EC Number   |
Protein Variants |
Reference |
|---|
    1.1.1.47 | A11L |
slight decrease in half-life at 25°C, decrease in specific activity |
686083 |
| 1.1.1.47 | A246V |
slight decrease in half-life at 25°C, decrease in specific activity |
686083 |
| 1.1.1.47 | A258F |
Km (D-glucose) increased at pH 6 compared to wild-type, decreased at pH 8 compared to wild-type. Mutant shows higher substrate specificity with D-xylose, D-mannose, D-galactose and D-glucosamine compared to wild-type. Mutant shows a markedly deteriorated thermostability |
724972 |
| 1.1.1.47 | DELTAG261 |
Km (D-glucose) highly increased at pH 6 and pH 8 compared to wild-type.Specific activity of mutant for D-glucose is severely decreased at both pH 6.0 and pH 8.0. Mutant shows a markedly deteriorated thermostability |
724972 |
| 1.1.1.47 | DS255 |
the mutant displays significantly enhanced thermal stability with considerable soluble expression and high specific activity. It is extremely stable at pH ranging from 4.5 to 10.5, as it retains nearly 100% activity after incubating at different buffers for 1 h. The mutant also exhibits high thermostability, having a half-life of 9900 min at 50°C, which is 1868fold as that of the wild type enzyme |
-, 740388 |
| 1.1.1.47 | E170K |
decrease in melting temperature by 7.1 degrees |
686083 |
| 1.1.1.47 | E170K |
increase in melting temperature by 18.5 degrees |
686083 |
| 1.1.1.47 | E170K |
increase in melting temperature by 25.9 degrees |
686083 |
| 1.1.1.47 | E170K |
mutant is unstable at an alkaline pH (26% residual activity at pH 10-10.5), dissociates into dimers at an alkaline pH |
-, 677657 |
| 1.1.1.47 | E170K/K252L |
increase in melting temperature by 5.6 degrees |
686083 |
