Table 2.
Kinetic parameters of mutated forms of glucokinase
| Mutant | S0.5 (mM) | Hill number | Vmax (units/mg) | Km ATP (mM) |
| Wild type | 7.52±0.31 | 1.65±0.04 | 19.9±2.0 | 0.41±0.03 |
| A456V | 1.81±0.12 | 1.25±0.20 | 32.4±1.7 | 0.28±0.02 |
| C457V | 5.90±0.92 | 1.15±0.22 | 22.9±3.2 | 0.65±0.06 |
| K458R | 12.28±1.10 | 1.34±0.11 | 21.8±0.6 | 0.81±0.15 |
| K459L | 7.03±0.32 | 1.65±0.19 | 33.4±2.0 | 0.60±0.04 |
| A460R | 1.94±0.31 | 1.10±0.15 | 23.3±3.2 | 0.55±0.03 |
| A208G | 5.66±0.61 | 1.38±0.23 | 17.0±2.0 | 0.43±0.08 |
| Y215A | 2.20±0.19 | 1.33±0.09 | 20.4±2.3 | 0.65±0.02 |
| Y214C | 1.87±0.30 | 1.32±0.15 | 41.6±2.1 | 0.29±0.02 |
Glucose-dependent activity (S0.5, Hill number, Vmax) and ATP-dependent activity (Km) parameters were determined in purified GST-GlkB fusion proteins. Values are the mean of at least three different purifications for each mutant±standard deviation.