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Literature summary for 3.6.1.10 extracted from
- Ppn2 endopolyphosphatase overexpressed in Saccharomyces cerevisiae Comparison with Ppn1, Ppx1, and Ddp1 polyphosphatases (2019), Biochimie, 163, 101-107 .
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene ddp1, recombinant overexpression in Saccharomyces cerevisiae strain CRN | Saccharomyces cerevisiae |
| gene ppn1, recombinant overexpression in Saccharomyces cerevisiae strain CRN | Saccharomyces cerevisiae |
| gene ppn2, recombinant overexpression of the soluble enzyme in Saccharomyces cerevisiae strain CRN | Saccharomyces cerevisiae |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| additional information | construction of a Saccharomyces cerevisiae strain CRN overexpressing Ppn2 polyphosphatase and comparison the properties of polyphosphatases Ppn2, Ppx1, Ppn1, and Ddp1 purified from overexpressing strains of Saccharomyces cerevisiae, overview. Construction of deletion mutant DELTAdpp1, that shows increased polyphosphate levels | Saccharomyces cerevisiae |
| additional information | construction of a Saccharomyces cerevisiae strain CRN overexpressing Ppn2 polyphosphatase and comparison the properties of polyphosphatases Ppn2, Ppx1, Ppn1, and Ddp1 purified from overexpressing strains of Saccharomyces cerevisiae, overview. Construction of deletion mutant DELTAppn1, that shows increased polyphosphate levels | Saccharomyces cerevisiae |
| additional information | construction of a Saccharomyces cerevisiae strain CRN overexpressing Ppn2 polyphosphatase and comparison the properties of polyphosphatases Ppn2, Ppx1, Ppn1, and Ddp1 purified from overexpressing strains of Saccharomyces cerevisiae, overview. Construction of deletion mutant DELTAppn2, that shows increased polyphosphate levels | Saccharomyces cerevisiae |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| heparin | inhibits the endopolyphosphatase activity by 50% at 0.01 mg/ml; inhibits the endopolyphosphatase activity slightly at 0.25 mg/ml | Saccharomyces cerevisiae |  |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| vacuole | - |
Saccharomyces cerevisiae | 5773 | - |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Co2+ | stimulates the endopolyphosphatase activity at 0.01 mM | Saccharomyces cerevisiae | |
| Co2+ | stimulates the endopolyphosphatase activity at 0.1 mM | Saccharomyces cerevisiae | |
| Mg2+ | stimulates the endopolyphosphatase activity at 1 mM | Saccharomyces cerevisiae | |
| Zn2+ | stimulates the endopolyphosphatase activity at 0.01 mM | Saccharomyces cerevisiae | |
| Zn2+ | stimulates the endopolyphosphatase activity at 0.1 mM | Saccharomyces cerevisiae | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Saccharomyces cerevisiae | P40152 | - |
- |
| Saccharomyces cerevisiae | Q04119 | - |
- |
| Saccharomyces cerevisiae | Q99321 | - |
- |
| Saccharomyces cerevisiae ATCC 204508 | P40152 | - |
- |
| Saccharomyces cerevisiae ATCC 204508 | Q04119 | - |
- |
| Saccharomyces cerevisiae ATCC 204508 | Q99321 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant enzyme DPP1 from Saccharomyces cerevisiae strain CRN by anion exchange chromatography and ultrafiltration | Saccharomyces cerevisiae |
| recombinant enzyme PPN1 from Saccharomyces cerevisiae strain CRN by ammonium sulfate fractionation, anion exchange chromatography, heparin affinity chromatography, all alternating with ultrafiltration steps | Saccharomyces cerevisiae |
| recombinant enzyme PPN2 from Saccharomyces cerevisiae strain CRN by ammonium sulfate fractionation, anion exchange chromatography, heparin affinity chromatography, all alternating with ultrafiltration steps | Saccharomyces cerevisiae |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 0.05 | - |
purified recombinant enzyme, exopolyphosphatase activity, pH 7.2, 30°C | Saccharomyces cerevisiae |
| 0.1 | - |
purified recombinant enzyme, exopolyphosphatase activity, pH 7.2, 30°C | Saccharomyces cerevisiae |
| 30 | - |
