EC Number | Activating Compound | Comment | Organism | Structure |
---|---|---|---|---|
3.1.3.8 | EDTA | slight activation | Penicillium oxalicum | |
3.1.3.26 | EDTA | slight activation | Penicillium oxalicum |
EC Number | Cloned (Comment) | Organism |
---|---|---|
3.1.3.8 | gene phyA, DNA and amino acid sequence determination and analysis | Penicillium oxalicum |
3.1.3.26 | gene phyA, DNA and amino acid sequence determination and analysis | Penicillium oxalicum |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
3.1.3.8 | Ca2+ | strong inhibition at 5 mM | Penicillium oxalicum | |
3.1.3.8 | Cu2+ | strong inhibition at 5 mM | Penicillium oxalicum | |
3.1.3.8 | PMSF | strong inhibition at 5 mM | Penicillium oxalicum | |
3.1.3.8 | Zn2+ | strong inhibition at 5 mM | Penicillium oxalicum | |
3.1.3.26 | Ca2+ | strong inhibition at 5 mM | Penicillium oxalicum | |
3.1.3.26 | Cu2+ | strong inhibition at 5 mM | Penicillium oxalicum | |
3.1.3.26 | PMSF | strong inhibition at 5 mM | Penicillium oxalicum | |
3.1.3.26 | Zn2+ | strong inhibition at 5 mM | Penicillium oxalicum |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
3.1.3.8 | additional information | - |
additional information | Line-Weaver Burk plot | Penicillium oxalicum | |
3.1.3.8 | 0.545 | - |
myo-inositol hexakisphosphate | pH 4.5, 55°C | Penicillium oxalicum | |
3.1.3.26 | additional information | - |
additional information | Line-Weaver Burk plot | Penicillium oxalicum | |
3.1.3.26 | 0.545 | - |
myo-inositol hexakisphosphate | pH 4.5, 55°C | Penicillium oxalicum |
EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|---|
3.1.3.8 | extracellular | - |
Penicillium oxalicum | - |
- |
3.1.3.26 | extracellular | - |
Penicillium oxalicum | - |
- |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.1.3.8 | 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 | - |
? | |
3.1.3.8 | 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 | - |
? | |
3.1.3.26 | 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 | - |
? | |
3.1.3.26 | 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 | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.1.3.8 | Penicillium oxalicum | Q6YNE9 | - |
- |
3.1.3.8 | Penicillium oxalicum PJ3 | Q6YNE9 | - |
- |
3.1.3.26 | Penicillium oxalicum | Q6YNE9 | - |
- |
3.1.3.26 | Penicillium oxalicum PJ3 | Q6YNE9 | - |
- |
EC Number | Posttranslational Modification | Comment | Organism |
---|---|---|---|
3.1.3.8 | glycoprotein | glycosylation of six potential N-glycosylation sites | Penicillium oxalicum |
3.1.3.26 | glycoprotein | glycosylation of six potential N-glycosylation sites | Penicillium oxalicum |
EC Number | Purification (Comment) | Organism |
---|---|---|
3.1.3.8 | 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 |
3.1.3.26 | 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 |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.1.3.8 | additional information | among the many phosphate conjugate substrates PhyA shows fairly high specificity for phytate | Penicillium oxalicum | ? | - |
? | |
3.1.3.8 | additional information | among the many phosphate conjugate substrates PhyA shows fairly high specificity for phytate | Penicillium oxalicum PJ3 | ? | - |
? | |
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 | Penicillium oxalicum | 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, substrate is sodium phytate | Penicillium oxalicum | 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 | Penicillium oxalicum PJ3 | 1D-myo-inositol pentakisphosphate + phosphate | - |
? | |
3.1.3.26 | additional information | among the many phosphate conjugate substrates PhyA shows fairly high specificity for phytate | Penicillium oxalicum | ? | - |
? | |
3.1.3.26 | additional information | among the many phosphate conjugate substrates PhyA shows fairly high specificity for phytate | Penicillium oxalicum PJ3 | ? | - |
? | |
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 | Penicillium oxalicum | 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, substrate is sodium phytate | Penicillium oxalicum | 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 | Penicillium oxalicum PJ3 | 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, substrate is sodium phytate | Penicillium oxalicum PJ3 | 1D-myo-inositol pentakisphosphate + phosphate | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
3.1.3.8 | ? | x * 65000, SDS-PAGE, x * 50481, sequence calculation | Penicillium oxalicum |
3.1.3.26 | ? | x * 65000, SDS-PAGE, x * 50481, sequence calculation | Penicillium oxalicum |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
3.1.3.8 | More | cf. EC 3.1.3.26 | Penicillium oxalicum |
3.1.3.8 | myo-inositol-hexakisphosphate phosphohydrolase | - |
Penicillium oxalicum |
3.1.3.8 | PhyA | - |
Penicillium oxalicum |
3.1.3.8 | phytase | - |
Penicillium oxalicum |
3.1.3.8 | PJ3 phytase | - |
Penicillium oxalicum |
3.1.3.26 | More | cf. EC 3.1.3.8 | Penicillium oxalicum |
3.1.3.26 | myo-inositol-hexakisphosphate phosphohydrolase | - |
Penicillium oxalicum |
3.1.3.26 | PhyA | - |
Penicillium oxalicum |
3.1.3.26 | phytase | - |
Penicillium oxalicum |
3.1.3.26 | PJ3 phytase | - |
Penicillium oxalicum |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
3.1.3.8 | 55 | - |
- |
Penicillium oxalicum |
3.1.3.26 | 55 | - |
- |
Penicillium oxalicum |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
3.1.3.8 | 4.5 | - |
- |
Penicillium oxalicum |
3.1.3.26 | 4.5 | - |
- |
Penicillium oxalicum |
EC Number | pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|---|
3.1.3.8 | 3.2 | 5.4 | over 70% of the maximum activity within this pH range | Penicillium oxalicum |
3.1.3.26 | 3.2 | 5.4 | over 70% of the maximum activity within this pH range | Penicillium oxalicum |
EC Number | General Information | Comment | Organism |
---|---|---|---|
3.1.3.8 | evolution | the enzyme belongs to the histidine acid phosphatase family, it contains the active-site motif RHGXRXP | Penicillium oxalicum |
3.1.3.8 | 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 |
3.1.3.8 | 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 |
3.1.3.26 | evolution | the enzyme belongs to the histidine acid phosphatase family, it contains the active-site motif RHGXRXP | Penicillium oxalicum |
3.1.3.26 | 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 |
3.1.3.26 | 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 |