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Literature summary for 3.1.3.26 extracted from
- Expression and characterization of Aspergillus thermostable phytases in Pichia pastoris (2009), FEMS Microbiol. Lett., 290, 18-24.
Application
| Application | Comment | Organism |
|---|---|---|
| biotechnology | in vitro digestibility tests show recombinantly expressed phytase is at least as efficient as commercial phytase for hydrolyzing phytate in corn-based animal feed and is therefore suitable sources of phytase supplement | Aspergillus japonicus |
| biotechnology | in vitro digestibility tests show recombinantly expressed phytase is at least as efficient as commercial phytase for hydrolyzing phytate in corn-based animal feed and is therefore suitable sources of phytase supplement | Aspergillus niger |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| recombinantly expressed as active extracellular, glycosylated proteins in Pichia pastoris | Aspergillus japonicus |
| recombinantly expressed as active extracellular, glycosylated proteins in Pichia pastoris | Aspergillus niger |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.08 | - |
myo-inositol hexakisphosphate | phytic acid dipotassium salt | Aspergillus japonicus |  |
| 0.14 | - |
myo-inositol hexakisphosphate | phytic acid sodium salt | Aspergillus japonicus | |
| 0.15 | - |
myo-inositol hexakisphosphate | phytic acid sodium salt | Aspergillus niger | |
| 0.16 | - |
myo-inositol hexakisphosphate | phytic acid dipotassium salt | Aspergillus niger | |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| extracellular | - |
Aspergillus japonicus | - |
- |
| extracellular | - |
Aspergillus niger | - |
- |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Ca2+ | stimulatory effect | Aspergillus japonicus | |
| Ca2+ | stimulatory effect | Aspergillus niger | |
| Cu2+ | inhibitory effect | Aspergillus japonicus | |
| Cu2+ | inhibitory effect | Aspergillus niger | |
| Fe2+ | stimulatory effect | Aspergillus japonicus | |
| Fe2+ | stimulatory effect | Aspergillus niger | |
| Mg2+ | stimulatory effect | Aspergillus japonicus | |
| Mg2+ | stimulatory effect | Aspergillus niger | |
| Mn2+ | stimulatory effect | Aspergillus japonicus | |
| Mn2+ | stimulatory effect | Aspergillus niger | |
| Ni2+ | stimulatory effect | Aspergillus japonicus | |
| Ni2+ | stimulatory effect | Aspergillus niger | |
| Sr2+ | stimulatory effect | Aspergillus japonicus | |
| Sr2+ | stimulatory effect | Aspergillus niger | |
| Zn2+ | inhibitory effect | Aspergillus japonicus | |
| Zn2+ | inhibitory effect | Aspergillus niger | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 66000 | - |
SDS-PAGE | Aspergillus japonicus |
| 66000 | - |
SDS-PAGE | Aspergillus niger |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Aspergillus japonicus | B3VPB2 | BCC18313 (TR86), 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 (3-phytase) or 1D-myo-inositol 1,2,3,5,6-pentakisphosphate (4-phytase) (i.e. 1L-myo-inositol 1,2,3,4,5-pentakisphosphate if 1L numbering is applied) has not been analyzed. The reaction was monitored by analyzing the released phosphate | - |
| Aspergillus niger | B3VPB3 | BCC18081 (TR170), 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 (3-phytase) or 1D-myo-inositol 1,2,3,5,6-pentakisphosphate (4-phytase) (i.e. 1L-myo-inositol 1,2,3,4,5-pentakisphosphate if 1L numbering is applied) has not been analyzed. The reaction was monitored by analyzing the released phosphate | - |
Posttranslational Modification
| Posttranslational Modification | Comment | Organism |
|---|---|---|
| glycoprotein | - |
Aspergillus japonicus |
| glycoprotein | - |
Aspergillus niger |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| myo-inositol hexakisphosphate + H2O | 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 (3-phytase) or 1D-myo-inositol 1,2,3,5,6-pentakisphosphate (4-phytase) (i.e. 1L-myo-inositol 1,2,3,4,5-pentakisphosphate if 1L numbering is applied) has not been analyzed. The reaction was monitored by analyzing the released phosphate | Aspergillus japonicus | ? + phosphate | - |
? | |
| myo-inositol hexakisphosphate + H2O | 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 (3-phytase) or 1D-myo-inositol 1,2,3,5,6-pentakisphosphate (4-phytase) (i.e. 1L-myo-inositol 1,2,3,4,5-pentakisphosphate if 1L numbering is applied) has not been analyzed. The reaction was monitored by analyzing the released phosphate | Aspergillus niger | ? + phosphate | - |
? | |
| myo-inositol hexakisphosphate + H2O | 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 (3-phytase) or 1D-myo-inositol 1,2,3,5,6-pentakisphosphate (4-phytase) (i.e. 1L-myo-inositol 1,2,3,4,5-pentakisphosphate if 1L numbering is applied) has not been analyzed. The reaction was monitored by analyzing the released phosphate | Aspergillus japonicus BCC18313 | ? + phosphate | - |
? | |
| myo-inositol hexakisphosphate + H2O | 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 (3-phytase) or 1D-myo-inositol 1,2,3,5,6-pentakisphosphate (4-phytase) (i.e. 1L-myo-inositol 1,2,3,4,5-pentakisphosphate if 1L numbering is applied) has not been analyzed. The reaction was monitored by analyzing the released phosphate | Aspergillus niger BCC18081 | ? + phosphate | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| phytase | - |
Aspergillus japonicus |
| phytase | - |
Aspergillus niger |
| r-PhyA170 | - |
Aspergillus niger |
| r-PhyA86 | - |
Aspergillus japonicus |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 50 | - |
- |
Aspergillus japonicus |
| 50 | - |
- |
Aspergillus niger |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| additional information | - |
more than 50% activity is retained after heating at 100°C for 10 min | Aspergillus japonicus |
| additional information | - |
more than 50% activity is retained after heating at 100°C for 10 min | Aspergillus niger |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 231 | - |
myo-inositol hexakisphosphate | phytic acid sodium salt | Aspergillus japonicus | |
| 253.5 | - |
myo-inositol hexakisphosphate | phytic acid dipotassium salt | Aspergillus niger | |
| 279.3 | - |
myo-inositol hexakisphosphate | phytic acid dipotassium salt | Aspergillus japonicus | |
| 281 | - |
myo-inositol hexakisphosphate | phytic acid sodium salt | Aspergillus niger | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 5.5 | - |
- |
Aspergillus japonicus |
| 5.5 | - |
- |
Aspergillus niger |
pH Stability
| pH Stability | pH Stability Maximum | Comment | Organism |
|---|---|---|---|
| 2 | 8 | - |
Aspergillus japonicus |
| 2 | 8 | - |
Aspergillus niger |
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