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Literature summary extracted from

  • Suleimanova, A.D.; Beinhauer, A.; Valeeva, L.R.; Chastukhina, I.B.; Balaban, N.P.; Shakirov, E.V.; Greiner, R.; Sharipova, M.R.
    Novel glucose-1-phosphatase with high phytase activity and unusual metal ion activation from soil bacterium Pantoea sp. strain 3.5.1 (2015), Appl. Environ. Microbiol., 81, 6790-6799 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.1.3.8 gene agpP, DNA and amino acid sequence determination and analysis, recombinant expression of His6-tagged enzyme lacking the signal peptide in Escherichia coli Pantoea sp. 3.5.1
3.1.3.10 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

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.1.3.8 Cu2+ 16% inhibition at 1 mM Pantoea sp. 3.5.1
3.1.3.8 Fe2+ 10% inhibition at 1 mM Pantoea sp. 3.5.1
3.1.3.8 additional information no effect by Co2+ at 1 mM Pantoea sp. 3.5.1
3.1.3.8 Zn2+ 42% inhibition at 1 mM Pantoea sp. 3.5.1

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.1.3.8 additional information
-
 additional information enzyme kinetics, also with other substrates, such as AMP, NADP, pNPP, 1-naphthyl phosphate, glucose phosphates, beta-glycerol phosphate, and diphosphate, overview Pantoea sp. 3.5.1
3.1.3.8 0.28
-
 myo-inositol hexakisphosphate recombinant His-tagged enzyme, pH and temperature not specified in the publication Pantoea sp. 3.5.1
3.1.3.10 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

EC Number Localization Comment Organism GeneOntology No. Textmining
3.1.3.8 extracellular
-
 Pantoea sp. 3.5.1
-
-
3.1.3.10 extracellular
-
 Pantoea sp. 3.5.1
-
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.1.3.8 Ca2+ 2fold activation at 1 mM Pantoea sp. 3.5.1
3.1.3.8 Mg2+ 2fold activation at 1 mM Pantoea sp. 3.5.1
3.1.3.8 Mn2+ 2fold activation at 1 mM Pantoea sp. 3.5.1
3.1.3.8 additional information no effect by Co2+ at 1 mM Pantoea sp. 3.5.1

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.1.3.8 55000 57000 native enzyme, gel filtration Pantoea sp. 3.5.1

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.1.3.8 additional information Pantoea sp. 3.5.1 the bifunctional enzyme also exhibits glucose-1-phosphatase, cf. EC 3.1.3.10 ?
-
 ?
3.1.3.8 myo-inositol hexakisphosphate + H2O Pantoea sp. 3.5.1
-
 1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
 ?
3.1.3.10 alpha-D-glucose 1-phosphate + H2O Pantoea sp. 3.5.1
-
 D-glucose + phosphate
-
 ?
3.1.3.10 additional information Pantoea sp. 3.5.1 the bifunctional enzyme also exhibits 3-phytase activity, cf. EC 3.1.3.8 ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.1.3.8 Pantoea sp. 3.5.1 A0A075FFV0 isolated from soil collected from four different ecological and geographical habitats of the Republic of Tatarstan, Russia, forest near the village Agerze, Aznakaevo District
-
3.1.3.10 Pantoea sp. 3.5.1 A0A075FFV0
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.1.3.8 native enzyme by dialysis, anion exchange chromatography, and gel filtration, recombinant His6-tagged enzyme lacking the signal peptide from Escherichia coli by nickel affinity chromatography. Native extracellular enzyme 528fold by dialysis, anion and cation exchange chromatography, and gel filtration Pantoea sp. 3.5.1
3.1.3.10 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

