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Literature summary for 3.1.3.8 extracted from
- Cloned and expressed fungal phyA gene in alfalfa produces a stable phytase (2002), Biochem. Biophys. Res. Commun., 290, 1343-1348.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expression in Medicago sativa leaves | Aspergillus ficuum |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| myo-inositol hexasulfate | - |
Aspergillus ficuum |  |
| Phenylglyoxal | - |
Aspergillus ficuum | |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.027 | - |
myo-inositol hexakisphosphate | pH 5.0, 58°C, native enzyme | Aspergillus ficuum | |
| 0.05 | - |
myo-inositol hexakisphosphate | pH 5.0, 58°C, recombinant enzyme | Aspergillus ficuum | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Aspergillus ficuum | - |
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified. | - |
Posttranslational Modification
| Posttranslational Modification | Comment | Organism |
|---|---|---|
| glycoprotein | - |
Aspergillus ficuum |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant enzyme | Aspergillus ficuum |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| additional information | - |
692.0 nKat/ml, recombinant enzyme | Aspergillus ficuum |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| myo-inositol hexakisphosphate + H2O | - |
Aspergillus ficuum | ? + phosphate | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| More | SDS-PAGE gives two broad bands in the regions 73000 Da and 100000 Da | Aspergillus ficuum |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 58 | - |
native and recombinant enzyme | Aspergillus ficuum |
Temperature Range [°C]
| Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 35 | 58 | 35°C: about 50% of maximal activity, 58°C: optimum, 68°C: enzyme is completely inactive, recombinant enzyme | Aspergillus ficuum |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 300 | - |
myo-inositol hexakisphosphate | pH 5.0, 58°C, recombinant enzyme | Aspergillus ficuum | |
| 348 | - |
myo-inositol hexakisphosphate | pH 5.0, 58°C, native enzyme | Aspergillus ficuum | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 5 | - |
recombinant enzyme | Aspergillus ficuum |
| 5 | 5.5 | native enzyme | Aspergillus ficuum |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| 2.5 | 6 | pH 2.5: about 35% of maximal activity, pH 6.0: about 25% of maximal activity, recombinant enzyme | Aspergillus ficuum |
Ki Value [mM]
| Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.00008 | - |
myo-inositol hexasulfate | pH 5.0, 58°C, recombinant enzyme | Aspergillus ficuum | |
| 0.0046 | - |
myo-inositol hexasulfate | pH 5.0, 58°C, native enzyme | Aspergillus ficuum | |
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