EC Number |
Protein Variants |
Reference |
---|
1.1.1.363 | D177N |
absence of a negatively charged aspartate at 177 accounts for the decrease in catalytic activity at pH 7.8 |
721583 |
1.1.1.363 | D177N |
kcat/KM for D-glucose 6-phosphate (with cosubstrate NADP+) is fold lower than the value for the wild-type enzyme, kcat/KM for NADP+ is fold lower than the value for the wild-type enzyme, kcat/KM for D-glucose 6-phosphate (with cosubstrate NAD) is fold lower than the value for the wild-type enzyme, kcat/KM for D-glucose 6-phosphate (with cosubstrate NAD+) is fold lower than the value for the wild-type enzyme |
721580 |
1.1.1.363 | D205C |
enzyme variant with cysteine close to the dimer interface, about 30% loss of specific activity compared to wild-type enzyme shows changes in activity and the efficacy of immobilization. |
722852 |
1.1.1.363 | D374Q |
kcat/Km for D-glucose 6-phosphate is 7.7fold lower compared to kcat/KM of wild-type enzyme, kcat/Km for NADP+ is 7.3fold lower compared to kcat/KM of wild-type enzyme, kcat/Km for NAD+ is 12.2fold lower compared to kcat/KM of wild-type enzyme |
721584 |
1.1.1.363 | D453C |
enzyme variant with cysteine far from the active center, no significant loss in specific activity compared to wild-type enzyme, in contrast to wild-type enzyme, the mutant enzyme is readily immobilited |
722852 |
1.1.1.363 | H178N |
kcat/KM for D-glucose 6-phosphate (with cosubstrate NADP+) is fold lower than the value for the wild-type enzyme, kcat/KM for NADP+ is fold lower than the value for the wild-type enzyme, kcat/KM for D-glucose 6-phosphate (with cosubstrate NAD) is fold lower than the value for the wild-type enzyme, kcat/KM for D-glucose 6-phosphate (with cosubstrate NAD+) is fold lower than the value for the wild-type enzyme |
721580 |
1.1.1.363 | H250N |
kcat/KM for D-glucose 6-phosphate (with cosubstrate NADP+) is fold lower than the value for the wild-type enzyme, kcat/KM for NADP+ is fold lower than the value for the wild-type enzyme, kcat/KM for D-glucose 6-phosphate (with cosubstrate NAD) is fold lower than the value for the wild-type enzyme, kcat/KM for D-glucose 6-phosphate (with cosubstrate NAD+) is fold lower than the value for the wild-type enzyme |
721580 |
1.1.1.363 | K182Q |
kcat/Km for D-glucose 6-phosphate is 127fold lower compared to kcat/KM of wild-type enzyme, kcat/Km for NADP+ is 1.1fold higher compared to kcat/KM of wild-type enzyme, kcat/Km for NAD+ is 1.4fold lower compared to kcat/KM of wild-type enzyme |
721584 |
1.1.1.363 | K182R |
kcat/Km for D-glucose 6-phosphate is 81fold lower compared to kcat/KM of wild-type enzyme, kcat/Km for NADP+ is 1.1fold lower compared to kcat/KM of wild-type enzyme, kcat/Km for NAD+ is 1.6fold lower compared to kcat/KM of wild-type enzyme |
721584 |
1.1.1.363 | K21Q |
kcat/Km for D-glucose 6-phosphate in the NADP+-dependent reaction is 76.2fold lower compared to wild-type value, kcat/Km for D-glucose 6-phosphate in the NAD+-dependent reaction is 28.5fold lower compared to wild-type value |
723718 |