TABLE 2.
Substrate | ΔG° (kJ/mol) | δ(ΔG°) (kJ/mol) | Control |
---|---|---|---|
Hypoxanthine | −34.4 | ||
Adenine | −31.9 | 2.5 | HX |
Allopurinol | −26.2 | 8.2 | HX |
Aminopurinol | −22.3 | 9.6 | Adenine |
Xanthine | −28.9 | 5.5 | HX |
Guanine | −34.2 | 0.2 | HX |
Inosine | −20.3 | 14.1 | HX |
Adenosine | −17.9 | 14.0 | Adenine |
Guanosine | −21.9 | 12.3 | Guanine |
Purine | −32.5 | −0.6 | Adenine |
1-Deazapurine | −25.3 | 7.2 | Purine |
3-Deazaguanine | −23.0 | 11.2 | Guanine |
6-Thioguanine | −29.7 | 4.5 | Guanine |
7-Deazaguanine | >−18 | 16.2 | Guanine |
9-Deazaguanine | −21.9 | 12.3 | Guanine |
The Gibbs free energy of substrate-transporter interaction was calculated from the Km and Ki values listed in Table 1, using the Nernst equation as described previously (19,58). The difference between the value and that with a control compound (either hypoxanthine [HX] as the highest-affinity compound, the corresponding physiological nucleobase [in the case of chemical analogues], or the corresponding nucleobase [in the case of nucleosides]) yielded the δ(ΔG°), the loss in binding energy relative to the control compound.