EC Number |
Protein Variants |
Reference |
---|
1.1.1.49 | A117S/F277I/Q324H/M381I/V443I/S470I |
t1/2 for the mutant enzyme at 60°C is 95fold higher than the t1/2 value for the wild-type enzyme |
-, 760410 |
1.1.1.49 | A117S/Q324H/M381I/V443I/S470I |
t1/2 for the mutant enzyme at 60°C is 75fold higher than the t1/2 value for the wild-type enzyme |
-, 760410 |
1.1.1.49 | A117S/Q324H/V443I/S470I |
t1/2 for the mutant enzyme at 60°C is 13.5fold higher than the t1/2 value for the wild-type enzyme |
-, 760410 |
1.1.1.49 | A44T |
asymptomatic patient with high in vitro glucose-6-phosphate dehydrogenase deficiency, carrying a inherited mutation at A55T |
686131 |
1.1.1.49 | G163D |
mutant is markedly less stable than wild-type G6PD in both thermostability and urea-induced inactivation tests. According to unfolding and refolding experiments, the mutant is impaired in its folding properties. KM-values and turnover numbers are similar to wild-type values |
689022 |
1.1.1.49 | G163S |
mutant markedly less stable than wild-type G6PD in both thermostability and urea-induced inactivation tests. According to unfolding and refolding experiments, the mutant is impaired in its folding properties. KM-values and turnover numbers are similar to wild-type values |
689022 |
1.1.1.49 | G488S |
clinical mutant G6PDFukaya, mutation in the vicinity of the structural NADP+ site, elevated Kd values of the structural NADP+, is denatured by guanidinium hydrochloride and refolded by rapid dilution in the presence of L-Arg, NADP+ and dithiothreitol at 25°C, displays decreased thermostability and high susceptibility to chymotrypsin digestion as compared to the wild-type |
696447 |
1.1.1.49 | G488V |
clinical mutant G6PDCampinas, mutation in the vicinity of the structural NADP+ site, elevated Kd values of the structural NADP+, is denatured by guanidinium hydrochloride and refolded by rapid dilution in the presence of L-Arg, NADP+ and dithiothreitol at 25°C, displays decreased thermostability and high susceptibility to chymotrypsin digestion as compared to the wild-type |
696447 |
1.1.1.49 | K18A |
the mutant with reduced catalytic efficiency shows 35fold preference for NADP+ over NAD+ as compared to the wild type enzyme (386fold) |
741254 |
1.1.1.49 | K18A/R50A |
the mutant shows almost no activity |
741254 |