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Literature summary for 3.1.3.26 extracted from
- Engineering the residual side chains of HAP phytases to improve their pepsin resistance and catalytic efficiency (2017), Sci. Rep., 7, 42133 .
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene appA, recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3) | Yersinia rohdei |
| gene appA, recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3) | Yersinia kristensenii |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| E153R | site-directed mutagenesis, the mutant shows reduced catalytic activity but increased thermal stability compared to the wild-type enzyme | Yersinia kristensenii |
| E230A | site-directed mutagenesis, the mutant shows reduced catalytic activity but increased thermal stability compared to the wild-type enzyme | Yersinia kristensenii |
| E230D | site-directed mutagenesis, the mutant shows reduced catalytic activity but increased thermal stability compared to the wild-type enzyme | Yersinia kristensenii |
| E230G | site-directed mutagenesis, the mutant shows reduced catalytic activity but increased thermal stability compared to the wild-type enzyme | Yersinia kristensenii |
| E230K | site-directed mutagenesis, the mutant shows reduced catalytic activity and thermal stability compared to the wild-type enzyme | Yersinia kristensenii |
| E230P | site-directed mutagenesis, the mutant shows reduced catalytic activity but increased thermal stability compared to the wild-type enzyme | Yersinia kristensenii |
| E230S | site-directed mutagenesis, the mutant shows reduced catalytic activity but increased thermal stability compared to the wild-type enzyme | Yersinia kristensenii |
| E230T | site-directed mutagenesis, the mutant shows reduced catalytic activity but increased thermal stability compared to the wild-type enzyme | Yersinia kristensenii |
| L162A | site-directed mutagenesis, the mutant shows reduced catalytic activity but increased thermal stability compared to the wild-type enzyme | Yersinia kristensenii |
| L162G | site-directed mutagenesis, the mutant shows reduced catalytic activity but increased thermal stability compared to the wild-type enzyme | Yersinia kristensenii |
| L162V | site-directed mutagenesis, the mutant shows reduced catalytic activity but increased thermal stability compared to the wild-type enzyme | Yersinia kristensenii |
| L99A | site-directed mutagenesis, the mutant shows reduced catalytic activity but increased thermal stability compared to the wild-type enzyme | Yersinia kristensenii |
| L99A/L162G | site-directed mutagenesis, the mutant shows reduced catalytic activity but increased thermal stability compared to the wild-type enzyme | Yersinia kristensenii |
| L99A/L162G/L230G | site-directed mutagenesis, the mutant shows reduced catalytic activity but increased thermal stability compared to the wild-type enzyme | Yersinia kristensenii |
| additional information | engineering the residual side chains of HAP phytases to improve their pepsin resistance and catalytic efficiency. Proteolytic resistance of wild-type and mutant phytases, overview | Yersinia rohdei |
| additional information | engineering the residual side chains of HAP phytases to improve their pepsin resistance and catalytic efficiency. Proteolytic resistance of wild-type and mutant phytases, overview | Yersinia kristensenii |
| V162L | site-directed mutagenesis, the mutant shows increased sensitivity to pepsin in contrast to the less sensitive wild-type enzyme | Yersinia rohdei |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| additional information | when treated with trypsin in 0.25 M Tris-HCl (pH 7.0) for 2 h, the enzyme mutants E230K and E230R of YkAPPA retain less activity than the wild-type at ratios ranging from 1/1000 to 1/1 and 1/200 to 1/1, but the activity in the other mutants is similar to the wild-type at the various ratios. Residues at positions 99, 162, and 230 in Yersinia phytases play a major role in pepsin resistance, especially position 230 | Yersinia kristensenii | |
| additional information | the mutant V162L shows increased sensitivity to cleavage by pepsin (loss of 73% activity) compared to the wild-type (loss of 35% activity), while the sensitivity to trypsin is unaltered. Residues at positions 99, 162, and 230 in Yersinia phytases play a major role in pepsin resistance, especially position 230 | Yersinia rohdei |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| myo-inositol hexakisphosphate + H2O | Yersinia rohdei | - |
1D-myo-inositol 1,2,3,5,6-pentakisphosphate + phosphate | - |
? |  |
| myo-inositol hexakisphosphate + H2O | Yersinia kristensenii | phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26 | 1D-myo-inositol pentakisphosphate + phosphate | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Yersinia kristensenii | B6RGT1 | - |
- |
| Yersinia rohdei | B4X9S4 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity and anion exchange chromatography | Yersinia rohdei |
| recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity and anion exchange chromatography | Yersinia kristensenii |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | the ferrous sulfate-molybdenum blue method is used for enzyme activity detection | Yersinia rohdei | ? | - |
? | |
| additional information | the ferrous sulfate-molybdenum blue method is used for enzyme activity detection | Yersinia kristensenii | ? | - |
? | |
| myo-inositol hexakisphosphate + H2O | - |
Yersinia rohdei | 1D-myo-inositol 1,2,3,5,6-pentakisphosphate + phosphate | - |
? | |
| myo-inositol hexakisphosphate + H2O | phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26 | Yersinia kristensenii | 1D-myo-inositol pentakisphosphate + phosphate | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| AppA | - |
Yersinia rohdei |
| AppA | - |
Yersinia kristensenii |
| HAP phytase | - |
Yersinia rohdei |
| HAP phytase | - |
Yersinia kristensenii |
| More | cf. EC 3.1.3.8 | Yersinia kristensenii |
| YkAPPA | - |
Yersinia kristensenii |
| YrAPPA | - |
Yersinia rohdei |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 37 | - |
assay at | Yersinia rohdei |
| 37 | - |
assay at | Yersinia kristensenii |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 4.5 | - |
assay at | Yersinia rohdei |
| 4.5 | - |
assay at | Yersinia kristensenii |
General Information
| General Information | Comment | Organism |
|---|---|---|
| additional information | catalytic center structures of wild-type YkAPPA and its mutants E230G and L162G, catalytic sites are R44, R48, D115, R119, H333, and D334, overview | Yersinia kristensenii |
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