EC Number |
Protein Variants |
Reference |
---|
2.4.1.248 | A452N |
3fold increase in reaction velocity, 9fold increase in Km value. Activation by Ca2+ and inactivation by Cu2+ are reduced |
-, 698518 |
2.4.1.248 | D144A |
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme |
721736 |
2.4.1.248 | D144N |
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme |
721736 |
2.4.1.248 | D264A |
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme |
721736 |
2.4.1.248 | D269A |
site-directed mutagenesis, the mutant is inactive |
721736 |
2.4.1.248 | D269N |
site-directed mutagenesis, the mutant is almost inactive |
721736 |
2.4.1.248 | D662A |
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme |
721736 |
2.4.1.248 | E341A |
site-directed mutagenesis, the mutant is inactive |
721736 |
2.4.1.248 | E341Q |
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme |
721736 |
2.4.1.248 | F268V/D469Y/A513V/Y515S |
mutant produces three times as much megalo-cycloisomaltooligosaccharides (10-12 glucose units) and 1.5 times as much total cycloisomaltooligosaccharides (7-12 glucose units) as compared with the wild-type. The modified product size specificity is attributable to the construction of novel substrate-binding sites in the B-2 substrate-binding site and reactivity is improved by mutation on subsite -3 on the catalytic domain |
-, 735639 |