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Literature summary for 3.1.3.8 extracted from
- Cumulative improvements of thermostability and pH-activity profile of Aspergillus niger PhyA phytase by site-directed mutagenesis (2008), Appl. Microbiol. Biotechnol., 77, 1033-1040.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expressed in Pichia pastoris strain X33 | Aspergillus niger |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| A58E/P65S/Q191R/T271R | retains 20% greater activity after being heated at 80°C for 10 min and has 7°C higher melting temperature than that of the wild type enzyme | Aspergillus niger |
| A58E/P65S/Q191R/T271R/E228K | pH-activity profile-improved mutant, optimum shift to pH 4.0, 64% increased specific activity at pH 3.5 | Aspergillus niger |
| A58E/P65S/Q191R/T271R/E228K/K300E | pH-activity profile-improved mutant, eliminates the activity dip at pH 3.5 shown in the wild type | Aspergillus niger |
| A58E/P65S/Q191R/T271R/E228K/S149P | improved thermostability | Aspergillus niger |
| A58E/P65S/Q191R/T271R/E228K/S149P/F131L | improved thermostability | Aspergillus niger |
| A58E/P65S/Q191R/T271R/E228K/S149P/F131L/K112R | Although the substitution of K112R is supposed to create a new hydrogen bond with Y113 at a distance of 2.56 A, it does not offer extra benefit to thermostability | Aspergillus niger |
| A58E/P65S/Q191R/T271R/E228K/S149P/F131L/K112R/K195R | 27% increased specific activity at pH 5.5, 100% increased specific activity at pH 3.5 | Aspergillus niger |
| A58E/P65S/Q191R/T271R/E228K/S149P/F131L/K112R/K195R/K300E | 33% decreased activity at pH 5.5, wild type specific activity at pH 3.5 | Aspergillus niger |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.0827 | - |
myo-inositol hexakisphosphate | mutant enzyme A58E/P65S/Q191R/T271R/E228K, at pH 4.0 | Aspergillus niger |  |
| 0.0864 | - |
myo-inositol hexakisphosphate | mutant enzyme A58E/P65S/Q191R/T271R/E228K/S149P, at pH 4.0 | Aspergillus niger | |
| 0.0934 | - |
myo-inositol hexakisphosphate | mutant enzyme A58E/P65S/Q191R/T271R/E228K/S149P/F131L/K112R/K195R, at pH 4.0 | Aspergillus niger | |
| 0.1076 | - |
myo-inositol hexakisphosphate | mutant enzyme A58E/P65S/Q191R/T271R/E228K/S149P, at pH 5.5 | Aspergillus niger | |
| 0.1083 | - |
myo-inositol hexakisphosphate | mutant enzyme A58E/P65S/Q191R/T271R/E228K, at pH 5.5 | Aspergillus niger | |
| 0.1224 | - |
myo-inositol hexakisphosphate | wild type enzyme, at pH 4.0 | Aspergillus niger | |
| 0.1719 | - |
myo-inositol hexakisphosphate | wild type enzyme, at pH 5.5 | Aspergillus niger | |
| 0.3847 | - |
myo-inositol hexakisphosphate | mutant enzyme A58E/P65S/Q191R/T271R/E228K/S149P/F131L/K112R/K195R, at pH 5.5 | Aspergillus niger | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Aspergillus niger | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| DEAE cation exchange chromatography and Sephadex100 gel filtration | Aspergillus niger |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| myo-inositol hexakisphosphate + H2O | - |
Aspergillus niger | 1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| PhyA | - |
Aspergillus niger |
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