EC Number   |
Protein Variants |
Reference |
|---|
    3.2.1.20 | A200V |
site-directed mutagenesis, the mutant is almost inactive |
-, 680563 |
| 3.2.1.20 | A200V/S202N/H203M |
site-directed mutagenesis, the mutant shows altered substrate specificity and highly reduced activity compared to the wild-type enzyme |
-, 680563 |
| 3.2.1.20 | A445P |
increased activity, enzyme mutants responsive to 1-deoxynojirimycin |
708660 |
| 3.2.1.20 | A610V |
increased activity, enzyme mutants responsive to 1-deoxynojirimycin |
708660 |
| 3.2.1.20 | D408G |
transglycosylation efficiency is improved. The mutant enzyme catalyzes the formation of a specific product from 4-nitrophenyl-alpha-D-glucopyranoside with a yield of 42.5% without further hydrolysis, while the wild-type enzyme produces two 4-nitrophenyl-alpha-D-glucopyranoside products at low yields |
748515 |
| 3.2.1.20 | E173S |
mutation with loss of al alpha-glucosidase activity, but the mutant protein exhibits no alpha-galactosidase activtiy |
705622 |
| 3.2.1.20 | E173S |
site-directed mutagenesis |
-, 705622 |
| 3.2.1.20 | E173S/I174V |
mutation with loss of al alpha-glucosidase activity, but the mutant protein exhibits no alpha-galactosidase activtiy |
705622 |
| 3.2.1.20 | E173S/I174V |
site-directed mutagenesis |
705622 |
| 3.2.1.20 | E257A |
site-directed mutagenesis, mutation of a catalytic residue, inactive mutant |
-, 750760 |
