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Literature summary extracted from
- Production of D-myo-inositol(1,2,4,5,6)pentakisphosphate using alginate-entrapped recombinant Pantoea agglomerans glucose-1-phosphatase (2008), Braz. Arch. Biol. Technol., 51, 235-246.
No PubMed abstract available
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 3.1.3.10 | expressed in Escherichia coli BL21(DE3), pET-22b(+) and pIP5 vectors | Pantoea agglomerans |
General Stability
| EC Number | General Stability | Organism |
|---|---|---|
| 3.1.3.10 | entrapped enzyme shows a high operational stability by retaining almost full activity even after ten uses | Pantoea agglomerans |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 3.1.3.10 | 0.35 | - |
myo-inositol hexakisphosphate | free enzyme, pH 4.5, 37°C | Pantoea agglomerans |  |
| 3.1.3.10 | 0.84 | - |
myo-inositol hexakisphosphate | entrapped enzyme, pH 4.5, 37°C | Pantoea agglomerans | |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.1.3.10 | D-glucose 1-phosphate + H2O | Pantoea agglomerans | - |
D-glucose + phosphate | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.1.3.10 | Pantoea agglomerans | Q1W5Y8 | - |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 3.1.3.10 | gel filtration | Pantoea agglomerans |
Specific Activity [micromol/min/mg]
| EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|---|
| 3.1.3.10 | additional information | - |
specific activities of recombinant enzymes similar to those of wild-type towards myo-inositol hexakisphosphate (i.e. phytate) and glucose 1-phosphate as substrates, entrapment in alginate beads, free enzyme looses less than 5% phosphatase activity within 2 h in 20 mM Tris-HCl buffer, pH 8.0, transfer limitation is responsible for the reduced reaction rate of the entrapped enzyme, complete conversion of myo-inositol hexakisphosphate into one single myo-inositol pentakisphosphate isomer, identified as D-myo-inositol(1,2,4,5,6)pentakisphosphate, shown to be feasible by using the enzyme-loaded alginate beads in batch operations | Pantoea agglomerans |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.1.3.10 | D-glucose 1-phosphate + H2O | - |
Pantoea agglomerans | D-glucose + phosphate | - |
? | |
| 3.1.3.10 | D-glucose 1-phosphate + H2O | activity of recombinant enzyme towards glucose 1-phosphate shown to be 4.8fold higher than activity towards myo-inositol hexakisphosphate (phytate), kinetic parameters affected by entrapment of the enzyme in alginate beads | Pantoea agglomerans | D-glucose + phosphate | - |
? | |
| 3.1.3.10 | myo-inositol hexakisphosphate + H2O | i.e. phytate, kinetic parameters affected by entrapment of the enzyme in alginate beads, conversion into one single myo-inositol pentakisphosphate isomer | Pantoea agglomerans | D-myo-inositol(1,2,4,5,6)pentakisphosphate + phosphate | - |
? | |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.1.3.10 | 60 | - |
free enzyme exhibits maximal activity at | Pantoea agglomerans |
| 3.1.3.10 | 70 | - |
maximum catalytic activity of entrapped enzyme at | Pantoea agglomerans |
Temperature Range [°C]
| EC Number | Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.1.3.10 | 25 | 80 | activities of free and entrapped enzyme determined at, dephosphorylation of myo-inositol hexakisphosphate (phytate) increases with raising temperature, compared to the free-form activity, reaction rate of the alginate reactor is markedly reduced, 30-75% depending on temperature | Pantoea agglomerans |
Temperature Stability [°C]
| EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.1.3.10 | additional information | - |
temperature stability enhanced as a consequence of entrapment in alginate beads | Pantoea agglomerans |
Turnover Number [1/s]
| EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 3.1.3.10 | 8 | - |
myo-inositol hexakisphosphate | entrapped enzyme, pH 4.5, dropped as a consequence of entrapment | Pantoea agglomerans | |
| 3.1.3.10 | 20.5 | - |
myo-inositol hexakisphosphate | free enzyme, pH 4.5 | Pantoea agglomerans | |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.1.3.10 | 4.5 | - |
determined for the free and the entrapped enzyme | Pantoea agglomerans |
pH Range
| EC Number | pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.1.3.10 | 3 | 8 | phytate dephosphorylation by the alginate reactor analyzed | Pantoea agglomerans |
pH Stability
| EC Number | pH Stability | pH Stability Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.1.3.10 | additional information | - |
pH dependence not affected by entrapment in alginate beads | Pantoea agglomerans |
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