EC Number   |
Protein Variants |
Reference |
|---|
    2.4.1.25 | A406L |
the mutant shows higher thermostability at 35-40°C, higher intermolecular transglucosylation activity with an upward shift in the optimum temperature and a slight increase in the optimum pH for disproportionation and cyclization reactions compared to the wild type enzyme. The mutant shows higher specific activities for starch transglucosylation (2.1fold) and disproportionation (1.4fold) than those of the wild type |
-, 736255 |
| 2.4.1.25 | A406V |
site-directed mutagenesis, the mutant shows higher thermostability and gives higher amount of LR-CD products, in comparison to the wild-type enzyme |
777118 |
| 2.4.1.25 | A406V |
the mutant shows higher thermostability at 50°C, higher intermolecular transglucosylation activity with an upward shift in the optimum temperature and a slight increase in the optimum pH for disproportionation and cyclization reactions compared to the wild type enzyme. The mutant shows higher specific activities for starch transglucosylation (2.8fold) and disproportionation (2.1fold) than those of the wild type |
-, 736255 |
| 2.4.1.25 | A413F |
site-directed mutagenesis, the mutant produces larger LR-CDs from CD36-CD40 as compared to CD29 by the wild-type, but with low yield. The A413F mutation affects the enzyme activities: starch tranglycosylation, disproportionation and cyclization |
-, 777118 |
| 2.4.1.25 | D214N |
the specific activity of the D214N mutant is decreased about 10000fold as compared with that of the wild-type enzyme |
-, 489022 |
| 2.4.1.25 | D293A |
site-directed mutagenesis of the active site nucleophile, the mutant shows reduced activity with malto-oligomers compared to the wild-type enzyme |
-, 685153 |
| 2.4.1.25 | D293N |
site-directed mutagenesis of the active site nucleophile, the D293N mutation reduces the pH stability of the enzyme, the mutant shows reduced activity with malto-oligomers compared to the wild-type enzyme |
-, 685153 |
| 2.4.1.25 | D294S |
site-directed mutagenesis, the mutant shows highly reduced kcat and reduced activity with malto-oligomers compared to the wild-type enzyme |
685153 |
| 2.4.1.25 | D395A |
site-directed mutagenesis of the active site transition stabilizer, the mutant shows reduced activity with malto-oligomers compared to the wild-type enzyme |
685153 |
| 2.4.1.25 | D395N |
site-directed mutagenesis of the active site transition stabilizer, the mutant shows reduced activity with malto-oligomers compared to the wild-type enzyme |
-, 685153 |
