Table 1.
Equilibrium dissociation constants for the binding of AXPs to phosphorylated AMPK.
Ligand | Kd (μM) | Kd,I (μM) | Kd,II (μM) |
---|---|---|---|
vs NADH | vs C-AXPs | ||
AMP | 1.6 (0.5) | 2.5 (0.6) | 80 (25) |
ADP | 1.3 (0.5) | 1.5 (0.4) | 50 (15) |
ATP | 0.9 (0.3) | 1.7 (0.5) | 65 (15) |
Mg-ATP | 32 (12) | 18 (7.5) | 230 (80) |
Dissociation constants were determined at 20°C by competition against NADH or C-AXPs in 25 mM Tris, 1 mM TCEP, 100 mM NaCl (pH 8) with and without 5 mM MgCl2. The Kd values are reported as the mean (± SD) determined from at least three independent measurements.