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and maximal turnover rate.
The maximal turnover rate for pNPB was 60±2.2 U/mg for wild type and 33±1.1 U/mg for AVA-AA (Figure 5 and Table 2).
Kinetic measurements revealed a maximal turnover rate of 60 U/mg and a S0.5 value of 0.15 mM under our pNPB assay conditions.
From Vmax, the maximal turnover rate Vmax/[BoNT-B] can be evaluated, where [BoNT-B] is the toxin concentration, which in our setting was 500 pM.
Results from single-turnover experiments showed that the values of the maximal turnover rate (kpol) for all the mutants were greatly reduced.
The pEC50 for ACh hydrolysis by AChE is -6.6 with a hill slope of 0.9, while the enzyme saturates at a maximal turnover rate of 25,000/sec [ 19].
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The kinetic profiles of both isozymes were nearly identical: maximal turnover rates, reflected by the kcat values, were (1.8 ± 0.3) × 10 3 s–1 for PHLPP1 and (1.8 ± 0.1) × 10 3 s–1 for PHLPP2.
As a result the experimentally determined rates of 2 − 8 × 10−5 s−1 presumably reflect a maximal possible turnover rate, rather than a physiological turnover rate.
Simulation of the interconnected energy, electron and proton transfer processes showed a half-maximal ATP turnover rate for a light intensity equivalent to only 1% of bright sunlight.
No correlation was found between the basal and maximal ATP turnover rates.
The type 2 diabetic and control groups showed similar basal and maximal ATP turnover rates (Table 3).
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