EC Number   |
Protein Variants |
Reference |
|---|
    2.4.1.19 | A137V |
the mutation produces a perturbation in the catalytic site of the enzyme which correlates with a 10fold reduction in its catalytic efficiency. Moreover, this mutant shows increased production of maltooligosaccharides with a high degree of polymerization, mostly maltopentaose to maltoheptaose |
-, 758273 |
| 2.4.1.19 | A144V |
the mutant shows slightly reduced activity compared to the wild type enzyme |
-, 758273 |
| 2.4.1.19 | A156V |
the mutant shows increased sophoricoside glycosylation activity compared to the wild type enzyme |
755859 |
| 2.4.1.19 | A156V/A166Y |
the mutant shows increased sophoricoside glycosylation activity compared to the wild type enzyme |
755859 |
| 2.4.1.19 | A156V/L174P |
the mutant shows increased sophoricoside glycosylation activity compared to the wild type enzyme |
755859 |
| 2.4.1.19 | A156V/L174P/A166Y |
the mutant shows increased sophoricoside glycosylation activity compared to the wild type enzyme |
755859 |
| 2.4.1.19 | A166Y |
the mutant shows increased sophoricoside glycosylation activity compared to the wild type enzyme |
755859 |
| 2.4.1.19 | A166Y/L174P |
the mutant shows increased sophoricoside glycosylation activity compared to the wild type enzyme |
755859 |
| 2.4.1.19 | A223H |
mutant snzyme shows slight decreases in gamma-cyclodextrin-forming activity at pH 10.0, but shows 2fold increases at pH 7.5. pH activity profiles of the mutant shows higher activity at neutral pHs (pH 6-9) than that of the wild type CGTase |
-, 674367 |
| 2.4.1.19 | A223K |
mutant enzyme shows slight decreases in gamma-cyclodextrin-forming activity at pH 10.0, but shows 3fold increases at pH 7.5. pH activity profiles of the mutant show higher activity at neutral pHs (pH 6-9) than that of the wild type CGTase |
-, 674367 |
