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Literature summary extracted from
- A novel extracellular low-temperature active phytase from Bacillus aryabhattai RS1 with potential application in plant growth (2017), Biotechnol. Prog., 33, 633-641 .
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 3.1.3.8 | gene phyB, sequence comparisons and phylogenetic analysis | Priestia aryabhattai |
| 3.1.3.26 | gene phyB, sequence comparisons and phylogenetic analysis | Priestia aryabhattai |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.1.3.8 | Co2+ | - |
Priestia aryabhattai |  |
| 3.1.3.8 | Cu2+ | - |
Priestia aryabhattai | |
| 3.1.3.8 | EDTA | - |
Priestia aryabhattai | |
| 3.1.3.8 | Fe2+ | - |
Priestia aryabhattai | |
| 3.1.3.8 | Mn2+ | - |
Priestia aryabhattai | |
| 3.1.3.8 | Zn2+ | - |
Priestia aryabhattai | |
| 3.1.3.26 | Co2+ | - |
Priestia aryabhattai | |
| 3.1.3.26 | Cu2+ | - |
Priestia aryabhattai | |
| 3.1.3.26 | EDTA | - |
Priestia aryabhattai | |
| 3.1.3.26 | Fe2+ | - |
Priestia aryabhattai | |
| 3.1.3.26 | Mn2+ | - |
Priestia aryabhattai | |
| 3.1.3.26 | Zn2+ | - |
Priestia aryabhattai | |
Localization
| EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|---|
| 3.1.3.8 | extracellular | - |
Priestia aryabhattai | - |
- |
| 3.1.3.26 | extracellular | - |
Priestia aryabhattai | - |
- |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.1.3.8 | Ca2+ | activates at 20 mM by 17% | Priestia aryabhattai | |
| 3.1.3.8 | Mg2+ | activates at 20 mM by 32% | Priestia aryabhattai | |
| 3.1.3.26 | Ca2+ | activates at 20 mM by 17% | Priestia aryabhattai | |
| 3.1.3.26 | Mg2+ | activates at 20 mM by 32% | Priestia aryabhattai | |
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 | Priestia aryabhattai | phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26 | 1D-myo-inositol pentakisphosphate + phosphate | - |
? | |
| 3.1.3.8 | myo-inositol hexakisphosphate + H2O | Priestia aryabhattai RS1 | phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26 | 1D-myo-inositol pentakisphosphate + phosphate | - |
? | |
| 3.1.3.26 | myo-inositol hexakisphosphate + H2O | Priestia aryabhattai | phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26 | 1D-myo-inositol pentakisphosphate + phosphate | - |
? | |
| 3.1.3.26 | myo-inositol hexakisphosphate + H2O | Priestia aryabhattai RS1 | phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26 | 1D-myo-inositol pentakisphosphate + phosphate | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.1.3.8 | Priestia aryabhattai | - |
isolated from chickpea (Cicer arietinum) rhizosphere | - |
| 3.1.3.8 | Priestia aryabhattai RS1 | - |
isolated from chickpea (Cicer arietinum) rhizosphere | - |
| 3.1.3.26 | Priestia aryabhattai | - |
isolated from chickpea (Cicer arietinum) rhizosphere | - |
| 3.1.3.26 | Priestia aryabhattai RS1 | - |
isolated from chickpea (Cicer arietinum) rhizosphere | - |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 3.1.3.8 | native extracellular enzyme 20.84fold from cell culture supernatant by ethanol precipitation, gel filtration, and anion exchange chromatography | Priestia aryabhattai |
| 3.1.3.26 | native extracellular enzyme 20.84fold from cell culture supernatant by ethanol precipitation, gel filtration, and anion exchange chromatography | Priestia aryabhattai |
Specific Activity [micromol/min/mg]
| EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|---|
| 3.1.3.8 | 72.97 | - |
purified enzyme, pH 6.5, 40°C | Priestia aryabhattai |
| 3.1.3.26 | 72.97 | - |
purified enzyme, pH 6.5, 40°C | Priestia aryabhattai |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.1.3.8 | additional information | no considerable activity with other phosphorylated substrates like ATP, ADP, dSPP, pNPP, glucose 6-phosphate, and fructose 6-phosphate | Priestia aryabhattai | ? | - |
? | |
| 3.1.3.8 | additional information | no considerable activity with other phosphorylated substrates like ATP, ADP, dSPP, pNPP, glucose 6-phosphate, and fructose 6-phosphate | Priestia aryabhattai RS1 | ? | - |
? | |
| 3.1.3.8 | myo-inositol hexakisphosphate + H2O | phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26 | Priestia aryabhattai | 1D-myo-inositol pentakisphosphate + phosphate | - |
? | |
