<p>Enzyme activity was determined at a fixed concentration of IMP (1 mM for IMPDHbt and 2 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 and the calculated parameters are displayed in <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0116578#pone.0116578.t004" target="_blank">Table 4</a>.</p
Several approaches for determining an enzyme’s kinetic parameter Km (Michaelis constant) from progre...
<p>The Km and Vmax of PPT1 and PPT1 C6S were calculated using the Michaelis-Menten equation followin...
<p>Reactions of 200 µl contained 50 mM Tris-HCl buffer, pH 7.4, 10 µM Abz-GGFLRKHGQ-EDDnp and 1 µg o...
<p>Enzyme activity was determined at a fixed concentration of NAD (2 mM for IMPDHbt and 6 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...
Enzyme specific activity (μmol/min per mg protein) measured for (A) varying malate concentrations at...
Several approaches for determining an enzyme’s kinetic parameter K$_m$ (Michaelis constant) from pro...
<p>a b Double reciprocal plots of the relationship between the concentration of peptide substrate an...
After a century of applications of the seminal Michaelis-Menten equation since its advent it is time...
Analysis of enzyme kinetic data requires more than just comparisons of Kms and Vmaxs using the corre...
The use of the classic Henry-Michaelis-Menten (HMM) model (or simply, Michaelis-Menten model) to stu...
A novel method of estimating enzyme kinetic parameters is presented using the Lambert ω function cou...
<p>Michaelis-Menten parameters from steady-state kinetics with 2-deoxy-d-ribose-5-phosphate (D5P) as...
Several approaches for determining an enzyme’s kinetic parameter Km (Michaelis constant) from progre...
<p>The Km and Vmax of PPT1 and PPT1 C6S were calculated using the Michaelis-Menten equation followin...
<p>Reactions of 200 µl contained 50 mM Tris-HCl buffer, pH 7.4, 10 µM Abz-GGFLRKHGQ-EDDnp and 1 µg o...
<p>Enzyme activity was determined at a fixed concentration of NAD (2 mM for IMPDHbt and 6 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...
Enzyme specific activity (μmol/min per mg protein) measured for (A) varying malate concentrations at...
Several approaches for determining an enzyme’s kinetic parameter K$_m$ (Michaelis constant) from pro...
<p>a b Double reciprocal plots of the relationship between the concentration of peptide substrate an...
After a century of applications of the seminal Michaelis-Menten equation since its advent it is time...
Analysis of enzyme kinetic data requires more than just comparisons of Kms and Vmaxs using the corre...
The use of the classic Henry-Michaelis-Menten (HMM) model (or simply, Michaelis-Menten model) to stu...
A novel method of estimating enzyme kinetic parameters is presented using the Lambert ω function cou...
<p>Michaelis-Menten parameters from steady-state kinetics with 2-deoxy-d-ribose-5-phosphate (D5P) as...
Several approaches for determining an enzyme’s kinetic parameter Km (Michaelis constant) from progre...
<p>The Km and Vmax of PPT1 and PPT1 C6S were calculated using the Michaelis-Menten equation followin...
<p>Reactions of 200 µl contained 50 mM Tris-HCl buffer, pH 7.4, 10 µM Abz-GGFLRKHGQ-EDDnp and 1 µg o...