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Literature summary for 2.7.4.1 extracted from
- Rational design of substrate binding pockets in polyphosphate kinase for use in cost-effective ATP-dependent cascade reactions (2017), Appl. Microbiol. Biotechnol., 101, 5325-5332 .
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| A106E | mutant enzyme does not show any detectable activity | Sinorhizobium meliloti |
| A106E/H102K | mutant enzyme does not show any detectable activity | Sinorhizobium meliloti |
| A106E/V115T | mutant enzyme does not show any detectable activity | Sinorhizobium meliloti |
| H102K | mutant enzyme does not show any detectable activity | Sinorhizobium meliloti |
| H102K/A106E/V115T | mutant enzyme H102K/A106E/V115T exhibits the capability to utilize polyP(4) as phosphate donor to synthesize ATP. The wild-type enzyme can not adopt polyphosphate(4) | Sinorhizobium meliloti |
| V115T | mutant enzyme does not show any detectable activity | Sinorhizobium meliloti |
| V115T/H102K | mutant enzyme does not show any detectable activity | Sinorhizobium meliloti |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| polyphosphate(4) | short polyphosphates inhibit the enzyme by blocking the ADP binding pocket | Corynebacterium glutamicum | |
| polyphosphate(4) | short polyphosphates inhibit the enzyme by blocking the ADP binding pocket | Sinorhizobium meliloti |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.03 | - |
ADP | pH 8.0, 30°C, wild-type enzyme | Corynebacterium glutamicum |  |
| 2.3 | - |
ADP | pH 8.0, 30°C, mutant enzyme H102K/A106E/V115T | Sinorhizobium meliloti | |
| 15.2 | - |
polyphosphate(4) | pH 8.0, 30°C, wild-type enzyme | Corynebacterium glutamicum | |
| 19 | - |
polyphosphate(4) | pH 8.0, 30°C, mutant enzyme H102K/A106E/V115T | Sinorhizobium meliloti |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ADP + (phosphate)n+1 | Corynebacterium glutamicum | polyphosphate kinases (PPKs) catalyzes the polyP formation or ATP formation, to store energy or to regenerate ATP, respectively | ATP + (phosphate)n | - |
r | |
| ADP + (phosphate)n+1 | Sinorhizobium meliloti | polyphosphate kinases (PPKs) catalyzes the polyP formation or ATP formation, to store energy or to regenerate ATP, respectively | ATP + (phosphate)n | - |
r | |
| ATP + (phosphate)n | Corynebacterium glutamicum | polyphosphate kinases (PPKs) catalyzes the polyP formation or ATP formation, to store energy or to regenerate ATP, respectively | ADP + (phosphate)n+1 | - |
r | |
| ATP + (phosphate)n | Sinorhizobium meliloti | polyphosphate kinases (PPKs) catalyzes the polyP formation or ATP formation, to store energy or to regenerate ATP, respectively | ADP + (phosphate)n+1 | - |
r | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Corynebacterium glutamicum | - |
- |
- |
| Sinorhizobium meliloti | Q92SA6 | - |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ADP + (phosphate)n+1 | - |
Corynebacterium glutamicum | ATP + (phosphate)n | - |
r | |
| ADP + (phosphate)n+1 | - |
Sinorhizobium meliloti | ATP + (phosphate)n | - |
r | |
| ADP + (phosphate)n+1 | polyphosphate kinases (PPKs) catalyzes the polyP formation or ATP formation, to store energy or to regenerate ATP, respectively | Corynebacterium glutamicum | ATP + (phosphate)n | - |
r | |
| ADP + (phosphate)n+1 | polyphosphate kinases (PPKs) catalyzes the polyP formation or ATP formation, to store energy or to regenerate ATP, respectively | Sinorhizobium meliloti | ATP + (phosphate)n | - |
r | |
| ADP + polyphosphate(4) | - |
Corynebacterium glutamicum | ATP + polyphosphate(3) | - |
? | |
| ADP + polyphosphate(4) | mutant enzyme H102K/A106E/V115T exhibits the capability to utilize polyP(4) as phosphate donor to synthesize ATP. The wild-type enzyme shows no activity with polyphosphate(4) | Sinorhizobium meliloti | ATP + polyphosphate(3) | - |
? | |
| ATP + (phosphate)n | - |
Corynebacterium glutamicum | ADP + (phosphate)n+1 | - |
r | |
| ATP + (phosphate)n | - |
Sinorhizobium meliloti | ADP + (phosphate)n+1 | - |
r | |
| ATP + (phosphate)n | polyphosphate kinases (PPKs) catalyzes the polyP formation or ATP formation, to store energy or to regenerate ATP, respectively | Corynebacterium glutamicum | ADP + (phosphate)n+1 | - |
r | |
| ATP + (phosphate)n | polyphosphate kinases (PPKs) catalyzes the polyP formation or ATP formation, to store energy or to regenerate ATP, respectively | Sinorhizobium meliloti | ADP + (phosphate)n+1 | - |
r | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| dimer | - |
Corynebacterium glutamicum |
| dimer | - |
Sinorhizobium meliloti |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| NCg12620 | - |
Corynebacterium glutamicum |
| SMc02148 | - |
Sinorhizobium meliloti |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 30 | - |
assay at | Corynebacterium glutamicum |
| 30 | - |
assay at | Sinorhizobium meliloti |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 2.9 | - |
ADP | pH 8.0, 30°C, mutant enzyme H102K/A106E/V115T | Sinorhizobium meliloti | |
| 5.6 | - |
polyphosphate(4) | pH 8.0, 30°C, wild-type enzyme | Corynebacterium glutamicum | |
| 9.1 | - |
ADP | pH 8.0, 30°C, wild-type enzyme | Corynebacterium glutamicum | |
| 15 | - |
polyphosphate(4) | pH 8.0, 30°C, mutant enzyme H102K/A106E/V115T | Sinorhizobium meliloti |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 8 | - |
assay at | Corynebacterium glutamicum |
| 8 | - |
assay at | Sinorhizobium meliloti |
General Information
| General Information | Comment | Organism |
|---|---|---|
| physiological function | polyphosphate kinases catalyzes the polyphosphate formation or ATP formation, to store energy or to regenerate ATP, respectively | Corynebacterium glutamicum |
| physiological function | polyphosphate kinases catalyzes the polyphosphate formation or ATP formation, to store energy or to regenerate ATP, respectively | Sinorhizobium meliloti |
kcat/KM [mM/s]
| kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.37 | - |
polyphosphate(4) | pH 8.0, 30°C, wild-type enzyme | Corynebacterium glutamicum | |
| 0.79 | - |
polyphosphate(4) | pH 8.0, 30°C, mutant enzyme H102K/A106E/V115T | Sinorhizobium meliloti | |
| 1.26 | - |
ADP | pH 8.0, 30°C, mutant enzyme H102K/A106E/V115T | Sinorhizobium meliloti | |
| 303.3 | - |
ADP | pH 8.0, 30°C, wild-type enzyme | Corynebacterium glutamicum | |
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