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Literature summary for 3.1.3.10 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)

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 [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

Localization Comment Organism GeneOntology No. Textmining
extracellular
-
Pantoea sp. 3.5.1
-
-

Natural Substrates/ Products (Substrates)

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

Organism UniProt Comment Textmining
Pantoea sp. 3.5.1 A0A075FFV0
-
-

Purification (Commentary)

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

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 [micromol/min/mg]

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 and Products (Substrate)

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

Synonyms Comment Organism
agpP
-
Pantoea sp. 3.5.1
More cf. EC 3.1.3.8 Pantoea sp. 3.5.1

General Information

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