purified recombinant enzyme, exopolyphosphatase activity in presence of 0.1 mM Co2+, substrate diphosphate, pH 7.2, 30°C | Saccharomyces cerevisiae |
| 40 | - |
purified recombinant enzyme, exopolyphosphatase activity in presence of 0.1 mM Co2+, substrate ATP, pH 7.2, 30°C | Saccharomyces cerevisiae |
| 80 | - |
purified recombinant enzyme, exopolyphosphatase activity in presence of 0.1 mM Co2+, substrate dATP, pH 7.2, 30°C | Saccharomyces cerevisiae |
| 190 | - |
purified recombinant enzyme, exopolyphosphatase activity in presence of 0.1 mM Co2+, substrate polyphosphate3, pH 7.2, 30°C | Saccharomyces cerevisiae |
| 210 | - |
purified recombinant enzyme, exopolyphosphatase activity in presence of 0.1 mM Co2+, substrate GTP, pH 7.2, 30°C | Saccharomyces cerevisiae |
| 420 | - |
purified recombinant enzyme, exopolyphosphatase activity in presence of 0.1 mM Co2+, substrate guanosine tetraphosphate, pH 7.2, 30°C | Saccharomyces cerevisiae |
| 530 | - |
purified recombinant enzyme, exopolyphosphatase activity in presence of 0.1 mM Co2+, substrate polyphosphate208, pH 7.2, 30°C | Saccharomyces cerevisiae |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + H2O | only in presence of Co2+, not with Mg2+, reaction of EC 3.6.1.1 | Saccharomyces cerevisiae | ADP + phosphate | - |
? | |
| ATP + H2O | only in presence of Co2+, not with Mg2+, reaction of EC 3.6.1.1 | Saccharomyces cerevisiae ATCC 204508 | ADP + phosphate | - |
? | |
| cAMP + H2O | - |
Saccharomyces cerevisiae | adenosine + phosphate | - |
? | |
| dATP + H2O | - |
Saccharomyces cerevisiae | dADP + phosphate | - |
? | |
| dATP + H2O | - |
Saccharomyces cerevisiae ATCC 204508 | dADP + phosphate | - |
? | |
| diphosphate + H2O | only in presence of Co2+, not with Mg2+, reaction of EC 3.6.1.1 | Saccharomyces cerevisiae | 2 phosphate | - |
? | |
| diphosphate + H2O | only in presence of Co2+, not with Mg2+, reaction of EC 3.6.1.1 | Saccharomyces cerevisiae ATCC 204508 | 2 phosphate | - |
? | |
| GTP + H2O | - |
Saccharomyces cerevisiae | GDP + phosphate | - |
? | |
| GTP + H2O | - |
Saccharomyces cerevisiae ATCC 204508 | GDP + phosphate | - |
? | |
| guanosine tetraphosphate + H2O | - |
Saccharomyces cerevisiae | guanosine triphosphate + phosphate | - |
? | |
| additional information | DPP1 has endopolyphosphatase activity (EC 3.6.1.10), and low exopolyphosphatase activity (EC 3.6.1.11). Exopolyphosphatases (polyphosphate phosphohydrolases) cleave phosphate from the end of the polyphosphate chain, whereas endopolyphosphatases (polyphosphate depolymerases) split long polyphosphate molecules into oligopolyphosphates | Saccharomyces cerevisiae | ? | - |
- |
|
| additional information | Ppn1 has endopolyphosphatase activity (EC 3.6.1.10), and high exopolyphosphatase activity (EC 3.6.1.11). The Ppn1 activity with guanosine tetraphosphate is nearly 80% of activity with long-chain polyphosphates. Ppn1 hydrolyzes dATP. Exopolyphosphatases (polyphosphate phosphohydrolases) cleave phosphate from the end of the polyphosphate chain, whereas endopolyphosphatases (polyphosphate depolymerases) split long polyphosphate molecules into oligopolyphosphates | Saccharomyces cerevisiae | ? | - |
- |
|
| additional information | Ppn2 has endopolyphosphatase activity (EC 3.6.1.10), and low exopolyphosphatase activity (EC 3.6.1.11). Exopolyphosphatases (polyphosphate phosphohydrolases) cleave phosphate from the end of the polyphosphate chain, whereas endopolyphosphatases (polyphosphate depolymerases) split long polyphosphate molecules into oligopolyphosphates | Saccharomyces cerevisiae | ? | - |
- |
|
| additional information | Ppn2 has endopolyphosphatase activity (EC 3.6.1.10), and low exopolyphosphatase activity (EC 3.6.1.11). Exopolyphosphatases (polyphosphate phosphohydrolases) cleave phosphate from the end of the polyphosphate chain, whereas endopolyphosphatases (polyphosphate depolymerases) split long polyphosphate molecules into oligopolyphosphates | Saccharomyces cerevisiae ATCC 204508 | ? | - |
- |
|
