EC Number | Activating Compound | Comment | Organism | Structure |
---|---|---|---|---|
3.1.3.8 | butanol | slightly stimulates the phytase activity | Thermothelomyces heterothallicus | |
3.1.3.8 | hexane | slightly stimulates the phytase activity | Thermothelomyces heterothallicus | |
3.1.3.8 | isoamyl alcohol | slightly stimulates the phytase activity | Thermothelomyces heterothallicus | |
3.1.3.8 | additional information | the chelating agent EDTA has no discernible effect on the activity of rSt-Phy | Thermothelomyces heterothallicus |
EC Number | Application | Comment | Organism |
---|---|---|---|
3.1.3.8 | agriculture | enzyme rSt-Phy is useful in the dephytinization of broiler feeds efficiently in simulated gut conditions of chick leading to the liberation of soluble inorganic phosphate with concomitant mitigation in anti-nutrient effects of phytates | Thermothelomyces heterothallicus |
EC Number | Cloned (Comment) | Organism |
---|---|---|
1.11.1.18 | gene phyA, DNA and amino acid sequence determination and analysis, recombinant expression of the codon-optimized phytase gene in Pichia pastoris strain X-33, quantitative real-time PCR for gene copy number determination | Thermothelomyces thermophilus |
3.1.3.8 | gene phyA, DNA and amino acid sequence determination and analysis, recombinant expression of the codon-optimized phytase gene in Pichia pastoris strain X-33, quantitative real-time PCR for gene copy number determination | Thermothelomyces heterothallicus |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
1.11.1.18 | additional information | the enzyme is resistant to both pepsin and trypsin. The chelating agent EDTA has no discernible effect on the activity of rSt-Phy | Thermothelomyces thermophilus | |
3.1.3.8 | 2,3-Butanedione | - |
Thermothelomyces heterothallicus | |
3.1.3.8 | Al3+ | 23% inhibition at 5 mM | Thermothelomyces heterothallicus | |
3.1.3.8 | Co2+ | 10% inhibition at 5 mM | Thermothelomyces heterothallicus | |
3.1.3.8 | Cu2+ | 18% inhibition at 5 mM | Thermothelomyces heterothallicus | |
3.1.3.8 | Fe2+ | 12% inhibition at 5 mM | Thermothelomyces heterothallicus | |
3.1.3.8 | Fe3+ | 18% inhibition at 5 mM | Thermothelomyces heterothallicus | |
3.1.3.8 | guanidinium hydrochloride | - |
Thermothelomyces heterothallicus | |
3.1.3.8 | Mn2+ | 12% inhibition at 5 mM | Thermothelomyces heterothallicus | |
3.1.3.8 | additional information | the enzyme is resistant to both pepsin and trypsin. The chelating agent EDTA has no discernible effect on the activity of rSt-Phy | Thermothelomyces heterothallicus | |
3.1.3.8 | Na+ | 8% inhibition at 5 mM | Thermothelomyces heterothallicus | |
3.1.3.8 | potassium iodide | - |
Thermothelomyces heterothallicus | |
3.1.3.8 | Urea | - |
Thermothelomyces heterothallicus | |
3.1.3.8 | Woodward's reagent K | - |
Thermothelomyces heterothallicus | |
3.1.3.8 | Zn2+ | 61% inhibition at 5 mM | Thermothelomyces heterothallicus |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
3.1.3.8 | additional information | - |
additional information | kinetics and thermodynamics, overview | Thermothelomyces heterothallicus | |
3.1.3.8 | 0.147 | - |
myo-inositol hexakisphosphate | calcium phytate, pH 5.0, 60°C | Thermothelomyces heterothallicus |
EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|---|
1.11.1.18 | extracellular | the enzyme is secreted | Thermothelomyces thermophilus | - |
- |
3.1.3.8 | extracellular | the enzyme is secreted | Thermothelomyces heterothallicus | - |
- |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
3.1.3.8 | Ba2+ | activates | Thermothelomyces heterothallicus | |
3.1.3.8 | Mg2+ | activates | Thermothelomyces heterothallicus | |
3.1.3.8 | additional information | poor effect by Ca2+ at 1-5 mM | Thermothelomyces heterothallicus |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.1.3.8 | myo-inositol hexakisphosphate + H2O | Thermothelomyces heterothallicus | - |
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.11.1.18 | Thermothelomyces thermophilus | V5M269 | - |
- |
3.1.3.8 | Thermothelomyces heterothallicus | V5M269 | i.e. Sporotrichum thermophile or Myceliophthora thermophila | - |
EC Number | Posttranslational Modification | Comment | Organism |
---|---|---|---|
1.11.1.18 | glycoprotein | the enzyme is N-glycosylated, but also contains three potential O-glycosylation sites at positions 181, 185, and 268, it may be possible that the enzyme has one or more O-glycosylation. Deglycosylation using 10.0 U of endoglycosidase Hf (EndoHf) for 3 h at 37°C | Thermothelomyces thermophilus |
3.1.3.8 | glycoprotein | the enzyme is N-glycosylated, but also contains three potential O-glycosylation sites at positions 181, 185, and 268, it may be possible that the enzyme has one or more O-glycosylation. Deglycosylation using 10.0 U of endoglycosidase Hf (EndoHf) for 3 h at 37°C | Thermothelomyces heterothallicus |
EC Number | Purification (Comment) | Organism |
---|---|---|
