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Exact(5)
We found no marked increases in the Ki values of AZTTP and d4TTP at the ATP concentrations around the Ki' ATP value (1.1±0.4 mM) for ATP binding to the RT-template-primer-dTTP complex for the excision reaction (Figures 2C and 2D).
Finally, the KiATP value was larger than the Ki' ATP value in both RTs, suggesting that ATP binds with higher affinity to the dTTP-bound RT than to the substrate-free RT.
The Ki' ATP values were 1.2±0.5 and 1.1±0.4 mM for the 93JP-NH1 and ERT-mt6 RTs, respectively, suggesting that the ATP molecule also binds with the equivalent Ki' ATP value to complex 2 of these RTs.
The high ATP value is indicative of less energetically efficient pathway usage.
The average ATP value of all results within an institute was presented in the risk plot.
Similar(55)
The D113A/N and K219Q/A substitutions induced changes in the Km, kcat, KiATP, and Ki' ATP values, suggesting that the D113 and K219 residues regulate the Km of substrate, kcat, and Ki values of ATP (Figure 5).
This was followed by an intermediary acid shift, increases in ATP values and decreases in ADP, a late alkaline rebound, a decrease in P-Creatine levels, and elevations in both ADP and lactate levels.
NAD(H), NADP(H), and ATP values were normalized to protein concentrations (micro-BCA kit, Pierce).
Using Equations 3 and 4 (see Materials and Methods), we calculated KiATP and Ki' ATP values of ATP to the RT complexes 1 and 2, respectively.
The active D113A/N and K219Q/A RTs were further examined for changes in the IC50 of AZTTP, and in the Km, kcat, KiATP, and Ki' ATP values.
Km, kcat, KiATP, and Ki' ATP values were estimated by using the substrate-velocity curves for the D113A/N and K219Q/A RTs (Figure S4D).
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