 0.14 | - |
diphosphate | recombinant enzyme, pH 8.3, temperature not specified in the publication | Trypanosoma cruzi | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.3 | - |
reverse reaction optimum | Trypanosoma cruzi |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| AMP | - |
Trypanosoma cruzi | |
| ATP | - |
Trypanosoma cruzi | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| physiological function | the diphosphate-dependent pyruvate phosphate dikinase, that converts phosphoenolpyruvate, diphosphate, and AMP into pyruvate, phosphate, and ATP, is the first enzyme of one branch of a two-branched glycolytic auxiliary system in glycosomes, thus contributing to the ATP/ADP balance within the glycosomes. During growth of epimastigotes in batch culture an apparent decrease in the specific activity of PPDK is observed | Trypanosoma cruzi |
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