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Literature summary extracted from

  • Martin, J.A.; Murphy, R.A.; Power, R.F.
    Purification and physico-chemical characterisation of genetically modified phytases expressed in Aspergillus awamori (2006), Biores. Technol., 97, 1703-1708.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.1.3.8 expressed in Aspergillus awamori strains pGP209 and pGF11 Aspergillus awamori

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.1.3.8 66000
-
 SDS-PAGE Aspergillus niger
3.1.3.8 70000
-
 SDS-PAGE, wild type enzyme PyhA Aspergillus awamori
3.1.3.8 84000
-
 SDS-PAGE Aspergillus sp.
3.1.3.8 84000
-
 SDS-PAGE, recombinant enzyme pGP209 Aspergillus awamori

Organism

EC Number Organism UniProt Comment Textmining
3.1.3.8 Aspergillus awamori
-
-
-
3.1.3.8 Aspergillus niger
-
 variant ficuum
-
3.1.3.8 Aspergillus sp.
-
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
3.1.3.8 glycoprotein
-
 Aspergillus niger
3.1.3.8 glycoprotein
-
 Aspergillus sp.
3.1.3.8 glycoprotein
-
 Aspergillus awamori

Purification (Commentary)

EC Number Purification (Comment) Organism
3.1.3.8 Sephadex G-100 gel filtration and DEAE-Sepharose CL-6B anion exchange column chromatography Aspergillus awamori

Renatured (Commentary)

EC Number Renatured (Comment) Organism
3.1.3.8 the enzyme denatures at temperatures of 50°C or above, when the temperature is reduced again the protein refolds almost entirely into a fully active, native conformation Aspergillus niger
3.1.3.8 the enzyme denatures at temperatures of 50°C or above, when the temperature is reduced again the protein refolds almost entirely into a fully active, native conformation Aspergillus sp.
3.1.3.8 the enzyme denatures at temperatures of 50°C or above, when the temperature is reduced again the protein refolds almost entirely into a fully active, native conformation Aspergillus awamori

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.3.8 myo-inositol hexakisphosphate + H2O
-
 Aspergillus niger 1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
 ?
3.1.3.8 myo-inositol hexakisphosphate + H2O
-
 Aspergillus sp. 1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
 ?
3.1.3.8 myo-inositol hexakisphosphate + H2O
-
 Aspergillus awamori 1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.1.3.8 Allzyme commercial preparation Aspergillus sp.
3.1.3.8 Natuphos commercial preparation Aspergillus niger
3.1.3.8 pGF11 phytase recombinant enzyme Aspergillus awamori
3.1.3.8 pGP209 phytase recombinant enzyme Aspergillus awamori
3.1.3.8 PhyA
-
 Aspergillus awamori

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.1.3.8 50
-
-
 Aspergillus sp.
3.1.3.8 55
-
-
 Aspergillus niger
3.1.3.8 55
-
 recombinant enzyme pGP209 Aspergillus awamori
3.1.3.8 60
-
 wild type PhyA Aspergillus awamori

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.1.3.8 50 70 the enzyme denatures at temperatures of 50°C or above, when the temperature is reduced again the protein refolds almost entirely into a fully active, native conformation, the activity is negligible at 70°C Aspergillus niger
3.1.3.8 50 70 the enzyme denatures at temperatures of 50°C or above, when the temperature is reduced again the protein refolds almost entirely into a fully active, native conformation, the activity is negligible at 70°C Aspergillus sp.
3.1.3.8 50 70 the enzyme denatures at temperatures of 50°C or above, when the temperature is reduced again the protein refolds almost entirely into a fully active, native conformation, the activity is negligible at 70°C Aspergillus awamori