EC Number | Cloned (Comment) | Organism |
---|---|---|
3.1.3.8 | gene PPHY, DNA sequence, promoter and terminator region, and amino acid sequence determination and analysis | Wickerhamomyces anomalus |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
3.1.3.8 | 2,3-Butanedione | - |
Wickerhamomyces anomalus | |
3.1.3.8 | guanidine hydrochloride | - |
Wickerhamomyces anomalus | |
3.1.3.8 | additional information | no inhibition by sodium azide, DTT, 2-mercaptoethanol, EDTA, toluene, glycerol, and PMSF | Wickerhamomyces anomalus | |
3.1.3.8 | phosphate | - |
Wickerhamomyces anomalus | |
3.1.3.8 | Triton X-100 | - |
Wickerhamomyces anomalus | |
3.1.3.8 | Tween 20 | - |
Wickerhamomyces anomalus | |
3.1.3.8 | Tween 80 | - |
Wickerhamomyces anomalus | |
3.1.3.8 | Urea | - |
Wickerhamomyces anomalus |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
3.1.3.8 | 0.2 | - |
myo-inositol-1,2,3,4,5,6-hexakisphosphate | pH 4.0, 60°C | Wickerhamomyces anomalus |
EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|---|
3.1.3.8 | cell bound | - |
Wickerhamomyces anomalus | - |
- |
3.1.3.8 | cell wall | about 78% of the enzyme is cell wall bound | Wickerhamomyces anomalus | 5618 | - |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
3.1.3.8 | additional information | no requirement of metal ions for the activity | Wickerhamomyces anomalus |
EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|---|
3.1.3.8 | 64000 | - |
6 * 64000, SDS-PAGE | Wickerhamomyces anomalus |
3.1.3.8 | 384000 | - |
about, native PAGE | Wickerhamomyces anomalus |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.1.3.8 | additional information | Wickerhamomyces anomalus | the cell-bound phytase is able to effectively dephytinize wheat flour, wheat bran, rice flour, and soybean flour, or soymilk, to varied extents | ? | - |
? | |
3.1.3.8 | myo-inositol-1,2,3,4,5,6-hexakisphosphate + H2O | Wickerhamomyces anomalus | - |
? + phosphate | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.1.3.8 | Wickerhamomyces anomalus | D3HIF3 | single copy gene PPHY | - |
EC Number | Purification (Comment) | Organism |
---|---|---|
3.1.3.8 | the native enzyme is purified to near homogeneity by acetone precipitation and anion exchange chromatography | Wickerhamomyces anomalus |
EC Number | Source Tissue | Comment | Organism | Textmining |
---|---|---|---|---|
3.1.3.8 | additional information | optimization of fermentation for production of cell-bound phytase, overview | Wickerhamomyces anomalus | - |
EC Number | Storage Stability | Organism |
---|---|---|
3.1.3.8 | purified enzyme, shelf life is 6 months at 4°C, no loss in the activity on lyophilization | Wickerhamomyces anomalus |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.1.3.8 | additional information | the cell-bound phytase is able to effectively dephytinize wheat flour, wheat bran, rice flour, and soybean flour, or soymilk, to varied extents | Wickerhamomyces anomalus | ? | - |
? | |
3.1.3.8 | additional information | the phytase exhibits broad substrate specificity since it hydrolyses 4-nitrophenyl phosphate, ATP, ADP, and glucose-6-phosphate besides phytic acid. The enzyme hydrolyzes insoluble calcium and magnesium phytates efficiently, but not iron phytate | Wickerhamomyces anomalus | ? | - |
? | |
3.1.3.8 | myo-inositol-1,2,3,4,5,6-hexakisphosphate + H2O | - |
Wickerhamomyces anomalus | ? + phosphate | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
3.1.3.8 | homohexamer | 6 * 64000, SDS-PAGE | Wickerhamomyces anomalus |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
3.1.3.8 | cell-bound phytase | - |
Wickerhamomyces anomalus |
3.1.3.8 | histidine acid phosphatase | - |
Wickerhamomyces anomalus |
3.1.3.8 | More | PPHY is a phytase belonging to histidine acid phosphatases | Wickerhamomyces anomalus |
3.1.3.8 | PPHY | - |
Wickerhamomyces anomalus |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
3.1.3.8 | 60 | - |
purified phytase | Wickerhamomyces anomalus |
3.1.3.8 | 75 | - |
cell bound phytase | Wickerhamomyces anomalus |
EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|---|
3.1.3.8 | additional information | - |
the cell-bound phytase exhibits better thermostability than the pure enzyme | Wickerhamomyces anomalus |
3.1.3.8 | 60 | - |
purified enzyme, half-life is 7 days | Wickerhamomyces anomalus |
3.1.3.8 | 70 | - |
purified enzyme, half-life is 48 h | Wickerhamomyces anomalus |
3.1.3.8 | 80 | - |
purified enzyme, half-life is 5 min | Wickerhamomyces anomalus |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
3.1.3.8 | 4 | - |
- |
Wickerhamomyces anomalus |
EC Number | Organism | Comment | pI Value Maximum | pI Value |
---|---|---|---|---|
3.1.3.8 | Wickerhamomyces anomalus | isoelectric focusing | - |
4.5 |