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Literature summary extracted from
- Characterization of the family I inorganic pyrophosphatase from Pyrococcus horikoshii OT3 (2005), Archaea, 1, 385-389.
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 3.6.1.1 | DNA and amino acid sequence determination and analysis, expression in Escherichia coli | Pyrococcus horikoshii |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.6.1.1 | Ca2+ | - |
Pyrococcus horikoshii |  |
| 3.6.1.1 | Co2+ | can substitute for Mg2+ at concentrations up to 0.5 mM, inhibitory above | Pyrococcus horikoshii | |
| 3.6.1.1 | fluoride | potent inhibition, IC50: 0.1 mM | Pyrococcus horikoshii | |
| 3.6.1.1 | Mn2+ | can substitute for Mg2+ at concentrations up to 0.5 mM, inhibitory above | Pyrococcus horikoshii | |
| 3.6.1.1 | Zn2+ | can substitute for Mg2+ at concentrations up to 0.5 mM, inhibitory above | Pyrococcus horikoshii | |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 3.6.1.1 | 0.113 | - |
diphosphate | pH 7.5, 60°C, recombinat enzyme | Pyrococcus horikoshii | |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.6.1.1 | Co2+ | can substitute for Mg2+ at concentrations up to 0.5 mM, inhibitory above | Pyrococcus horikoshii | |
| 3.6.1.1 | Mg2+ | required, best divalent cation, 5 mM, Km is 0.303 mM | Pyrococcus horikoshii | |
| 3.6.1.1 | Mn2+ | can substitute for Mg2+ at concentrations up to 0.5 mM, inhibitory above | Pyrococcus horikoshii | |
| 3.6.1.1 | additional information | no activation by Ni2+ | Pyrococcus horikoshii | |
| 3.6.1.1 | Zn2+ | can substitute for Mg2+ at concentrations up to 0.5 mM, inhibitory above | Pyrococcus horikoshii | |
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 3.6.1.1 | 20833 | - |
x * 24500, recombinant enzyme, SDS-PAGE, x * 20833, amino acid sequence calculation | Pyrococcus horikoshii |
| 3.6.1.1 | 24500 | - |
x * 24500, recombinant enzyme, SDS-PAGE, x * 20833, amino acid sequence calculation | Pyrococcus horikoshii |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.6.1.1 | diphosphate + H2O | Pyrococcus horikoshii | - |
2 phosphate | - |
? | |
| 3.6.1.1 | diphosphate + H2O | Pyrococcus horikoshii OT-3 | - |
2 phosphate | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.6.1.1 | Pyrococcus horikoshii | O59570 | strain OT3 | - |
| 3.6.1.1 | Pyrococcus horikoshii OT-3 | O59570 | strain OT3 | - |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 3.6.1.1 | recombinant enzyme from Escherichia coli by ion exchange chromatography and gel filtration | Pyrococcus horikoshii |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.6.1.1 | diphosphate + H2O | - |
Pyrococcus horikoshii | 2 phosphate | - |
? | |
| 3.6.1.1 | diphosphate + H2O | specific for | Pyrococcus horikoshii | 2 phosphate | - |
? | |
| 3.6.1.1 | diphosphate + H2O | - |
Pyrococcus horikoshii OT-3 | 2 phosphate | - |
? | |
| 3.6.1.1 | diphosphate + H2O | specific for | Pyrococcus horikoshii OT-3 | 2 phosphate | - |
? | |
| 3.6.1.1 | additional information | triphosphate, ATP, and ADP are poor substrates, AMP, phosphoenolpyruvate, and 4-nitrophenyl phosphate are no substrates | Pyrococcus horikoshii | ? | - |
? | |
| 3.6.1.1 | additional information | triphosphate, ATP, and ADP are poor substrates, AMP, phosphoenolpyruvate, and 4-nitrophenyl phosphate are no substrates | Pyrococcus horikoshii OT-3 | ? | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 3.6.1.1 | ? | x * 24500, recombinant enzyme, SDS-PAGE, x * 20833, amino acid sequence calculation | Pyrococcus horikoshii |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.6.1.1 | family I inorganic pyrophosphatase | - |
Pyrococcus horikoshii |
| 3.6.1.1 | family I PPase | - |
Pyrococcus horikoshii |
| 3.6.1.1 | PPase | - |
Pyrococcus horikoshii |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.6.1.1 | 70 | - |
- |
Pyrococcus horikoshii |
Temperature Range [°C]
| EC Number | Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.6.1.1 | 25 | 90 | activity range, high activity at 60-75°C | Pyrococcus horikoshii |
Temperature Stability [°C]
| EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.6.1.1 | 105 | - |
half-life about 50 min, recombinant enzyme | Pyrococcus horikoshii |
Turnover Number [1/s]
| EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 3.6.1.1 | 744 | - |
diphosphate | pH 7.5, 60°C, recombinat enzyme | Pyrococcus horikoshii | |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.6.1.1 | 7.5 | - |
assay at | Pyrococcus horikoshii |
IC50 Value
| EC Number | IC50 Value | IC50 Value Maximum | Comment | Organism | Inhibitor | Structure |
|---|---|---|---|---|---|---|
| 3.6.1.1 | 0.1 | - |
potent inhibition, IC50: 0.1 mM | Pyrococcus horikoshii | fluoride | |
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