<p>Enzyme activity was determined at a fixed concentration of NAD (2 mM for IMPDHbt and 6 mM for IMPDHlpp), and in the absence (red curve) or in the presence (blue curve) of 5 mM MgATP. The curves correspond to the fit of the experimental data to the Michaelis-Menten equation for IMPDHbt and Hill equation for IMPDHlpp and the calculated parameters are displayed in <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0116578#pone.0116578.t005" target="_blank">Table 5</a>.</p
<p>In (A, C and E) the effect of Fru 1,6-BP (closed symbols) is shown in <i>Vc</i>IPK and in (B, D a...
Several approaches for determining an enzyme’s kinetic parameter K$_m$ (Michaelis constant) from pro...
<p>MIPS-160 (<b>A</b>) and IMPase 1 (<b>B</b>) activity changes when concentration of ions (NaCl or ...
<p>Enzyme activity was determined at a fixed concentration of IMP (1 mM for IMPDHbt and 2 mM for IMP...
<p>Reaction rates were determined at constant IMP and NAD concentrations (respectively, 0.05 mM and ...
<p>NADP<sup>+</sup>-dependent activity (black circles) and activity with NAD<sup>+</sup> (white circ...
<p>NADP<sup>+</sup>-dependent activity (black circles) and activity with NAD<sup>+</sup> (white circ...
<p>(<b>A</b>) MIPS-160 and IMPase 1 were incubated with their respective substrates at different pH,...
<p>a b Double reciprocal plots of the relationship between the concentration of peptide substrate an...
<p>(A) Semi-log plot of the V<sub>i</sub> concentration dependence of the trapped enzyme fraction wi...
a<p>When calculating the <i>K</i><sub>m</sub> for isocitrate, the concentration of D-isocitrate was ...
A novel rate equation is derived to characterize the dose-response behavior of a moderately potent (...
<p><i>Mt</i>PRS expressed as its fractional activity; and ADP, GDP and UMP concentrations were plott...
<p>X-axis represents the concentration of added TMTFA corresponding to actual enzyme concentrations ...
<p>Reactions of 200 µl contained 50 mM Tris-HCl buffer, pH 7.4, 10 µM Abz-GGFLRKHGQ-EDDnp and 1 µg o...
<p>In (A, C and E) the effect of Fru 1,6-BP (closed symbols) is shown in <i>Vc</i>IPK and in (B, D a...
Several approaches for determining an enzyme’s kinetic parameter K$_m$ (Michaelis constant) from pro...
<p>MIPS-160 (<b>A</b>) and IMPase 1 (<b>B</b>) activity changes when concentration of ions (NaCl or ...
<p>Enzyme activity was determined at a fixed concentration of IMP (1 mM for IMPDHbt and 2 mM for IMP...
<p>Reaction rates were determined at constant IMP and NAD concentrations (respectively, 0.05 mM and ...
<p>NADP<sup>+</sup>-dependent activity (black circles) and activity with NAD<sup>+</sup> (white circ...
<p>NADP<sup>+</sup>-dependent activity (black circles) and activity with NAD<sup>+</sup> (white circ...
<p>(<b>A</b>) MIPS-160 and IMPase 1 were incubated with their respective substrates at different pH,...
<p>a b Double reciprocal plots of the relationship between the concentration of peptide substrate an...
<p>(A) Semi-log plot of the V<sub>i</sub> concentration dependence of the trapped enzyme fraction wi...
a<p>When calculating the <i>K</i><sub>m</sub> for isocitrate, the concentration of D-isocitrate was ...
A novel rate equation is derived to characterize the dose-response behavior of a moderately potent (...
<p><i>Mt</i>PRS expressed as its fractional activity; and ADP, GDP and UMP concentrations were plott...
<p>X-axis represents the concentration of added TMTFA corresponding to actual enzyme concentrations ...
<p>Reactions of 200 µl contained 50 mM Tris-HCl buffer, pH 7.4, 10 µM Abz-GGFLRKHGQ-EDDnp and 1 µg o...
<p>In (A, C and E) the effect of Fru 1,6-BP (closed symbols) is shown in <i>Vc</i>IPK and in (B, D a...
Several approaches for determining an enzyme’s kinetic parameter K$_m$ (Michaelis constant) from pro...
<p>MIPS-160 (<b>A</b>) and IMPase 1 (<b>B</b>) activity changes when concentration of ions (NaCl or ...