| 3.1.3.8 | myo-inositol hexakisphosphate + H2O | absolutely specific for the substrate, the phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26 | Priestia aryabhattai | 1D-myo-inositol pentakisphosphate + phosphate | - |
? | |
| 3.1.3.8 | myo-inositol hexakisphosphate + H2O | phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26 | Priestia aryabhattai RS1 | 1D-myo-inositol pentakisphosphate + phosphate | - |
? | |
| 3.1.3.26 | additional information | no considerable activity with other phosphorylated substrates like ATP, ADP, dSPP, pNPP, glucose 6-phosphate, and fructose 6-phosphate | Priestia aryabhattai | ? | - |
? | |
| 3.1.3.26 | additional information | no considerable activity with other phosphorylated substrates like ATP, ADP, dSPP, pNPP, glucose 6-phosphate, and fructose 6-phosphate | Priestia aryabhattai RS1 | ? | - |
? | |
| 3.1.3.26 | myo-inositol hexakisphosphate + H2O | phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26 | Priestia aryabhattai | 1D-myo-inositol pentakisphosphate + phosphate | - |
? | |
| 3.1.3.26 | myo-inositol hexakisphosphate + H2O | absolutely specific for, the phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26 | Priestia aryabhattai | 1D-myo-inositol pentakisphosphate + phosphate | - |
? | |
| 3.1.3.26 | myo-inositol hexakisphosphate + H2O | phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26 | Priestia aryabhattai RS1 | 1D-myo-inositol pentakisphosphate + phosphate | - |
? | |
| 3.1.3.26 | myo-inositol hexakisphosphate + H2O | absolutely specific for, the phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26 | Priestia aryabhattai RS1 | 1D-myo-inositol pentakisphosphate + phosphate | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 3.1.3.8 | ? | x * 40000, about, SDS-PAGE | Priestia aryabhattai |
| 3.1.3.26 | ? | x * 40000, about, SDS-PAGE | Priestia aryabhattai |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.1.3.8 | More | cf. EC 3.1.3.26 | Priestia aryabhattai |
| 3.1.3.8 | PhyB | - |
Priestia aryabhattai |
| 3.1.3.8 | phytase | - |
Priestia aryabhattai |
| 3.1.3.26 | More | cf. EC 3.1.3.8 | Priestia aryabhattai |
| 3.1.3.26 | PhyB | - |
Priestia aryabhattai |
| 3.1.3.26 | phytase | - |
Priestia aryabhattai |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.1.3.8 | 40 | - |
- |
Priestia aryabhattai |
| 3.1.3.26 | 40 | - |
- |
Priestia aryabhattai |
Temperature Range [°C]
| EC Number | Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.1.3.8 | 10 | 40 | the enzyme exhibits markedly higher activity at low temperature with retention of 65% and 43% of the optimum activity at reaction temperature 25°C and 10°C, respectively | Priestia aryabhattai |
| 3.1.3.26 | 10 | 40 | the enzyme exhibits markedly higher activity at low temperature with retention of 65% and 43% of the optimum activity at reaction temperature 25°C and 10°C, respectively | Priestia aryabhattai |
Temperature Stability [°C]
| EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.1.3.8 | 10 | 50 | purified enzyme, 30 min, pH 6.5, in presence of 20 mM Ca2+, completely stable, 40% activity is retained at 10°C. The enzyme is more thermostable in presence of CaCl2 and exhibits almost 100% residual activity at temperature range 20-50°C and 63% activity at 70°C after 30 min of preincubation, followed by sharp decline in thermostability | Priestia aryabhattai |
| 3.1.3.26 | 10 | 50 | purified enzyme, 30 min, pH 6.5, in presence of 20 mM Ca2+, completely stable, 40% activity is retained at 10°C. The enzyme is more thermostable in presence of CaCl2 and exhibits almost 100% residual activity at temperature range 20-50°C and 63% activity at 70°C after 30 min of preincubation, followed by sharp decline in thermostability | Priestia aryabhattai |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.1.3.8 | 6.5 | - |
- |
Priestia aryabhattai |
| 3.1.3.26 | 6.5 | - |
- |
Priestia aryabhattai |
pH Range
| EC Number | pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.1.3.8 | 3.5 | 9.5 | activity range, profile overview | Priestia aryabhattai |
| 3.1.3.26 | 3.5 | 9.5 | activity range, profile overview | Priestia aryabhattai |
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Release 2023.1 (January 2023)
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