Cloned (Comment) | Organism |
---|---|
gene ppx1, recombinant overexpression in Saccharomyces cerevisiae strain CRN | Saccharomyces cerevisiae |
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 DELTAppx1, that shows increased polyphosphate levels | Saccharomyces cerevisiae |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
heparin | inhibits the endopolyphosphatase activity by 50% at 0.05 mg/ml | Saccharomyces cerevisiae |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.0033 | - |
cAMP | pH 7.2, 30°C, recombinant enzyme | Saccharomyces cerevisiae |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Saccharomyces cerevisiae | P38698 | - |
- |
Saccharomyces cerevisiae ATCC 204508 | P38698 | - |
- |
Purification (Comment) | Organism |
---|---|
recombinant enzyme PPX1 from Saccharomyces cerevisiae strain CRN by ammonium sulfate fractionation, anion exchange chromatography, heparin affinity chromatography, all alternating with ultrafiltration steps | Saccharomyces cerevisiae |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
240 | - |
purified recombinant enzyme, pH 7.2, 30°C | Saccharomyces cerevisiae |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
cAMP + H2O | - |
Saccharomyces cerevisiae | adenosine + phosphate | - |
? | |
cAMP + H2O | - |
Saccharomyces cerevisiae ATCC 204508 | adenosine + 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 | - |
? | |
guanosine tetraphosphate + H2O | - |
Saccharomyces cerevisiae ATCC 204508 | guanosine triphosphate + phosphate | - |
? | |
additional information | Ppx1 has high exopolyphosphatase activity (EC 3.6.1.11), but no endopolyphosphatase activity (EC 3.6.1.10). The Ppx1 activity with guanosine tetraphosphate is nearly 80% of activity with long-chain polyphosphates. Ppx1 does not hydrolyze ATP and dATP. Exopolyphosphatases (polyphosphate phosphohydrolases, EC 3.6.1.11) cleave phosphate from the end of the polyphosphate chain | Saccharomyces cerevisiae | ? | - |
- |
|
additional information | Ppx1 has high exopolyphosphatase activity (EC 3.6.1.11), but no endopolyphosphatase activity (EC 3.6.1.10). The Ppx1 activity with guanosine tetraphosphate is nearly 80% of activity with long-chain polyphosphates. Ppx1 does not hydrolyze ATP and dATP. Exopolyphosphatases (polyphosphate phosphohydrolases, EC 3.6.1.11) cleave phosphate from the end of the polyphosphate chain | Saccharomyces cerevisiae ATCC 204508 | ? | - |
- |
|
polyphosphate208 + H2O | - |
Saccharomyces cerevisiae | ? | - |
? | |
polyphosphate3 + H2O | - |
Saccharomyces cerevisiae | diphosphate + phosphate | - |
? |
Subunits | Comment | Organism |
---|---|---|
monomer | 1 * 45050, SDS-PAGE | Saccharomyces cerevisiae |
Synonyms | Comment | Organism |
---|---|---|
exopolyphosphatase | - |
Saccharomyces cerevisiae |
PPX1 | - |
Saccharomyces cerevisiae |
YHR201C | locus name | Saccharomyces cerevisiae |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
30 | - |
assay at | Saccharomyces cerevisiae |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.2 | - |
assay at | Saccharomyces cerevisiae |
General Information | Comment | Organism |
---|---|---|
evolution | the enzyme belongs to the DHH family of phosphoesterases. 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 | the enzyme PPN1 shows only exopolyphosphatase activity | Saccharomyces cerevisiae |