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Literature summary extracted from
- Molecular modeling and docking of recombinant HAP-phytase of a thermophilic mould Sporotrichum thermophile reveals insights into molecular catalysis and biochemical properties (2018), Int. J. Biol. Macromol., 115, 501-508 .
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 3.1.3.8 | recombinant overexpression in Pichia pastoris strain X-33 using inducible promoter AOX1, the enzyme is secreted | Thermothelomyces heterothallicus |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.1.3.8 | 2,3-Butanedione | strong inhibition, interacts with arginine residues | Thermothelomyces heterothallicus |  |
| 3.1.3.8 | meta-vanadate | - |
Thermothelomyces heterothallicus | |
| 3.1.3.8 | additional information | inhibitor docking study, overview. The enzyme is protease resistant | Thermothelomyces heterothallicus | |
| 3.1.3.8 | myo-inositol hexasulfate | a potent competitive inhibitor for phytase | Thermothelomyces heterothallicus | |
| 3.1.3.8 | Phenylglyoxal | interacts with arginine residues. Phenylglyoxal does not show any inhibition under acidic pH 5.0 | Thermothelomyces heterothallicus | |
| 3.1.3.8 | phosphate | - |
Thermothelomyces heterothallicus | |
| 3.1.3.8 | tartaric acid | - |
Thermothelomyces heterothallicus | |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 3.1.3.8 | 0.159 | - |
myo-inositol hexakisphosphate | substrate sodium phytate, pH 5.0, 60°C, recombinant enzyme | Thermothelomyces heterothallicus | |
| 3.1.3.8 | 0.208 | - |
myo-inositol hexakisphosphate | substrate potassium phytate, pH 5.0, 60°C, recombinant enzyme | Thermothelomyces heterothallicus | |
| 3.1.3.8 | 0.667 | - |
myo-inositol hexakisphosphate | substrate calcium phytate, pH 5.0, 60°C, recombinant enzyme | Thermothelomyces heterothallicus | |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.1.3.8 | additional information | the enzyme shows no requirement for metal ions | Thermothelomyces heterothallicus |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.1.3.8 | myo-inositol hexakisphosphate + H2O | Thermothelomyces heterothallicus | - |
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.1.3.8 | Thermothelomyces heterothallicus | - |
i.e. Myceliophthora thermophila or Sporotrichum thermophile strain BJTLR50 | - |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 3.1.3.8 | recombinant extracellular phytase from Pichia pastoris strain X-33 culture medium by lyophilization, dialysis, and anion exchange chromatography | Thermothelomyces heterothallicus |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.1.3.8 | additional information | the recombinant enzyme displayed broad substrate specificity. Molecular modeling and docking of phytase with various substrates show differential binding patterns, overview. Strong binding affinity with ATP and phytic acid, while the lowest with AMP and phosphoenol pyruvate. The enzyme is also active with ATP and 4-nitrophenyl phosphate | Thermothelomyces heterothallicus | ? | - |
? | |
| 3.1.3.8 | myo-inositol hexakisphosphate + H2O | - |
Thermothelomyces heterothallicus | 1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate | - |
? | |
| 3.1.3.8 | myo-inositol hexakisphosphate + H2O | substrates are sodium phytate, potassium phytate, and calcium phytate. Highest activity with calcium phytate | Thermothelomyces heterothallicus | 1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 3.1.3.8 | ? | x * 70000, recombinant enzyme, SDS-PAGE | Thermothelomyces heterothallicus |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.1.3.8 | HAP-phytase | - |
Thermothelomyces heterothallicus |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.1.3.8 | 60 | - |
- |
Thermothelomyces heterothallicus |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.1.3.8 | 5 | - |
- |
Thermothelomyces heterothallicus |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 3.1.3.8 | additional information | structure of the active site pocket of phytase protein, homology modeling of HAP-phytase, overview | Thermothelomyces heterothallicus |
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