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Literature summary for 3.1.3.8 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)

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

Protein Variants

Protein Variants Comment Organism
D461N site-directed mutagenesis, the mutant exhibits a two-peak ppH profile with optima at pH 2.5 and pH 6.0 Aspergillus niger
G377T site-directed mutagenesis, the mutant exhibits a two-peak ppH profile with optima at pH 2.5 and pH 6.0 Aspergillus niger
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
additional information three-dimensional structure analysis of wild-type phytase and mutants P212H, T255E, S238D, G377T, and D461N Aspergillus niger
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
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
S238D site-directed mutagenesis, the mutant exhibits a two-peak ppH profile with optima at pH 2.5 and pH 6.0 Aspergillus niger
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)

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

Organism

Organism UniProt Comment Textmining
Aspergillus niger G8GYH6
-
-
Aspergillus niger NII 08121 G8GYH6
-
-

Purification (Commentary)

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

Source Tissue Comment Organism Textmining

Substrates and Products (Substrate)

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

Subunits

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

Synonyms

Synonyms Comment Organism
PhyA
-
Aspergillus niger
phytase A
-
Aspergillus niger

Temperature Optimum [°C]

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

pH Optimum

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

pH Range

pH Minimum pH Maximum Comment Organism
additional information
-
mutant enzymes pH profiles, overview Aspergillus niger
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
2.5
-
wild-type enzyme exhibits high activity at, bi-peak profile Aspergillus niger
5.5
-
wild-type enzyme exhibits high activity at, bi-peak profile Aspergillus niger

General Information

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