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Determining enzyme kinetics for systems biology with nuclear magnetic resonance spectroscopy

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Figure

Figure 1. A work flow diagram. 3. Deconvolution V f S0.5 P0.5 h M0.5 α Mv = Vf S0.5S 1− K eqΓ S0.5S + P 0.5P h− 11+MM 0.5h1+ α M 2h MM 0.5h+S0.5S+P 0.5P h((((((((0chemical shift (ppm)timeconcentration4
Figure 2. 31 P NMR (a) The e ffect of EDTA on the line shapes of ATP using 31 P NMR.
Figure 3. Spline fits of 31 P-NMR Phosphofructokinase data. Data were acquired using a 90 ◦ pulse angle to collect 100 transients per FID using a repetition time of 1 s (0.5 s acquisition time, 0.5 s relaxation delay)
Table 1. Cont. PFK v = V f f6p h atp h1+peph1+α4hpeph+1+α2hpeph1+α4hpeph( f6p h +atp h ) + ( f6p h atp h ) V f 0.4435 ±0.0001 µmol.min −1 .mg −1F6P0.50.4174 ±0.00006mMATP0.50.5444 ±0.0003dmM allosteric modifier: PEP PEP 0.5 0.0863 ±0.0001 mM bi-substr
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