EC Number   |
Protein Variants |
Reference |
|---|
    1.4.1.2 | A242G |
site-directed mutagenesis, the mutant shows A242G showed a decreased overall catalytic efficiency for NADH at all pH values of pH 6.0-8.0 after Ala replacement with Gly compared to the wild-type enzyme, the mutation had a severe effect on the overall catalytic efficiency with NADPH as coenzyme |
724888 |
| 1.4.1.2 | C1141T |
no large changes in catalytic activity |
742113 |
| 1.4.1.2 | C1141T |
residue C1141 is responsible for the inhibition of enzyme activity by HgCl2, and HgCl2 functions as an activating compound for mutant C1141T |
742113 |
| 1.4.1.2 | C825G |
no large changes in catalytic activity |
742113 |
| 1.4.1.2 | C872R |
no large changes in catalytic activity |
742113 |
| 1.4.1.2 | D165H |
site-directed mutagenesis, catalytically inactive mutant |
724249 |
| 1.4.1.2 | D165N |
residual 2% of wild-type activity when purified after expression in Escherichia coli at 37°C, cells induced at 8°C are 1000fold less active than that produced at 37°C, spontaneous deamidation, which depends on the residual catalytic machinery of the mutated GDH active site |
672020 |
| 1.4.1.2 | D165N/K125A |
correctly folded, no significant deamidation |
673612 |
| 1.4.1.2 | D245K |
site-directed mutagenesis, discrimination against NADPH by factor 32, compared to 1000 for the wild-type enzyme |
726044 |
| 1.4.1.2 | D245K |
the mutation shows reduced activity and 36.4fold discrimination against NADPH compared to NADH |
686673 |
