TABLE 2.
Thermodynamic parameters, ΔG, ΔH, ΔS, number of binding sites (n), and the binding constant, Kd for donor binding with wild type K4CP in solution at 20 °C
UDP-GlcA and UDP-GalNAc concentrations were 1 mm; UDP and UDP-GalNAc concentrations were 4 mm. K4CP concentration was 124.8 μm. All of the experiments were conducted in triplicate to confirm the results obtained. Fresh enzyme was prepared for each experiment.
| Substrate | ΔG | ΔH | ΔS | Kd | n |
|---|---|---|---|---|---|
| cal/mol | cal/mol | cal/mol/deg | μm | ||
| UDP-GlcA | -7209.1 ± 1124 | -11,270 ± 1124 | -13.86 | 8.05 ± 1.52 | 0.95 ± 0.07 |
| UDP-GalNAc | -4779.2 ± 483.9 | -11,630 ± 483.9 | -22.61 | 358.17 ± 26.64 | 1.25 ± 0.32 |
| UDP | -5431.7 ± 1953 | -8643 ± 1953 | -10.96 | 89.53 ± 22.77 | 0.91 ± 0.09 |