| additional information | Ppn1 has endopolyphosphatase activity (EC 3.6.1.10), and high exopolyphosphatase activity (EC 3.6.1.11). The Ppn1 activity with guanosine tetraphosphate is nearly 80% of activity with long-chain polyphosphates. Ppn1 hydrolyzes dATP. Exopolyphosphatases (polyphosphate phosphohydrolases) cleave phosphate from the end of the polyphosphate chain, whereas endopolyphosphatases (polyphosphate depolymerases) split long polyphosphate molecules into oligopolyphosphates | Saccharomyces cerevisiae ATCC 204508 | ? | - |
- |
|
| additional information | DPP1 has endopolyphosphatase activity (EC 3.6.1.10), and low exopolyphosphatase activity (EC 3.6.1.11). Exopolyphosphatases (polyphosphate phosphohydrolases) cleave phosphate from the end of the polyphosphate chain, whereas endopolyphosphatases (polyphosphate depolymerases) split long polyphosphate molecules into oligopolyphosphates | Saccharomyces cerevisiae ATCC 204508 | ? | - |
- |
|
| polyphosphate208 + H2O | - |
Saccharomyces cerevisiae | ? | - |
? | |
| polyphosphate208 + H2O | - |
Saccharomyces cerevisiae ATCC 204508 | ? | - |
? | |
| polyphosphate3 + H2O | - |
Saccharomyces cerevisiae | ? | - |
? | |
| polyphosphate3 + H2O | - |
Saccharomyces cerevisiae ATCC 204508 | ? | - |
? | |
| polyphosphate3 + H2O | - |
Saccharomyces cerevisiae | diphosphate + phosphate | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| homotetramer | 4 * 33000-35000, SDS-PAGE | Saccharomyces cerevisiae |
| monomer | 1 * 21570, SDS-PAGE | Saccharomyces cerevisiae |
| monomer | 1 * 37150, SDS-PAGE | Saccharomyces cerevisiae |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| DDP1 | - |
Saccharomyces cerevisiae |
| dual exo/endopolyphoshatase | - |
Saccharomyces cerevisiae |
| endopolyphosphatase | - |
Saccharomyces cerevisiae |
| More | cf. EC 3.6.1.60 | Saccharomyces cerevisiae |
| Ppn1 | - |
Saccharomyces cerevisiae |
| Ppn2 | - |
Saccharomyces cerevisiae |
| YDR452W | locus name | Saccharomyces cerevisiae |
| YNL217W | locus name | Saccharomyces cerevisiae |
| YOR163W | locus name | Saccharomyces cerevisiae |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 30 | - |
assay at | Saccharomyces cerevisiae |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.2 | - |
assay at | Saccharomyces cerevisiae |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | the enzyme belongs to the endopolyphosphatase Ppn1 family. Polyphosphatases Ppx1, Ppn1, Ddp1, and Ppn2 show distinct substrate specificities and levels of endo- and exopolyphosphatase activities, as well as distinct patterns of stimulation by metal ions. The differences in the mode of polyphosphate hydrolysis, substrate specificity, metal ion dependence and cell localization suggest distinct roles of these enzymes in yeast | Saccharomyces cerevisiae |
| evolution | the enzyme belongs to the Nudix hydrolase family. Polyphosphatases Ppx1, Ppn1, Ddp1, and Ppn2 show distinct substrate specificities and levels of endo- and exopolyphosphatase activities, as well as distinct patterns of stimulation by metal ions. The differences in the mode of polyphosphate hydrolysis, substrate specificity, metal ion dependence and cell localization suggest distinct roles of these enzymes in yeast | Saccharomyces cerevisiae |
| evolution | the enzyme belongs to the PPP superfamily of metallophosphatases. Polyphosphatases Ppx1, Ppn1, Ddp1, and Ppn2 show distinct substrate specificities and levels of endo- and exopolyphosphatase activities, as well as distinct patterns of stimulation by metal ions. The differences in the mode of polyphosphate hydrolysis, substrate specificity, metal ion dependence and cell localization suggest distinct roles of these enzymes in yeast | Saccharomyces cerevisiae |
| metabolism | diphosphoinositol polyphosphate phosphohydrolase (DDP1, EC 3.6.1.52) is also a diadenosine hexaphosphate hydrolase (AMP-forming) (EC 3.6.1.60) and shows endopolyphosphatase (EC 3.6.1.10) activity and exopolyphosphatase activity (EC 3.6.1.11) | Saccharomyces cerevisiae |
| metabolism | the enzyme PPN1 shows exo- and endopolyphosphatase activities, EC 3.6.1.11 and EC 3.6.1.10, respectively | Saccharomyces cerevisiae |
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