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Literature summary extracted from

  • Ushasree, M.V.; Vidya, J.; Pandey, A.
    Replacement P212H altered the pH-temperature profile of phytase from Aspergillus niger NII 08121 (2015), Appl. Biochem. Biotechnol., 175, 3084-3092 .
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.1.3.8 gene phyA, the mutants are constructed and expressed in Kluyveromyces lactis strain GG799, the enzymes are secreted Aspergillus niger
3.1.3.8 recombinant expression of wild-type and mutant enzymes in Kluyveromyces lactis strain GG799, the enzymes are secreted Aspergillus niger

Protein Variants

EC Number Protein Variants Comment Organism
3.1.3.8 D461N site-directed mutagenesis, the mutant exhibits a two-peak ppH profile with optima at pH 2.5 and pH 6.0 Aspergillus niger
3.1.3.8 G377T site-directed mutagenesis, the mutant exhibits a two-peak ppH profile with optima at pH 2.5 and pH 6.0 Aspergillus niger
3.1.3.8 additional information protein engineering is carried out to shift the pH optimum of a thermostable Aspergillus fumigatus phytase to acidic range. The wild enzyme exhibits enhanced activities at pH 2.5 and pH 5.5. Mutants D461N, G377T, T255E, and S238D retain bi-peak pH profiles, but there is an observed enhancement in activity at pH 6.0 compared to pH 5.5. Mutant P212H exhibits enhancement in activity at pH 3.0-3.5 compared to the wild-type enzyme Aspergillus niger
3.1.3.8 additional information three-dimensional structure analysis of wild-type phytase and mutants P212H, T255E, S238D, G377T, and D461N Aspergillus niger
3.1.3.8 P212H site-directed mutagenesis, the mutant exhibits a two-peak ppH profile with optima at pH 3.2 and pH 5.5. The substitution of histidine at position 212 has remarkable effect on pH and temperature properties of the enzyme Aspergillus niger
3.1.3.8 P212H site-directed mutagenesis, the mutant shows altered the pH optimum shifted from pH 2.5 to pH 3.2 and a decrease in thermostability compared to wild-type enzyme, the mutant exhibits a two-peak pH profile with optima at pH 3.2 and pH 5.5 Aspergillus niger
3.1.3.8 S238D site-directed mutagenesis, the mutant exhibits a two-peak ppH profile with optima at pH 2.5 and pH 6.0 Aspergillus niger
3.1.3.8 T255E site-directed mutagenesis, the mutant exhibits a two-peak ppH profile with optima at pH 2.0 and pH 6.0 Aspergillus niger

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.1.3.8 myo-inositol hexakisphosphate + H2O Aspergillus niger
-
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
?
3.1.3.8 myo-inositol hexakisphosphate + H2O Aspergillus niger NII 08121
-
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
?

Organism

EC Number Organism UniProt Comment Textmining
3.1.3.8 Aspergillus niger G8GYH6
-
-
3.1.3.8 Aspergillus niger NII 08121 G8GYH6
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.1.3.8 recombinant mutant enzymes from Kluyveromyces lactis strain GG799 culture supernatant by lyophilization, anion exchange chromatography, and hydrophobic interaction chromatography Aspergillus niger
3.1.3.8 recombinant wild-type and mutant enzymes from Kluyveromyces lactis strain GG799 culture supernatant by lyophilization, anion exchange chromatography, and hydrophobic interaction chromatography Aspergillus niger

Source Tissue

EC Number Source Tissue Comment Organism Textmining

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 1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
?
3.1.3.8 myo-inositol hexakisphosphate + H2O
-
Aspergillus niger NII 08121 1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
?

Subunits

EC Number Subunits Comment Organism
3.1.3.8 More three-dimensional structure analysis of wild-type phytase and mutants P212H, T255E, S238D, G377T, and D461N Aspergillus niger

Synonyms

EC Number Synonyms Comment Organism
3.1.3.8 PhyA
-
Aspergillus niger
3.1.3.8 phytase A
-
Aspergillus niger

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.1.3.8 55
-
recombinant wild-type and mutant enzymes Aspergillus niger
3.1.3.8 55
-
wild-type enzyme and mutant P212H Aspergillus niger

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.1.3.8 2.5
-
optimum 1, wild-type enzyme Aspergillus niger
3.1.3.8 5.5
-
optimum 2, wild-type enzyme Aspergillus niger

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.1.3.8 additional information
-
mutant enzymes pH profiles, overview Aspergillus niger
3.1.3.8 additional information
-
mutants D461N, G377T, T255E and S238D retain bi-peak pH profiles, but there is an observed enhancement in activity at pH 6.0 compared to pH 5.5. Mutant P212H exhibits enhancement in activity at pH 3.0-3.5 compared to the wild-type enzyme Aspergillus niger
3.1.3.8 2.5
-
wild-type enzyme exhibits high activity at, bi-peak profile Aspergillus niger
3.1.3.8 5.5
-
wild-type enzyme exhibits high activity at, bi-peak profile Aspergillus niger

General Information

EC Number General Information Comment Organism
3.1.3.8 additional information three-dimensional structure analysis of wild-type phytase and mutants P212H, T255E, S238D, G377T, and D461N Aspergillus niger