TABLE 1.
Experimental inhibition constants (KEO,I) obtained from kinetic studies
| DmADH (30)
|
DlADH (27,66)
|
||||
|---|---|---|---|---|---|
| PYR
|
TFE
|
PYR
|
TFE
|
||
| pH | KEO,I (μM) | KEO,I (mM) | pH | KEO,I (μM) | KEO,I (mM) |
| 10 | 4.5 (−7.26) | 1.1 (−4.01) | 10 | 12 (−6.69) | |
| 9.5 | 4.3 (−7.29) | 1.1 (−4.01) | 9.5 | 14 (−6.58) | 2.5 (−3.53) |
| 8.5 | 4.5 (−7.26) | 1.1 (−4.01) | 9 | 12 (−6.69) | |
| 7.5 | 8.8 (−6.86) | 2.1 (−3.63) | 8 | 15 (−6.55) | |
| 6.6 | 26 (−6.23) | 7.3 (−2.9) | 7 | 22 (−6.32) | |
| 5.9 | 37 (−6.02) | 9.3 (−2.7) | 6 | 63 (−5.71) | |
E = enzyme, O = NAD+, and I = inhibitor. The values in parentheses are the corresponding free energy of binding (kcal/mol) calculated by ΔG = −RTlnKi.