Cloned (Comment) | Organism |
---|---|
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 |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
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 |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
extracellular | the enzyme is secreted | Thermothelomyces thermophilus | - |
- |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Thermothelomyces thermophilus | V5M269 | - |
- |
Posttranslational Modification | Comment | Organism |
---|---|---|
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 |
Purification (Comment) | Organism |
---|---|
recombinant enzyme from Pichia pastoris strain X-33 by ultrafiltration, anion exchange chromatography, dialysis, and gel filtration | Thermothelomyces thermophilus |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
additional information | the thermophilic mold Sporotrichum thermophile produces very low titers of phytase extracellularly in both solid state and submerged fermentations | Thermothelomyces thermophilus | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
KBr + 2 H2O | - |
Thermothelomyces thermophilus | KH + HBr + H2O2 | - |
? | |
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 | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
? | x * 70000, recombinant enzyme, SDS-PAGE, x * 90000, native enzyme, SDS-PAGE | Thermothelomyces thermophilus |
Synonyms | Comment | Organism |
---|---|---|
HAP phytase | - |
Thermothelomyces thermophilus |
More | cf. EC 3.1.3.8 | Thermothelomyces thermophilus |
St-Phy | - |
Thermothelomyces thermophilus |
vanadate haloperoxidase | - |
Thermothelomyces thermophilus |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assay at | Thermothelomyces thermophilus |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7 | - |
assay at | Thermothelomyces thermophilus |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
metavanadate | required for activity | Thermothelomyces thermophilus |