Table 3. Kinetic characterisation of GCK-MODY mutations.
| GCK-GST | S0.5 [mmol/L] | Hill number | ATPKm [mmol/L] | Kcat S0.5 [s−1] | Relative Activity Index (RAI) |
| WT | 7.69±0.10 | 1.67±0.01 | 0.44±0.01 | 65.78±0.84 | 1 |
| I110N | 14.87±0.25 | 1.37±0.03 | 0.03±<0.01 | 3.07±0.04 | 0.02 |
| V200A** | 78.3±0.97 | 1.28±0.01 | 0.69±0.07 | 56.85±0.81 | 0.01 |
| N204D | NO | NO | 5.42±0.10 | NO | NO |
| V244G* | 12.77±0.33 | 1.52±0.02 | 0.4±0.01 | 75.71±1.36 | 0.43 |
| G258R | NO | NO | NO | NO | NO |
| G223S | 16.5±0.16 | 1.46±0.02 | 0.47±0.01 | 74.45±1.63 | 0.25 |
| L315H | 8.09±0.06 | 1.67±0.01 | 0.50±0.01 | 69.21±0.63 | 0.89 |
| F419S# | 161.50±1.64 | 1.12±0.01 | 6.14±0.23 | 82.10±0.80 | <0.01 |
| I436N | 7.84±0.25 | 1.66±0.02 | 0.50±0.03 | 73.77±0.73 | 1.07 |
Data are given as mean ±SEM measured in n≥12 experiments. GCK-GST enzymes were prepared as 3 (WT)/2 (G258R)/1 (others) independent protein expressions. Glucose S0.5 values were normally measured in the glucose range 0–100 mmol/L with 5 mmol/L ATP, however for some mutant enzymes the glucose range was increased to 0–300 mmol/L (*), 0–600 mmol/L (**), or 0–1000 mmol/L with 25 mmol/L ATP (#).
NO = data not obtainable due to the severity of the kinetic inactivation which prevented the data from reaching a plateau even with a 10-fold increase in glucose concentration.