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Literature summary for 3.1.3.8 extracted from

  • Nassiri, M.; Ariannejad, H.
    Comparative analysis of peripheral alkaline phytase protein structures expressed in E. coli (2015), Rep. Biochem. Mol. Biol., 4, 10-18 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.1.3.8

Cloned(Commentary)

Cloned (Comment) Organism
gene phyC, DNA and amino acid determination and analysis, functional recombinant expression of thioredoxin-His-tagged enzyme from vector pET32a-PhyC and His-tagged enzyme from vector pET21a-PhyC in Escherichia coli cytoplasm. The concentration of the alkaline phytase expressed by pET32a is approximately 59% greater than that expressed by pET21, but its phytase activity is approximately 77% lower Bacillus subtilis

Localization

Localization Comment Organism GeneOntology No. Textmining
additional information the enzyme contains a signal peptide Bacillus subtilis
-
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
myo-inositol hexakisphosphate + H2O Bacillus subtilis
-
 1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
 ?
myo-inositol hexakisphosphate + H2O Bacillus subtilis DR8886
-
 1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
 ?

Organism

Organism UniProt Comment Textmining
Bacillus subtilis O31097 isolated from Dig Rostam hot mineral spring in Iran
-
Bacillus subtilis DR8886 O31097 isolated from Dig Rostam hot mineral spring in Iran
-

Posttranslational Modification

Posttranslational Modification Comment Organism
proteolytic modification the mature peptide sequence lacked RHGXRXP, a conserved motif at the catalytic site of acidic phytases. The enzyme contains a signal peptide Bacillus subtilis

Purification (Commentary)

Purification (Comment) Organism
recombinant thioredoxin-His-tagged enzyme and His-tagged enzyme from Escherichia coli by nickel affinity chromatography Bacillus subtilis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information enzyme activity assay using color reagent containing 1.5% w/v ammonium molybdate, 5.5% v/v sulfuric acid solution, and 2.7% w/v ferrous sulfate Bacillus subtilis ?
-
 ?
additional information enzyme activity assay using color reagent containing 1.5% w/v ammonium molybdate, 5.5% v/v sulfuric acid solution, and 2.7% w/v ferrous sulfate Bacillus subtilis DR8886 ?
-
 ?
myo-inositol hexakisphosphate + H2O
-
 Bacillus subtilis 1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
 ?
myo-inositol hexakisphosphate + H2O phytate Bacillus subtilis 1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
 ?
myo-inositol hexakisphosphate + H2O
-
 Bacillus subtilis DR8886 1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
 ?
myo-inositol hexakisphosphate + H2O phytate Bacillus subtilis DR8886 1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
 ?

Subunits

Subunits Comment Organism
? x * 60000, recombinant thioredoxin-tagged enzyme, SDS-PAGE, x * 42000, recombinant nontagged enzyme, SDS-PAGE Bacillus subtilis

Synonyms

Synonyms Comment Organism
PhyC
-
 Bacillus subtilis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
39
-
 assay at Bacillus subtilis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5
-
 assay at Bacillus subtilis

General Information

General Information Comment Organism
additional information the deduced amino acid sequence of phyC harbors a putative -35 and -10 sequences, a ribosomal binding site, and a transcription terminator Bacillus subtilis