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Literature summary for 3.1.3.26 extracted from

  • Demir, Y.; Dikbas, N.; Beydemir, S.
    Purification and biochemical characterization of phytase enzyme from Lactobacillus coryniformis (MH121153) (2018), Mol. Biotechnol., 60, 783-790 .
    View publication on PubMed
Search for more literature for 3.1.3.26

Inhibitors

Inhibitors Comment Organism Structure
Pb2+ slight inhibition at 5 mM Loigolactobacillus coryniformis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.32
-
 myo-inositol hexakisphosphate sodium phytate, pH 5.0, 60°C Loigolactobacillus coryniformis

Metals/Ions

Metals/Ions Comment Organism Structure
Cu2+ slight activation at 5 mM Loigolactobacillus coryniformis
additional information Ca2+, Ag+, Mg2+, Co2+, Zn2+, and Ni2+ have poor effects at 1-5 mM Loigolactobacillus coryniformis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
myo-inositol hexakisphosphate + H2O Loigolactobacillus coryniformis phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26 1D-myo-inositol pentakisphosphate + phosphate
-
 ?
myo-inositol hexakisphosphate + H2O Loigolactobacillus coryniformis MH121153 phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26 1D-myo-inositol pentakisphosphate + phosphate
-
 ?

Organism

Organism UniProt Comment Textmining
Loigolactobacillus coryniformis
-
 isolated from Lor cheese samples
-
Loigolactobacillus coryniformis MH121153
-
 isolated from Lor cheese samples
-

Purification (Commentary)

Purification (Comment) Organism
native enzyme 9.53fold by ammonium sulfate fractionation, anion exchange chromatography, and gel filtration Loigolactobacillus coryniformis

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
202.25
-
 purified native enzyme, pH 5.0, 60°C Loigolactobacillus coryniformis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the enzyme is also active with glucose 6-phosphate, but not with NADP+, ATP, and diphosphate Loigolactobacillus coryniformis ?
-
 ?
additional information the enzyme is also active with glucose 6-phosphate, but not with NADP+, ATP, and diphosphate Loigolactobacillus coryniformis MH121153 ?
-
 ?
myo-inositol hexakisphosphate + H2O phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26 Loigolactobacillus coryniformis 1D-myo-inositol pentakisphosphate + phosphate
-
 ?
myo-inositol hexakisphosphate + H2O phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26, preferred substrate is sodium phytate Loigolactobacillus coryniformis 1D-myo-inositol pentakisphosphate + phosphate
-
 ?
myo-inositol hexakisphosphate + H2O phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26 Loigolactobacillus coryniformis MH121153 1D-myo-inositol pentakisphosphate + phosphate
-
 ?
myo-inositol hexakisphosphate + H2O phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26, preferred substrate is sodium phytate Loigolactobacillus coryniformis MH121153 1D-myo-inositol pentakisphosphate + phosphate
-
 ?

Subunits

Subunits Comment Organism
? x * 43250, SDS_PAGE Loigolactobacillus coryniformis

Synonyms

Synonyms Comment Organism
More cf. EC 3.1.3.8 Loigolactobacillus coryniformis
phytase
-
 Loigolactobacillus coryniformis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
60
-
-
 Loigolactobacillus coryniformis

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
10 80 purified native enzyme, over 70% activity remains after 180 h Loigolactobacillus coryniformis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5
-
-
 Loigolactobacillus coryniformis

pH Stability

pH Stability pH Stability Maximum Comment Organism
2 12 purified native enzyme, over 65% activity remains after 96 h Loigolactobacillus coryniformis

General Information

General Information Comment Organism
evolution the enzyme belongs to the histidine acid phosphatase (HAP) family Loigolactobacillus coryniformis