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Literature summary for 3.1.3.26 extracted from

  • Fu, S.; Sun, J.; Qian, L.; Li, Z.
    Bacillus phytases: present scenario and future perspectives (2008), Appl. Biochem. Biotechnol., 151, 1-8.
    View publication on PubMed

Application

Application Comment Organism
biotechnology phytase from Bacillus subtilis (168phyA) is constitutively expressed in tobacco and Arabidopsis to generate transgenic plants capable of utilizing exogenous phytate. In tobacco, phytase activities in transgenic leaf and root extracts are seven to eight times higher than those in wild-type extracts; whereas, the extracellular phytase activities of transgenic plants are enhanced by four to six times. Similar results are observed from the transgenic Arabidopsis. These results may offer a new perspective on mobilizing soil phytate into inorganic phosphate for plant uptake Bacillus subtilis
biotechnology phytase from Bacillus subtilis is introduced into the cytoplasm of tobacco cells that results in equilibrium shift of inositol biosynthesis pathway, thereby making more phosphate available for primary metabolism. The transgenic line exhibit phenotypic changes like increased flowering, lower seed IP6/IP5 ratio, and enhanced growth under phosphate starvation conditions compared to wild type Bacillus subtilis
biotechnology phytase is very suitable to be used in animal feed particularly in common carp feed because of its optimum pH with excellent thermal stability. Bacillus phytase supplementation of 300 U/kg can gain the same result as that of 1000 U/kg supplementation of acidic phytase and neutral phytase supplementation of 1000 U/kg can replace the inorganic phosphorus supplement. A combination of Bacillus phytases and other acidic phytases might induce a more effective hydrolysis of phytate in both the stomach and small intestine of animals in terms of the pH of the animal gastrointestinal tract Bacillus sp. (in: Bacteria)

Cloned(Commentary)

Cloned (Comment) Organism
overexpressed the phytase gene phyL from Bacillus licheniformis and phytase gene (168phyA) identified from Bacillus subtilis strain 168 in Bacillus subtilis using a omega105MU331 prophage vector system. Up to 35 U/ml are secreted into the culture media. Both phytases exhibit broad temperature and pH optima and show high thermal stability Bacillus subtilis
overexpressed the phytase gene phyL from Bacillus licheniformis and phytase gene (168phyA) identified from Bacillus subtilis strain 168 in Bacillus subtilis using a omega105MU331 prophage vector system. Up to 35 U/ml are secreted into the culture media. Both phytases exhibit broad temperature and pH optima and show high thermal stability Bacillus licheniformis

Crystallization (Commentary)

Crystallization (Comment) Organism
crystal structure of the phytase from Bacillus amyloliquefaciens DS11 demonstrate that a negatively charged active site provides a favorable electrostatic environment for the positively charged calcium-phytate complex Bacillus amyloliquefaciens
determined at 2.1 A resolution in partially and fully Ca2+-loaded states. Two calcium ions form a biocalcium center where the Asp308 carboxylate serves as a bridging arm, stabilizing the circular arrangement of the propeller structure. Three calcium ions at the active site form a triadic calcium center and neutralize an otherwise negatively charged calcium cage surrounded by a total of six aspartate and glutamate residues. The top of the molecular structure forms a shallow cleft that is lined predominantly with negatively charged side chains. The calcium-occupied cleft turns into a favorable electrostatic environment for the binding of phytate together with nearby Lys76, Lys77, Arg122, and Lys179. In addition, Ca2+ participates in catalysis directly by binding the phosphate group(s) of the substrate. Ca2+ reduces the negative charge around the active site cleft such that phytate neutralized by Ca2+ can easily fit to the active site Bacillus amyloliquefaciens

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular
-
Bacillus sp. (in: Bacteria)
-
-

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ enhances thermal stablity and shows an impact on pH-optimum and temperature optimum Bacillus sp. (in: Bacteria)

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
36000
-
molecular weight: 36 - 38 kDa Bacillus subtilis
36500
-
-
Bacillus subtilis
44000
-
-
Bacillus sp. (in: Bacteria)

Organism

Organism UniProt Comment Textmining
Bacillus amyloliquefaciens
-
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
-
Bacillus licheniformis
-
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
-
Bacillus sp. (in: Bacteria)
-
-
-
Bacillus sp. (in: Bacteria)
-
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
-
Bacillus sp. (in: Bacteria) KHU-10
-
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
-
Bacillus subtilis
-
-
-
Bacillus subtilis
-
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
-
Sporolactobacillus laevolacticus
-
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
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
specific activity of the purified protein: 8.5-9 U/mg Bacillus subtilis
additional information
-
specific activity of the purified protein: 8.7 U/mg Bacillus subtilis
additional information
-
specific activity of the purified protein: 8.7 U/mg Bacillus sp. (in: Bacteria)
additional information
-
specific activity of the purified protein: 8.7 U/mg Sporolactobacillus laevolacticus

Synonyms

Synonyms Comment Organism
(natto) phytase
-
Bacillus subtilis
(natto) phytase
-
Bacillus sp. (in: Bacteria)
168phyA
-
Bacillus subtilis
phyL
-
Bacillus licheniformis
phytase
-
Bacillus subtilis
phytase
-
Bacillus sp. (in: Bacteria)
phytase
-
Bacillus amyloliquefaciens
phytase
-
Sporolactobacillus laevolacticus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
40
-
without 10 mM CaCl2 Bacillus sp. (in: Bacteria)
60
-
-
Bacillus subtilis
60
-
with 10 mM CaCl2 Bacillus sp. (in: Bacteria)
70
-
-
Sporolactobacillus laevolacticus

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
additional information
-
phyL exhibits high thermal stability, even at a lower calcium concentration, as it is able to recover 80% of its original activity after denaturation at 95 °C for 10 min Bacillus licheniformis
70
-
80% activity at 70°C and pH 8.0 for up to 3 h Sporolactobacillus laevolacticus
70
-
enzyme is stable up to 70°C Bacillus subtilis
80
-
about 50% of its original activity remains after incubation at 80°C for 10 min in the presence of 10 mM CaCl2 Bacillus sp. (in: Bacteria)

pH Range

pH Minimum pH Maximum Comment Organism
6 6.5
-
Bacillus subtilis
6.5 8.5 without 10 mM CaCl2 Bacillus sp. (in: Bacteria)
6.5 9.5 with 10 mM CaCl2 Bacillus sp. (in: Bacteria)
7 8
-
Sporolactobacillus laevolacticus
7 7.5
-
Bacillus subtilis

pH Stability

pH Stability pH Stability Maximum Comment Organism
6.5 10
-
Bacillus sp. (in: Bacteria)