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 |
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 |
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 | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.1.3.8 | Aspergillus niger | G8GYH6 | - |
- |
3.1.3.8 | Aspergillus niger NII 08121 | G8GYH6 | - |
- |
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 |
EC Number | Source Tissue | Comment | Organism | Textmining |
---|
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 | - |
? |
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 |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
3.1.3.8 | PhyA | - |
Aspergillus niger |
3.1.3.8 | phytase A | - |
Aspergillus niger |
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 |
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 |
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 |
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 |