Activating Compound | Comment | Organism | Structure |
---|---|---|---|
EDTA | slight activation | Penicillium oxalicum |
Cloned (Comment) | Organism |
---|---|
gene phyA, DNA and amino acid sequence determination and analysis | Penicillium oxalicum |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
Ca2+ | strong inhibition at 5 mM | Penicillium oxalicum | |
Cu2+ | strong inhibition at 5 mM | Penicillium oxalicum | |
PMSF | strong inhibition at 5 mM | Penicillium oxalicum | |
Zn2+ | strong inhibition at 5 mM | Penicillium oxalicum |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | Line-Weaver Burk plot | Penicillium oxalicum | |
0.545 | - |
myo-inositol hexakisphosphate | pH 4.5, 55°C | Penicillium oxalicum |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
extracellular | - |
Penicillium oxalicum | - |
- |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
myo-inositol hexakisphosphate + H2O | Penicillium oxalicum | 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 | Penicillium oxalicum PJ3 | phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26 | 1D-myo-inositol pentakisphosphate + phosphate | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Penicillium oxalicum | Q6YNE9 | - |
- |
Penicillium oxalicum PJ3 | Q6YNE9 | - |
- |
Posttranslational Modification | Comment | Organism |
---|---|---|
glycoprotein | glycosylation of six potential N-glycosylation sites | Penicillium oxalicum |
Purification (Comment) | Organism |
---|---|
native enzyme PhyA 427fold from strain PJ3 by ammonium sulfate fractionation, dialysis, gel filtration, and cation exchange chromatography, and again dialysis, to homogeneity | Penicillium oxalicum |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | among the many phosphate conjugate substrates PhyA shows fairly high specificity for phytate | Penicillium oxalicum | ? | - |
? | |
additional information | among the many phosphate conjugate substrates PhyA shows fairly high specificity for phytate | Penicillium oxalicum PJ3 | ? | - |
? | |
myo-inositol hexakisphosphate + H2O | phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26 | Penicillium oxalicum | 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, substrate is sodium phytate | Penicillium oxalicum | 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 | Penicillium oxalicum PJ3 | 1D-myo-inositol pentakisphosphate + phosphate | - |
? |
Subunits | Comment | Organism |
---|---|---|
? | x * 65000, SDS-PAGE, x * 50481, sequence calculation | Penicillium oxalicum |
Synonyms | Comment | Organism |
---|---|---|
More | cf. EC 3.1.3.26 | Penicillium oxalicum |
myo-inositol-hexakisphosphate phosphohydrolase | - |
Penicillium oxalicum |
PhyA | - |
Penicillium oxalicum |
phytase | - |
Penicillium oxalicum |
PJ3 phytase | - |
Penicillium oxalicum |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
55 | - |
- |
Penicillium oxalicum |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
4.5 | - |
- |
Penicillium oxalicum |
pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|
3.2 | 5.4 | over 70% of the maximum activity within this pH range | Penicillium oxalicum |
General Information | Comment | Organism |
---|---|---|
evolution | the enzyme belongs to the histidine acid phosphatase family, it contains the active-site motif RHGXRXP | Penicillium oxalicum |
additional information | the enzyme has an active-site motif RHGXRXP and a remote C-teminal His-Asp (HD motif) which takes part in the catalysis | Penicillium oxalicum |
physiological function | phytase hydrolyzes phytic acid (myo-inositol-hexakisphosphate), which is the major storage form of phosphorus in cereals, legumes, and oilseed crops | Penicillium oxalicum |