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Literature summary 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
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 2.7.4.1 | A106E | mutant enzyme does not show any detectable activity | Sinorhizobium meliloti |
| 2.7.4.1 | A106E/H102K | mutant enzyme does not show any detectable activity | Sinorhizobium meliloti |
| 2.7.4.1 | A106E/V115T | mutant enzyme does not show any detectable activity | Sinorhizobium meliloti |
| 2.7.4.1 | H102K | mutant enzyme does not show any detectable activity | Sinorhizobium meliloti |
| 2.7.4.1 | 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 |
| 2.7.4.1 | V115T | mutant enzyme does not show any detectable activity | Sinorhizobium meliloti |
| 2.7.4.1 | V115T/H102K | mutant enzyme does not show any detectable activity | Sinorhizobium meliloti |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 2.7.4.1 | polyphosphate(4) | short polyphosphates inhibit the enzyme by blocking the ADP binding pocket | Corynebacterium glutamicum | |
| 2.7.4.1 | polyphosphate(4) | short polyphosphates inhibit the enzyme by blocking the ADP binding pocket | Sinorhizobium meliloti |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 2.7.4.1 | 0.03 | - |
ADP | pH 8.0, 30°C, wild-type enzyme | Corynebacterium glutamicum |  |
| 2.7.4.1 | 2.3 | - |
ADP | pH 8.0, 30°C, mutant enzyme H102K/A106E/V115T | Sinorhizobium meliloti | |
| 2.7.4.1 | 15.2 | - |
polyphosphate(4) | pH 8.0, 30°C, wild-type enzyme | Corynebacterium glutamicum | |
| 2.7.4.1 | 19 | - |
polyphosphate(4) | pH 8.0, 30°C, mutant enzyme H102K/A106E/V115T | Sinorhizobium meliloti |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 2.7.4.1 | 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 | |
| 2.7.4.1 | 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 | |
| 2.7.4.1 | 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 | |
| 2.7.4.1 | 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
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 2.7.4.1 | Corynebacterium glutamicum | - |
- |
- |
| 2.7.4.1 | Sinorhizobium meliloti | Q92SA6 | - |
- |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 2.7.4.1 | ADP + (phosphate)n+1 | - |
Corynebacterium glutamicum | ATP + (phosphate)n | - |
r | |
| 2.7.4.1 | ADP + (phosphate)n+1 | - |
Sinorhizobium meliloti | ATP + (phosphate)n | - |
r | |
| 2.7.4.1 | 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 | |
| 2.7.4.1 | 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 | |
| 2.7.4.1 | ADP + polyphosphate(4) | - |
Corynebacterium glutamicum | ATP + polyphosphate(3) | - |
? | |
| 2.7.4.1 | 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) | - |
? | |
| 2.7.4.1 | ATP + (phosphate)n | - |
Corynebacterium glutamicum | ADP + (phosphate)n+1 | - |
r | |
| 2.7.4.1 | ATP + (phosphate)n | - |
Sinorhizobium meliloti | ADP + (phosphate)n+1 | - |
r | |
| 2.7.4.1 | 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 | |
| 2.7.4.1 | 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
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 2.7.4.1 | dimer | - |
Corynebacterium glutamicum |
| 2.7.4.1 | dimer | - |
Sinorhizobium meliloti |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 2.7.4.1 | NCg12620 | - |
Corynebacterium glutamicum |
| 2.7.4.1 | SMc02148 | - |
Sinorhizobium meliloti |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 2.7.4.1 | 30 | - |
assay at | Corynebacterium glutamicum |
| 2.7.4.1 | 30 | - |
assay at | Sinorhizobium meliloti |
Turnover Number [1/s]
| EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 2.7.4.1 | 2.9 | - |
ADP | pH 8.0, 30°C, mutant enzyme H102K/A106E/V115T | Sinorhizobium meliloti | |
| 2.7.4.1 | 5.6 | - |
polyphosphate(4) | pH 8.0, 30°C, wild-type enzyme | Corynebacterium glutamicum | |
| 2.7.4.1 | 9.1 | - |
ADP | pH 8.0, 30°C, wild-type enzyme | Corynebacterium glutamicum | |
| 2.7.4.1 | 15 | - |
polyphosphate(4) | pH 8.0, 30°C, mutant enzyme H102K/A106E/V115T | Sinorhizobium meliloti |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 2.7.4.1 | 8 | - |
assay at | Corynebacterium glutamicum |
| 2.7.4.1 | 8 | - |
assay at | Sinorhizobium meliloti |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 2.7.4.1 | physiological function | polyphosphate kinases catalyzes the polyphosphate formation or ATP formation, to store energy or to regenerate ATP, respectively | Corynebacterium glutamicum |
| 2.7.4.1 | 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]
| EC Number | kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 2.7.4.1 | 0.37 | - |
polyphosphate(4) | pH 8.0, 30°C, wild-type enzyme | Corynebacterium glutamicum | |
| 2.7.4.1 | 0.79 | - |
polyphosphate(4) | pH 8.0, 30°C, mutant enzyme H102K/A106E/V115T | Sinorhizobium meliloti | |
| 2.7.4.1 | 1.26 | - |
ADP | pH 8.0, 30°C, mutant enzyme H102K/A106E/V115T | Sinorhizobium meliloti | |
| 2.7.4.1 | 303.3 | - |
ADP | pH 8.0, 30°C, wild-type enzyme | Corynebacterium glutamicum | |
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