Table 1. Thermodynamic parameters of ligand binding to mycobacterial CoaE at pH 7.8 and 20°C.
| Titrant | N | ΔH (cal/M−1) | Ka (M−1*104) | ΔS (calM−1K−1) |
| ATP alone | 0.683 | −495.3 (±36.3) | 1.18 (±0.14) | 16.9 (±1.21) |
| DCoA alone | 0.810 | −3719 (±201.5) | 1.43 (±0.34) | 6.32 (±0.34) |
| NHATP binding on DCoA-saturated CoaE | 0.947 | −3776 (±234.5) | 2.06 (±0.47) | 6.85 (±0.48) |
| DCoA binding on NH-ATP-saturated CoaE | 0.839 | −1063 (±71.3) | 1.85 (±0.25) | 15.9 (±0.91) |
| CoA alone | NB | NB | NB | NB |
| ADP binding on DCoA-saturated CoaE | 1.07 | −3612 (274.8) | 2.03 (±0.51) | 7.38 (±0.78) |
| ADP binding on CoA-saturated CoaE | 1.23 | −2138 (±181.5) | 2.88 (±0.58) | 13.1 (±0.98) |
| dATP binding on DCoA-saturated CoaE | 0.871 | −848 (±54.7) | 1.74 (±0.24) | 16.4 (±1.85) |
| CTP binding | 1.08 | −482.5 (±37.4) | 1.59 (±0.19) | 17.6 (±1.11) |
| GTP binding | NB | NB | NB | NB |
Values of ΔH and ΔS are in cal mol−1K−1. Values are the mean of five individual experiments. Ka is the binding constant determined by ITC and its values are in M−1.