Table 2. Statistics of Kd Values of Wild-Type UGT708C1 and Mutants for Binding of Different Substrates.
| Protein | Kd (for UDP-Galactose) | Kd (for 2′,4′,6′-Trihydroxyacetophenone) |
|---|---|---|
| Wild-type UGT708C1 | 181 ± 2.3 µM | 5.42 ± 2.00 mMa |
| Kd (for UDP-Glucose) | Kd (for Phloretin) | |
| Wild-type UGT708C1 | 47.88 ± 5.74 µM | 12.90 ± 2.53 µM |
| F130A | 130 ± 20 µM | 1.56 ± 0.33 µM |
| Y102F | 470 ± 90 µM | 12 ± 67 mMa |
| F198A | 130 ± 30 µM | 250 ± 150 µMa |
| T150A | 102 ± 32 µM | 25.76 ± 4.72 µM |
| T151A | 1.06 ± 0.30 mM | 3.48 ± 0.85 µM |
| D382E | 0.80 ± 0.23 mM | 1.71 ± 3.65 mMa |
| Q383H | 670 ± 80 µM | 22.46 ± 8.90 µM |
| Q383A | 630 ± 110 µM | 16.98 ± 2.92 µM |
Each kinetic parameter was calculated from three independent thermophoresis measurements. Data are shown as means ± sd (n = 3).
a
In these values, the Kd value between the corresponding protein and the substrate is too large to be measured more accurately, due to the solubility limitation of the substrate.