Any feedback?
Literature summary extracted from
- Purification and biochemical characterization of phytase enzyme from Lactobacillus coryniformis (MH121153) (2018), Mol. Biotechnol., 60, 783-790 .
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.1.3.8 | Pb2+ | slight inhibition at 5 mM | Loigolactobacillus coryniformis |  |
| 3.1.3.26 | Pb2+ | slight inhibition at 5 mM | Loigolactobacillus coryniformis | |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 3.1.3.8 | 0.32 | - |
myo-inositol hexakisphosphate | sodium phytate, pH 5.0, 60°C | Loigolactobacillus coryniformis | |
| 3.1.3.26 | 0.32 | - |
myo-inositol hexakisphosphate | sodium phytate, pH 5.0, 60°C | Loigolactobacillus coryniformis | |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.1.3.8 | Cu2+ | slight activation at 5 mM | Loigolactobacillus coryniformis | |
| 3.1.3.8 | additional information | Ca2+, Ag+, Mg2+, Co2+, Zn2+, and Ni2+ have poor effects at 1-5 mM | Loigolactobacillus coryniformis | |
| 3.1.3.26 | Cu2+ | slight activation at 5 mM | Loigolactobacillus coryniformis | |
| 3.1.3.26 | additional information | Ca2+, Ag+, Mg2+, Co2+, Zn2+, and Ni2+ have poor effects at 1-5 mM | Loigolactobacillus coryniformis |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.1.3.8 | 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 | - |
? | |
| 3.1.3.8 | 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 | - |
? | |
| 3.1.3.26 | 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 | - |
? | |
| 3.1.3.26 | 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
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.1.3.8 | Loigolactobacillus coryniformis | - |
isolated from Lor cheese samples | - |
| 3.1.3.8 | Loigolactobacillus coryniformis MH121153 | - |
isolated from Lor cheese samples | - |
| 3.1.3.26 | Loigolactobacillus coryniformis | - |
isolated from Lor cheese samples | - |
| 3.1.3.26 | Loigolactobacillus coryniformis MH121153 | - |
isolated from Lor cheese samples | - |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 3.1.3.8 | native enzyme 9.53fold by ammonium sulfate fractionation, anion exchange chromatography, and gel filtration | Loigolactobacillus coryniformis |
| 3.1.3.26 | native enzyme 9.53fold by ammonium sulfate fractionation, anion exchange chromatography, and gel filtration | Loigolactobacillus coryniformis |
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 | 202.25 | - |
purified native enzyme, pH 5.0, 60°C | Loigolactobacillus coryniformis |
| 3.1.3.26 | 202.25 | - |
purified native enzyme, pH 5.0, 60°C | Loigolactobacillus coryniformis |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.1.3.8 | additional information | the enzyme is also active with glucose 6-phosphate, but not with NADP+, ATP, and diphosphate | Loigolactobacillus coryniformis | ? | - |
? | |
| 3.1.3.8 | additional information | the enzyme is also active with glucose 6-phosphate, but not with NADP+, ATP, and diphosphate | Loigolactobacillus coryniformis MH121153 | ? | - |
? | |
| 3.1.3.8 | 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 | - |
? | |
| 3.1.3.8 | 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 | - |
? | |
| 3.1.3.8 | 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 | - |
? | |
| 3.1.3.26 | additional information | the enzyme is also active with glucose 6-phosphate, but not with NADP+, ATP, and diphosphate | Loigolactobacillus coryniformis | ? | - |
? | |
| 3.1.3.26 | additional information | the enzyme is also active with glucose 6-phosphate, but not with NADP+, ATP, and diphosphate | Loigolactobacillus coryniformis MH121153 | ? | - |
? | |
| 3.1.3.26 | 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 | - |
? | |
| 3.1.3.26 | 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 | - |
? | |
| 3.1.3.26 | 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 | - |
? | |
| 3.1.3.26 | 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
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 3.1.3.8 | ? | x * 43250, SDS_PAGE | Loigolactobacillus coryniformis |
| 3.1.3.26 | ? | x * 43250, SDS_PAGE | Loigolactobacillus coryniformis |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.1.3.8 | More | cf. EC 3.1.3.26 | Loigolactobacillus coryniformis |
| 3.1.3.8 | phytase | - |
Loigolactobacillus coryniformis |
| 3.1.3.26 | More | cf. EC 3.1.3.8 | Loigolactobacillus coryniformis |
| 3.1.3.26 | phytase | - |
Loigolactobacillus coryniformis |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.1.3.8 | 60 | - |
- |
Loigolactobacillus coryniformis |
| 3.1.3.26 | 60 | - |
- |
Loigolactobacillus coryniformis |
Temperature Stability [°C]
| EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.1.3.8 | 10 | 80 | purified native enzyme, over 70% activity remains after 180 h | Loigolactobacillus coryniformis |
| 3.1.3.26 | 10 | 80 | purified native enzyme, over 70% activity remains after 180 h | Loigolactobacillus coryniformis |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.1.3.8 | 5 | - |
- |
Loigolactobacillus coryniformis |
| 3.1.3.26 | 5 | - |
- |
Loigolactobacillus coryniformis |
pH Stability
| EC Number | pH Stability | pH Stability Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.1.3.8 | 2 | 12 | purified native enzyme, over 65% activity remains after 96 h | Loigolactobacillus coryniformis |
| 3.1.3.26 | 2 | 12 | purified native enzyme, over 65% activity remains after 96 h | Loigolactobacillus coryniformis |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 3.1.3.8 | evolution | the enzyme belongs to the histidine acid phosphatase (HAP) family | Loigolactobacillus coryniformis |
| 3.1.3.26 | evolution | the enzyme belongs to the histidine acid phosphatase (HAP) family | Loigolactobacillus coryniformis |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
