Table 1.
Opposing Base | K1/2 (μM) | kmax (min−1) | kmax/K1/2b (M−1s−1) | Relative kmax/K1/2 |
---|---|---|---|---|
Bulge (none) | 0.08 | 5.4 | 1.1×106 | 3 |
T | 0.30 | 6.3 | 3.5×105 | (1) |
G | 0.41 | 1.5 | 6.2×104 | 0.2 |
C | 3.8 | 3.3 | 1.4×104 | 0.04 |
A | 2.3 | 2.0 | 1.4×104 | 0.04 |
Single strand | 0.34 | 0.0035 | 1.7×102 | 0.0005 |
Data from 23 °C in 50 mM NaMES, pH 6.1, 1 mM EDTA, 1 mM DTT, 0.1 mg/mL BSA. Ionic strength was adjusted to 200 mM with NaCl.
kmax/K1/2 is a measure of the catalytic efficiency, analogous to kcat/KM in steady state kinetics.