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Literature summary extracted from
- Improving the neutral phytase activity from Bacillus amyloliquefaciens DSM 1061 by site-directed mutagenesis (2015), Appl. Biochem. Biotechnol., 175, 3184-3194 .
Application
| EC Number | Application | Comment | Organism |
|---|---|---|---|
| 3.1.3.8 | agriculture | neutral phytase is used as a feed additive for degradation of anti-nutritional phytate in aquatic feed industry. Mutant phytases D148E and S197E with increased activities and thermostabilities have application potential as additives in aquaculture feed | Bacillus amyloliquefaciens |
| 3.1.3.8 | additional information | phytase has great potential applications not only in the areas of animal nutrition and resource conservation, but also in environmental protection and public health | Bacillus amyloliquefaciens |
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 3.1.3.8 | gene phyC, sequence comparisons, recombinant overexpression of His6-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3) | Bacillus amyloliquefaciens |
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 3.1.3.8 | D148E | site-directed mutagenesis, mutation on the surface, the specific activity of mutant D148E increases by about 35% over a temperature range of 40-75°C at pH 7.0 compared to wild-type. The mutant enzyme shows a much higher thermostability than the wild-type phytase | Bacillus amyloliquefaciens |
| 3.1.3.8 | D52E | site-directed mutagenesis, mutation in the active site, the mutation leads to significant loss of specific activity of the mutant compared to wild-type enzyme, probably because that the side chain of residue D52 is involved in formation of octahedral coordination shells with bridging water molecules in the active site | Bacillus amyloliquefaciens |
| 3.1.3.8 | N156E | site-directed mutagenesis, mutation on the surface, the mutation leads to significant loss of specific activity of the mutant compared to wild-type enzyme. The mutation site N156 is in the vicinity of residue Y159 which coordinates with Ca2+ by its hydroxyl group. The substitution of Glu for N156 may indirectly change the micro-environment around residue Y159, leading to the reduction in activity of phytase | Bacillus amyloliquefaciens |
| 3.1.3.8 | S197E | site-directed mutagenesis, mutation on the surface, the specific activity of mutant S197E increases by about 13% over a temperature range of 40-75°C at pH 7.0 compared to wild-type. The mutant enzyme shows a much higher thermostability than the wild-type phytase | Bacillus amyloliquefaciens |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 3.1.3.8 | additional information | - |
additional information | Michaelis-Menten kinetics | Bacillus amyloliquefaciens |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.1.3.8 | Ca2+ | activates | Bacillus amyloliquefaciens |  |
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 | Bacillus amyloliquefaciens | - |
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate | - |
? | |
| 3.1.3.8 | myo-inositol hexakisphosphate + H2O | Bacillus amyloliquefaciens DSM 1061 | - |
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.1.3.8 | Bacillus amyloliquefaciens | F4ZE79 | - |
- |
| 3.1.3.8 | Bacillus amyloliquefaciens DSM 1061 | F4ZE79 | - |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 3.1.3.8 | recombinant His6-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and dialysis | Bacillus amyloliquefaciens |
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 | 15.3 | - |
about, purified recombinant His-tagged wild-type PhyC, pH 7.0, 65°C | Bacillus amyloliquefaciens |
| 3.1.3.8 | 17.88 | - |
purified recombinant His-tagged mutant S197E, pH 7.0, 65°C | Bacillus amyloliquefaciens |
| 3.1.3.8 | 20.64 | - |
purified recombinant His-tagged mutant D148E, pH 7.0, 65°C | Bacillus amyloliquefaciens |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.1.3.8 | additional information | usage of chromogenic agent containing 1:3 mixture of 100 g/l ammonium molybdate, and 0.785 g/l ammonium metavanadate in 15% HNO3 for the phosphate product detection in enzyme assay | Bacillus amyloliquefaciens | ? | - |
? | |
| 3.1.3.8 | additional information | usage of chromogenic agent containing 1:3 mixture of 100 g/l ammonium molybdate, and 0.785 g/l ammonium metavanadate in 15% HNO3 for the phosphate product detection in enzyme assay | Bacillus amyloliquefaciens DSM 1061 | ? | - |
? | |
| 3.1.3.8 | myo-inositol hexakisphosphate + H2O | - |
Bacillus amyloliquefaciens | 1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate | - |
? | |
| 3.1.3.8 | myo-inositol hexakisphosphate + H2O | i.e. phytate | Bacillus amyloliquefaciens | 1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate | - |
? | |
| 3.1.3.8 | myo-inositol hexakisphosphate + H2O | - |
Bacillus amyloliquefaciens DSM 1061 | 1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate | - |
? | |
| 3.1.3.8 | myo-inositol hexakisphosphate + H2O | i.e. phytate | Bacillus amyloliquefaciens DSM 1061 | 1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 3.1.3.8 | ? | x * 41000, about, recombinant His6-tagged enzyme, SDS-PAGE | Bacillus amyloliquefaciens |
| 3.1.3.8 | More | molecular model of phytase constructed by homology modeling method, overview | Bacillus amyloliquefaciens |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.1.3.8 | neutral phytase | - |
Bacillus amyloliquefaciens |
| 3.1.3.8 | PhyC | - |
Bacillus amyloliquefaciens |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.1.3.8 | 60 | - |
recombinant mutants N156E and D52E | Bacillus amyloliquefaciens |
| 3.1.3.8 | 65 | - |
recombinant wild-type and mutants D148E and S197E | Bacillus amyloliquefaciens |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.1.3.8 | 7 | - |
assay at | Bacillus amyloliquefaciens |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 3.1.3.8 | additional information | Bacillus phytases exhibit their desirable activity profile at neutral pH. They have higher thermal stability, and strict substrate specificity for the calcium-phytate complex than that of acidic phytase. Molecular model of phytase constructed by homology modeling method using the structure with PDB ID 2POO as template, overview | Bacillus amyloliquefaciens |
| 3.1.3.8 | physiological function | phytase hydrolyzes phytate (myo-inositol 1,2,3,4,5,6-hexakisphosphate, IP6) and its salts present in cereals and legumes to release inorganic phosphate. It contributes to the removal of phytate, an anti-nutritional factor in feed, and thereby increases the bioavailability of phosphate, minerals, protein, and starch | Bacillus amyloliquefaciens |
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