EC Number   |
Protein Variants |
Reference |
|---|
    2.4.1.25 | E123Q |
the specific activity of the mutant enzyme toward maltotriose is about 15000fold lower than the specific activity of the wild-type enzyme |
726933 |
| 2.4.1.25 | E129Q |
the specific activity of the mutant enzyme is almost the same as that of the wild-type enzyme |
726933 |
| 2.4.1.25 | E231Y |
site-directed mutagenesis, the E231Y mutant exhibits much higher kcat and Km values for starch transglycosylation, compared to that of the wild-type |
-, 777118 |
| 2.4.1.25 | E340A |
site-directed mutagenesis of the active site general acid/base catalyst, the mutant shows reduced activity with malto-oligomers compared to the wild-type enzyme |
-, 685153 |
| 2.4.1.25 | E340Q |
site-directed mutagenesis of the active site general acid/base catalyst, the mutant shows reduced activity with malto-oligomers compared to the wild-type enzyme |
-, 685153 |
| 2.4.1.25 | E758Q |
the mutant shows highly reduced activity compared to the wild-type enzyme |
687557 |
| 2.4.1.25 | F251G |
mutation results in significantly lower glucose production but increased maltose production from maltopentose substrates, showing an altered substrate-binding affinity |
721013 |
| 2.4.1.25 | F366L |
site-directed mutagenesis, the mutant shows reduced kcat compared and reduced activity with malto-oligomers compared to the wild-type enzyme |
685153 |
| 2.4.1.25 | G417F |
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 G417F mutation hinders the enzyme's cyclization activity |
777118 |
| 2.4.1.25 | H461A |
the mutation leads to a significant (8.6fold) decrease in transglucosylation activity compared to the wild type enzyme, while hydrolysis activity is barely affected. The mutant cannot produce large-ring cyclodextrins from maltotriose and prefers maltose over maltotriose as substrate |
-, 755897 |