EC Number Source Tissue Comment Organism Textmining
3.1.3.8 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. Growth dynamics and extracellular and intracellular phytate-hydrolyzing activities of Pantoea sp. 3.5.1 culture, overview Pantoea sp. 3.5.1
-
3.1.3.10 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 [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.1.3.8 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
3.1.3.10 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 and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.3.8 additional information the bifunctional enzyme also exhibits glucose-1-phosphatase, cf. EC 3.1.3.10 Pantoea sp. 3.5.1 ?
-
 ?
3.1.3.8 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 exhibits 3-phytase activity, and also glucose-1-phosphatase, cf. EC 3.1.3.10. 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 ?
-
 ?
3.1.3.8 myo-inositol hexakisphosphate + H2O
-
 Pantoea sp. 3.5.1 1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
 ?
3.1.3.10 alpha-D-glucose 1-phosphate + H2O
-
 Pantoea sp. 3.5.1 D-glucose + phosphate
-
 ?
3.1.3.10 alpha-D-glucose 6-phosphate + H2O
-
 Pantoea sp. 3.5.1 D-glucose + phosphate
-
 ?
3.1.3.10 beta-glyceryl phosphate + H2O
-
 Pantoea sp. 3.5.1 glycerol + phosphate
-
 ?
3.1.3.10 additional information the bifunctional enzyme also exhibits 3-phytase activity, cf. EC 3.1.3.8 Pantoea sp. 3.5.1 ?
-
 ?
3.1.3.10 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 ?
-
 ?

Subunits

EC Number Subunits Comment Organism
3.1.3.8 monomer 1 * 48000, native enzyme, SDS-PAGE Pantoea sp. 3.5.1

Synonyms

EC Number Synonyms Comment Organism
3.1.3.8 agpP
-
 Pantoea sp. 3.5.1
3.1.3.8 AgpP phytase
-
 Pantoea sp. 3.5.1
3.1.3.8 More cf. EC 3.1.3.10 Pantoea sp. 3.5.1
3.1.3.10 agpP
-
 Pantoea sp. 3.5.1
3.1.3.10 More cf. EC 3.1.3.8 Pantoea sp. 3.5.1

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.1.3.8 37
-
-
 Pantoea sp. 3.5.1

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
3.1.3.8 10 65 activity range, profile overview Pantoea sp. 3.5.1

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.1.3.8 10 65 purified AgpP phytase remains stable for 1 h at a temperature interval of 10-45°C losing only up to 20% of activity at 45°C, only 40% and 12% of its maximum activity are retained at 55°C and 65°C, respectively Pantoea sp. 3.5.1
3.1.3.8 70
-
 purified enzyme, 1 h, inactivation Pantoea sp. 3.5.1

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.1.3.8 4.5
-
-
 Pantoea sp. 3.5.1

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.1.3.8 2.5 8 activity range, profile overview, narrow optimum, over 50% activity only at pH 4.0-5.0 Pantoea sp. 3.5.1

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
3.1.3.8 4 9 1 h, 4°C, the purified native phytase does not show any significant decline in activity at pH 4.0-5.5, almost 80% of the activity is lost at pH 9.0. At the optimum pH 4.5, the enzyme retains over 90% of its initial activity even after 10 days of incubation Pantoea sp. 3.5.1

General Information

EC Number General Information Comment Organism
3.1.3.8 evolution the enzyme AgpP from Pantoea sp. 3.5.1. belongs to the Agp subfamily of histidine acid phosphatases with 3-phytase specificity. The amino acid sequence of the Pantoea sp. 3.5.1 AgpP phytase harbors an N-terminal RHNLRAP motif (where the italicized residues are variable) and a C-terminal HD motif, which are the structural hallmarks of the highly conserved catalytic core of histidine acid phosphatases (HAPs) [consensus sequence RH(G/N)XRXP/HD, where the slash separates the N- and C-terminal sequences] Pantoea sp. 3.5.1
3.1.3.8 physiological function AgpP phytase and its unusual regulation by metal ions highlight the remarkable diversity of phosphorus metabolism regulation in soil bacteria Pantoea sp. 3.5.1
3.1.3.10 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