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Literature summary for 3.1.3.8 extracted from

  • Hong, S.; Chu, I.; Chung, K.
    Purification and biochemical characterization of thermostable phytase from newly isolated Bacillus subtilis CF92 (2011), J. Appl. Biol. Chem., 54, 89-94.
No PubMed abstract available
Search for more literature for 3.1.3.8

Activating Compound

Activating Compound Comment Organism Structure
EDTA
-
 Bacillus subtilis

Inhibitors

Inhibitors Comment Organism Structure
Ca2+
-
 Bacillus subtilis
Co2+
-
 Bacillus subtilis
Cu2+
-
 Bacillus subtilis
Fe2+
-
 Bacillus subtilis
Mg2+
-
 Bacillus subtilis
Mn2+
-
 Bacillus subtilis
Zn2+
-
 Bacillus subtilis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.42
-
 myo-inositol-1,2,3,4,5,6-hexakisphosphate pH 7.0, 37°C Bacillus subtilis

Metals/Ions

Metals/Ions Comment Organism Structure
additional information the enzyme is inhibited by metal ions Mn2+, Zn2+, Ca2+, Cu2+, Fe2+, Mg2+, and Co2+ Bacillus subtilis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
46000
-
 x * 46000, SDS-PAGE Bacillus subtilis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
myo-inositol-1,2,3,4,5,6-hexakisphosphate + H2O Bacillus subtilis
-
 ? + phosphate
-
 ?
myo-inositol-1,2,3,4,5,6-hexakisphosphate + H2O Bacillus subtilis CF92
-
 ? + phosphate
-
 ?

Organism

Organism UniProt Comment Textmining
Bacillus subtilis
-
 KCCM 90097
-
Bacillus subtilis CF92
-
 KCCM 90097
-

Purification (Commentary)

Purification (Comment) Organism
native enzyme 24fold by ethanol precipitation, anion exchange chromatography, and gel filtration Bacillus subtilis

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
79.3
-
 purified enzyme, pH 7.0, 37°C Bacillus subtilis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the native enzyme is also active on ADP, ATP, alpha- and beta-glycerophosphate, 2-naphthyl phosphate, and 4-nitrophenyl phosphate. No activity with sodium tripolyphosphate, fructose-6-phosphate, diphosphate, AMP Bacillus subtilis ?
-
 ?
additional information the native enzyme is also active on ADP, ATP, alpha- and beta-glycerophosphate, 2-naphthyl phosphate, and 4-nitrophenyl phosphate. No activity with sodium tripolyphosphate, fructose-6-phosphate, diphosphate, AMP Bacillus subtilis CF92 ?
-
 ?
myo-inositol-1,2,3,4,5,6-hexakisphosphate + H2O
-
 Bacillus subtilis ? + phosphate
-
 ?
myo-inositol-1,2,3,4,5,6-hexakisphosphate + H2O substrate Na-phytate Bacillus subtilis ? + phosphate
-
 ?
myo-inositol-1,2,3,4,5,6-hexakisphosphate + H2O
-
 Bacillus subtilis CF92 ? + phosphate
-
 ?
myo-inositol-1,2,3,4,5,6-hexakisphosphate + H2O substrate Na-phytate Bacillus subtilis CF92 ? + phosphate
-
 ?

Subunits

Subunits Comment Organism
? x * 46000, SDS-PAGE Bacillus subtilis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
60
-
-
 Bacillus subtilis

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
80
-
 purified native enzyme, 40% of original activity remaining after 30 min Bacillus subtilis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
-
 Bacillus subtilis

pH Range

pH Minimum pH Maximum Comment Organism
4 10 activity range, pH profile, overview Bacillus subtilis

pH Stability

pH Stability pH Stability Maximum Comment Organism
4 8 purified native enzyme, the activity remains fairly stable over pH range of pH 4.0 to pH 8.0, 83% of maxcimal activity remain after 6 h, pH profile, overview Bacillus subtilis