EC Number   |
Protein Variants |
Reference |
|---|
   3.2.1.193 | more |
the hydrolytic pathways of enzyme mutants E83A, R131A, R199A, H238A, E332A, and L509A convert GypXVII to GypLXXV, showing the same regioselectivity as the wild-type enzyme. But mutant W512A converts GypXVII to GypLXXV and F2 (cf. EC 3.2.1.193), indicating that the variant simultaneously hydrolyzes the inner glucose linked to the C-3 position and the outer glucose linked to the C-20 position in GypXVII. Mutant W512F variant enzyme containing an aromatic side chain converts GypXVII as a substrate to GypLXXV, while mutant W512R containing a positively charged side chain converts GypXVII to F2 |
-, 752583 |
| 3.2.1.193 | W512A |
site-directed mutagenesis, mutation of a potential catalytic residue, the mutant shows slightly decreased activity with ginsenoside Rb1 and decreased activity with gypenoside XVII compared to the wild-type enzyme. Mutant W512A converts GypXVII to GypLXXV and F2 (cf.. EC 3.2.1.193) |
-, 752583 |
| 3.2.1.193 | W512K |
site-directed mutagenesis, mutation of a potential catalytic residue, the mutant shows strongly decreased activity with ginsenoside Rb1 and with gypenoside XVII compared to the wild-type enzyme |
-, 752583 |
| 3.2.1.193 | W512R |
site-directed mutagenesis, mutation of a potential catalytic residue, the mutant shows strongly decreased activity with ginsenoside Rb1 and with gypenoside XVII compared to the wild-type enzyme. mutant W512R containing a positively charged side chain converts GypXVII to F2, cf. EC 3.2.1.193 |
-, 752583 |