1.11.1.18 | recombinant enzyme from Pichia pastoris strain X-33 by ultrafiltration, anion exchange chromatography, dialysis, and gel filtration | Thermothelomyces thermophilus |
3.1.3.8 | recombinant enzyme from Pichia pastoris strain X-33 by ultrafiltration, anion exchange chromatography, dialysis, and gel filtration | Thermothelomyces heterothallicus |
EC Number | Source Tissue | Comment | Organism | Textmining |
---|---|---|---|---|
1.11.1.18 | additional information | the thermophilic mold Sporotrichum thermophile produces very low titers of phytase extracellularly in both solid state and submerged fermentations | Thermothelomyces thermophilus | - |
3.1.3.8 | additional information | the thermophilic mold Sporotrichum thermophile produces very low titers of phytase extracellularly in both solid state and submerged fermentations | Thermothelomyces heterothallicus | - |
EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|---|
3.1.3.8 | 0.0524 | - |
purified native enzyme, pH 5.0, 60°C | Thermothelomyces heterothallicus |
3.1.3.8 | 46 | - |
purified recombinant enzyme, pH 5.0, 60°C | Thermothelomyces heterothallicus |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.11.1.18 | KBr + 2 H2O | - |
Thermothelomyces thermophilus | KH + HBr + H2O2 | - |
? | |
1.11.1.18 | additional information | besides its phytase activity (EC 3.1.3.8) with myo-inositol hexakisphosphate, the enzyme rSt-Phy also shows haloperoxidase activity. Enzyme rSt-Phy brings out a change in color of phenol red from red-orange to blue-violet in the presence of metavanadate ions, H2O2 and KBr in the reaction mixture, which confirms the bromoperoxidation of phenol red. Only histidine acid phosphatases with the active site sequence RHGXRXP can function as haloperoxidase, when vanadate ion is incorporated into the active site. Vanadate is a phosphate analogue, which is generally considered to bind as a transition state analogue to the phosphoryl transfer enzymes and inhibits their activities | Thermothelomyces thermophilus | ? | - |
? | |
3.1.3.8 | additional information | enzyme rSt-Phy also shows haloperoxidase activity with KBr, metavanadate, and H2O2, only histidine acid phosphatases with the active site sequence RHGXRXP can function as haloperoxidase, overview | Thermothelomyces heterothallicus | ? | - |
? | |
3.1.3.8 | myo-inositol hexakisphosphate + H2O | - |
Thermothelomyces heterothallicus | 1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate | - |
? | |
3.1.3.8 | myo-inositol hexakisphosphate + H2O | substrate is calcium phytate | Thermothelomyces heterothallicus | 1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
1.11.1.18 | ? | x * 70000, recombinant enzyme, SDS-PAGE, x * 90000, native enzyme, SDS-PAGE | Thermothelomyces thermophilus |
3.1.3.8 | ? | x * 70000, recombinant enzyme, SDS-PAGE, x * 90000, native enzyme, SDS-PAGE | Thermothelomyces heterothallicus |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.11.1.18 | HAP phytase | - |
Thermothelomyces thermophilus |
1.11.1.18 | More | cf. EC 3.1.3.8 | Thermothelomyces thermophilus |
1.11.1.18 | St-Phy | - |
Thermothelomyces thermophilus |
1.11.1.18 | vanadate haloperoxidase | - |
Thermothelomyces thermophilus |
3.1.3.8 | HAP phytase | - |
Thermothelomyces heterothallicus |
3.1.3.8 | More | cf. EC 1.11.1.18 | Thermothelomyces heterothallicus |
3.1.3.8 | St-Phy | - |
Thermothelomyces heterothallicus |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
1.11.1.18 | 37 | - |
assay at | Thermothelomyces thermophilus |
3.1.3.8 | 60 | - |
native and recombinant enzyme | Thermothelomyces heterothallicus |
EC Number | Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
---|---|---|---|---|
3.1.3.8 | 30 | 75 | activity range, profile overview | Thermothelomyces heterothallicus |
EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|---|
3.1.3.8 | 60 | - |
purified enzyme, pH 5.0, half-life of recombinant enzyme is 6 h and of native enzyme 16 h | Thermothelomyces heterothallicus |
3.1.3.8 | 80 | - |
purified enzyme, pH 5.0, half-life of recombinant enzyme is 1 h and of native enzyme 1.5 h | Thermothelomyces heterothallicus |
EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
3.1.3.8 | 1300 | - |
myo-inositol hexakisphosphate | calcium phytate, pH 5.0, 60°C | Thermothelomyces heterothallicus |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
1.11.1.18 | 7 | - |
assay at | Thermothelomyces thermophilus |
3.1.3.8 | 5 | - |
native and recombinant enzyme | Thermothelomyces heterothallicus |
EC Number | pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|---|
3.1.3.8 | 2 | 7.5 | activity range, profile overview | Thermothelomyces heterothallicus |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.11.1.18 | metavanadate | required for activity | Thermothelomyces thermophilus |
EC Number | kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
3.1.3.8 | 8843.5 | - |
myo-inositol hexakisphosphate | calcium phytate, pH 5.0, 60°C | Thermothelomyces heterothallicus |