Table 2 Thermodynamic parameters of ligand binding to PfCCT enzyme constructs.
PfCCT | Kd,CDP-Cho (µM) | ΔHCDP-Cho (kcal/mol) | −TΔSCDP-Cho (kcal/mol) | ΔGCDP-Cho (kcal/mol) | Kd,CTP (µM) | ΔHCTP (kcal/mol) | −TΔSCTP (kcal/mol) | ΔGCTP (kcal/mol) |
|---|---|---|---|---|---|---|---|---|
581–775 | 47 ± 5 | −10.5 ± 0.3 | 4.7 ± 0.4 | −5.8 ± 0.1 | N.D. | N.D. | N.D. | N.D. |
528–795 | 34 ± 1 | −16.1 ± 0.1 | 10.1 ± 0.1 | −6.0 ± 0.2 | 60 ± 2 | −8.6 ± 0.3 | 3.0 ± 0.4 | −5.7 ± 0.1 |
528–795 (K663A) | 210 ± 60 | −11.4 ± 1.5 | 6.5 ± 1.6 | −5.0 ± 1.4 | 520 ± 50 | 6.1 ± 9.3 | −10.5 ± 0.6 | −4.4 ± 0.1 |
528–795 (Y626F/Q636A) | 22.2 ± 0.2 | −12.0 ± 0.2 | 5.8 ± 0.1 | −6.2 ± 0.1 | 60 ± 2 | −10.8 ± 0.1 | 5.1 ± 0.2 | −5.7 ± 0.1 |
528–795 (T761A) | N.D. | N.D. | N.D. | N.D. | 170 ± 35 | −7.0 ± 0.8 | 1.9 ± 1.0 | −5.1 ± 0.1 |
528–795 (T762A) | N.D. | N.D. | N.D. | N.D. | 170 ± 12 | −10.5 ± 0.7 | 5.5 ± 0.8 | −5.1 ± 0.1 |
