EC Number   |
Protein Variants |
Reference |
|---|
    1.17.1.9 | A10C |
there are no significant changes in the optimum temperature and pH between variant and wild type enzyme but the mutant shows a significant increase in copper ion resistance and acid resistance, a 6.7fold increase in half-life at 60°C, and a 1.4fold increase in catalytic efficiency compared with the wild type |
739917 |
| 1.17.1.9 | A10C/I239C |
there are no significant changes in the optimum temperature and pH between variant and wild type enzyme |
739917 |
| 1.17.1.9 | A191G |
non-optimal residue located by Ramachandran-plot, mutation has no significant effect on enzyme stability. No significant change in enzyme kinetic properties |
672296 |
| 1.17.1.9 | A198G |
the mutant shows 1.8 fold increased activity compared to the wild type enzyme |
741547 |
| 1.17.1.9 | A198G |
the mutation reduces the KM value for NAD+ while the KM for CO2 remains practically unchanged, compared to the wild type enzyme |
741547 |
| 1.17.1.9 | A198G/D221Q |
the mutant has the highest catalytic efficiency (kcat/Km) with NADP+ |
-, 724079 |
| 1.17.1.9 | A198G/D221S |
the mutant has its coenzyme specificity changed from NAD+ to NADP+ compared to the wild type enzyme |
741547 |
| 1.17.1.9 | A267M |
the mutant shows increased catalytic efficiency compared to the wild type enzyme |
739827 |
| 1.17.1.9 | A267M/I272V |
the mutant shows reduced catalytic efficiency compared to the wild type enzyme |
739827 |
| 1.17.1.9 | A267M/I272V/F290D |
the mutant shows reduced catalytic efficiency compared to the wild type enzyme |
739827 |
