EC Number   |
Protein Variants |
Reference |
|---|
    4.1.1.32 | A467G |
PEPCK has a 14fold higher Km value for oxaloacetate than wild type, coupled with a reduction in kcat (26% of wild type), resulting in a reduction in catalytic efficiency by nearly two orders of magnitude (1.9% of wild type). There is little change in the Km for GTP (factor of 1.4), resulting in the catalytic efficiency for GTP decreasing by less than a factor of three. In the reverse reaction, the mutant shows a decrease in the Km value for phosphoenolpyruvate (21% of wild type), a kcat reduced to 5% of the wild type value, and a factor of four reduction in the catalytic efficiency relative to wild type |
714195 |
| 4.1.1.32 | C306A |
catalytically active mutant, kinetics |
649467 |
| 4.1.1.32 | C306S |
catalytically active mutant, kinetics |
649467 |
| 4.1.1.32 | D262N |
active site mutant, 5times higher catalytic efficiency than wild-type enzyme |
653038 |
| 4.1.1.32 | D263N |
increased Km-value for Mn2+ and phosphoenolpyruvate |
653038 |
| 4.1.1.32 | D75A |
75% reduced activity |
680727 |
| 4.1.1.32 | D75N |
reduced activity |
680727 |
| 4.1.1.32 | D75Q |
reduced activity |
680727 |
| 4.1.1.32 | D75S |
reduced activity |
680727 |
| 4.1.1.32 | D78A |
severely reduced activity |
680727 |
