Any feedback?
Literature summary for 3.1.3.8 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)
| Cloned (Comment) | Organism |
|---|---|
| gene phyB, sequence comparisons and phylogenetic analysis | Priestia aryabhattai |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| Co2+ | - |
Priestia aryabhattai |  |
| Cu2+ | - |
Priestia aryabhattai | |
| EDTA | - |
Priestia aryabhattai | |
| Fe2+ | - |
Priestia aryabhattai | |
| Mn2+ | - |
Priestia aryabhattai | |
| Zn2+ | - |
Priestia aryabhattai | |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| extracellular | - |
Priestia aryabhattai | - |
- |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Ca2+ | activates at 20 mM by 17% | Priestia aryabhattai | |
| Mg2+ | activates at 20 mM by 32% | Priestia aryabhattai | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 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 | - |
? | |
| 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
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Priestia aryabhattai | - |
isolated from chickpea (Cicer arietinum) rhizosphere | - |
| Priestia aryabhattai RS1 | - |
isolated from chickpea (Cicer arietinum) rhizosphere | - |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| 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]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 72.97 | - |
purified enzyme, pH 6.5, 40°C | Priestia aryabhattai |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | no considerable activity with other phosphorylated substrates like ATP, ADP, dSPP, pNPP, glucose 6-phosphate, and fructose 6-phosphate | Priestia aryabhattai | ? | - |
? | |
| additional information | no considerable activity with other phosphorylated substrates like ATP, ADP, dSPP, pNPP, glucose 6-phosphate, and fructose 6-phosphate | Priestia aryabhattai RS1 | ? | - |
? | |
| 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 | - |
? | |
| 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 | - |
? | |
| 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 | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 40000, about, SDS-PAGE | Priestia aryabhattai |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| More | cf. EC 3.1.3.26 | Priestia aryabhattai |
| PhyB | - |
Priestia aryabhattai |
| phytase | - |
Priestia aryabhattai |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 40 | - |
- |
Priestia aryabhattai |
Temperature Range [°C]
| Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 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]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 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
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 6.5 | - |
- |
Priestia aryabhattai |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| 3.5 | 9.5 | activity range, profile overview | Priestia aryabhattai |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
