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Literature summary extracted from

  • Farhat, A.; Chouayekh, H.; Ben Farhat, M.; Bouchaala, K.; Bejar, S.
    Gene cloning and characterization of a thermostable phytase from Bacillus subtilis US417 and assessment of its potential as a feed additive in comparison with a commercial enzyme (2008), Mol. Biotechnol., 40, 127-135.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.1.3.8 EDTA 1 mM, complete inhibition Bacillus subtilis
3.1.3.26 EDTA
-
 Bacillus subtilis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.1.3.8 0.52
-
 myo-inositol hexakisphosphate pH 7.5, 55°C Bacillus subtilis
3.1.3.26 0.52
-
 myo-inositol hexakisphosphate
-
 Bacillus subtilis

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.1.3.8 Ca2+ required Bacillus subtilis
3.1.3.26 Ca2+ enzyme is Ca2+-dependent, drastically improves thermal stability of the enzyme Bacillus subtilis

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.1.3.8 41800
-
 x * 41800, calculated Bacillus subtilis
3.1.3.26 41000
-
 SDS-PAGE Bacillus subtilis
3.1.3.26 41800
-
 deduced from cDNA Bacillus subtilis

Organism

EC Number Organism UniProt Comment Textmining
3.1.3.8 Bacillus subtilis Q84B22
-
-
3.1.3.8 Bacillus subtilis US417 Q84B22
-
-
3.1.3.26 Bacillus subtilis B1GSN6 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
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.1.3.26 using fast-performance liquid chromatography (FPLC) using a PL aquagel-OH 40 column from Agilent Bacillus subtilis

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 25
-
 pH 7.5, 55°C Bacillus subtilis
3.1.3.26 25
-
 purified enzyme Bacillus subtilis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.3.8 ADP + H2O 80% of the activity with myo-inositol hexakisphosphate Bacillus subtilis ? + phosphate
-
 ?
3.1.3.8 ADP + H2O 80% of the activity with myo-inositol hexakisphosphate Bacillus subtilis US417 ? + phosphate
-
 ?
3.1.3.8 AMP + H2O 10% of the activity with myo-inositol hexakisphosphate Bacillus subtilis adenosine + phosphate
-
 ?
3.1.3.8 AMP + H2O 10% of the activity with myo-inositol hexakisphosphate Bacillus subtilis US417 adenosine + phosphate
-
 ?
3.1.3.8 ATP + H2O 97% of the activity with myo-inositol hexakisphosphate Bacillus subtilis ? + phosphate
-
 ?
3.1.3.8 ATP + H2O 97% of the activity with myo-inositol hexakisphosphate Bacillus subtilis US417 ? + phosphate
-
 ?
3.1.3.8 myo-inositol hexakisphosphate + H2O
-
 Bacillus subtilis 1D-myo-inositol 1,2,4,5,6-pentakisphosphate + 1D-myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
 ?
3.1.3.8 myo-inositol hexakisphosphate + H2O
-
 Bacillus subtilis US417 1D-myo-inositol 1,2,4,5,6-pentakisphosphate + 1D-myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
 ?
3.1.3.26 ADP + H2O
-
 Bacillus subtilis AMP + phosphate
-
 ?
3.1.3.26 ATP + H2O
-
 Bacillus subtilis ADP + phosphate
-
 ?
3.1.3.26 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 Bacillus subtilis ? + phosphate
-
 ?

Subunits

EC Number Subunits Comment Organism
3.1.3.8 ? x * 41800, calculated Bacillus subtilis

Synonyms

EC Number Synonyms Comment Organism
3.1.3.26 PHY US417
-
 Bacillus subtilis
3.1.3.26 phytase
-
 Bacillus subtilis

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.1.3.8 55
-
-
 Bacillus subtilis
3.1.3.26 37
-
 assay at Bacillus subtilis
3.1.3.26 55
-
-
 Bacillus subtilis

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.1.3.8 60
-
 10 min, 22% of initial activity, absence of Ca2+ Bacillus subtilis
3.1.3.8 75
-
 10 min, 77% of initial activity, presence of 5 mM Ca2+ Bacillus subtilis
3.1.3.26 additional information
-
 in the presence CaCl2, PHY US417 recoveres 77% of its activity after incubation at 75°C for 10 min. In the absence of calcium, even so PHY US417 is absolutely stable when incubated for 30 min at 50°C it retains only 22% of activity after 10 min at 60°C Bacillus subtilis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.1.3.8 7.5
-
-
 Bacillus subtilis
3.1.3.26 5.5
-
 assay at Bacillus subtilis
3.1.3.26 7.5
-
-
 Bacillus subtilis

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.1.3.26 6 8
-
 Bacillus subtilis

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
3.1.3.26 2 9
-
 Bacillus subtilis