EC Number   |
Protein Variants |
Reference |
|---|
    3.2.1.23 | D332N |
mutation seriously reduces catalytic activity |
654479 |
| 3.2.1.23 | D429A |
the mutant has wild type activity |
702342 |
| 3.2.1.23 | D453A |
inactive |
702342 |
| 3.2.1.23 | E157G |
site-directed mutagenesis, altered kinetics compared to the wild-type enzyme |
678474 |
| 3.2.1.23 | E173N |
mutant enzyme shows no activity |
751822 |
| 3.2.1.23 | E184A |
site-directed mutagenesis, the mutant functions as an efficient thioglycoligase, which synthesises thiogalactosides with linkages to the 3 and 4 positions of glucosides and galactosides in high yields, the mutant shows reduced galactohydrolase activity compared to the wild-type enzyme |
679834 |
| 3.2.1.23 | E184Q |
site-directed mutagenesis, the mutant does not function as a thioglycoligase, the mutant shows reduced galactohydrolase activity compared to the wild-type enzyme |
679834 |
| 3.2.1.23 | E229D |
site-directed mutagenesis, enzyme BgaS7a, the mutant shows slightly increased activity compared to the wild-type enzyme |
-, 679711 |
| 3.2.1.23 | E229D/G803D |
site-directed mutagenesis, inactive mutant |
-, 679711 |
| 3.2.1.23 | E229D/V405A |
site-directed mutagenesis, enzyme BgaS7, the mutant shows similar thermal optima and thermostabilities as BgaS, but shows a 2.5fold increase in catalytic activity at 15°C and hydrolyzes 80% of lactose in skim milk in less than half the time of BgaS at 2.5°C |
679711 |
