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Literature summary for 3.1.3.26 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

Inhibitors Comment Organism Structure
EDTA
-
Bacillus subtilis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.52
-
myo-inositol hexakisphosphate
-
Bacillus subtilis

Metals/Ions

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

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
41000
-
SDS-PAGE Bacillus subtilis
41800
-
deduced from cDNA Bacillus subtilis

Organism

Organism UniProt Comment Textmining
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)

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

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
25
-
purified enzyme Bacillus subtilis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ADP + H2O
-
Bacillus subtilis AMP + phosphate
-
?
ATP + H2O
-
Bacillus subtilis ADP + phosphate
-
?
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
-
?

Synonyms

Synonyms Comment Organism
PHY US417
-
Bacillus subtilis
phytase
-
Bacillus subtilis

Temperature Optimum [°C]

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

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
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

pH Optimum Minimum pH Optimum Maximum Comment Organism
5.5
-
assay at Bacillus subtilis
7.5
-
-
Bacillus subtilis

pH Range

pH Minimum pH Maximum Comment Organism
6 8
-
Bacillus subtilis

pH Stability

pH Stability pH Stability Maximum Comment Organism
2 9
-
Bacillus subtilis