Cloned (Comment) | Organism |
---|---|
gene agpP, DNA and amino acid sequence determination and analysis, recombinant expression of His-tagged enzyme lacking the signal peptide in Escherichia coli | Pantoea sp. 3.5.1 |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.24 | - |
alpha-D-glucose 1-phosphate | recombinant His-tagged enzyme, pH and temperature not specified in the publication | Pantoea sp. 3.5.1 |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
extracellular | - |
Pantoea sp. 3.5.1 | - |
- |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
alpha-D-glucose 1-phosphate + H2O | Pantoea sp. 3.5.1 | - |
D-glucose + phosphate | - |
? | |
additional information | Pantoea sp. 3.5.1 | the bifunctional enzyme also exhibits 3-phytase activity, cf. EC 3.1.3.8 | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Pantoea sp. 3.5.1 | A0A075FFV0 | - |
- |
Purification (Comment) | Organism |
---|---|
native enzyme by dialysis, anion exchange chromatography, and gel filtration, recombinant His-tagged enzyme lacking the signal peptide from Escherichia coli by nickel affinity chromatography | Pantoea sp. 3.5.1 |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
additional information | ability of the Pantoea sp. 3.5.1 isolate to grow with insoluble Ca-phytate as the sole source of phosphorus, not due to the secretion of an extracellular phytase | Pantoea sp. 3.5.1 | - |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
5.92 | - |
purified recombinant His-tagged enzyme, pH and temperature not specified in the publication, substrate alpha-D-glucose 1-phosphate | Pantoea sp. 3.5.1 |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
alpha-D-glucose 1-phosphate + H2O | - |
Pantoea sp. 3.5.1 | D-glucose + phosphate | - |
? | |
alpha-D-glucose 6-phosphate + H2O | - |
Pantoea sp. 3.5.1 | D-glucose + phosphate | - |
? | |
beta-glyceryl phosphate + H2O | - |
Pantoea sp. 3.5.1 | glycerol + phosphate | - |
? | |
additional information | the bifunctional enzyme also exhibits 3-phytase activity, cf. EC 3.1.3.8 | Pantoea sp. 3.5.1 | ? | - |
? | |
additional information | glucose-1-phosphatase enzymes and, specifically, Agp phytases are known to have a broad substrate specificity. The bifunctional enzyme from Pantoea sp. 3.5.1 also exhibits 3-phytase activity, cf. EC 3.1.3.8. Broad substrate specificity, substrates are phytate and many other phosphate-containing substrates, such as AMP, NADP, pNPP, 1-naphthyl phosphate, glucose phosphates, beta-glycerol phosphate, and diphosphate, overview | Pantoea sp. 3.5.1 | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
agpP | - |
Pantoea sp. 3.5.1 |
More | cf. EC 3.1.3.8 | Pantoea sp. 3.5.1 |
General Information | Comment | Organism |
---|---|---|
evolution | the enzyme AgpP from Pantoea sp. 3.5.1. belongs to the Agp subfamily of histidine acid phosphatases with 3-phytase specificity | Pantoea sp. 3.5.1 |