a<p>In all cases except for the cooperative model with the mutant S35A, k<sub>obs</sub> and K correspond to k<sub>cat</sub> and K<sub>m</sub> of the applied Michaelis-Menten model;</p>b<p>WT = 100; <sup>c</sup> k<sub>obs</sub> and K could not be determined in a reliable manner, since the substrate did not reach the range of saturating levels.</p
<p>*the best fit values of <i>k<sub>cat</sub></i> and <i>K<sub>M</sub></i> were determined by non-li...
<p>Michaelis-Menten parameters from steady-state kinetics with 2-deoxy-d-ribose-5-phosphate (D5P) as...
<p>Rate constants for model of cooperative enzyme kinetics with substrate input (SBML files F3 and F...
<p>(<b>A</b>) Basal GTPase activities of wild-type DNM1L, DNM1L GG fusion protein and full-length mu...
<p>NADP<sup>+</sup>-dependent activity (black circles) and activity with NAD<sup>+</sup> (white circ...
<p>(A) Domain architecture of dynamin showing the position of point mutation within the GTPase domai...
<p>NADP<sup>+</sup>-dependent activity (black circles) and activity with NAD<sup>+</sup> (white circ...
<p>Identified Chk1 target residues in GST-wt CK1δ (FP449) were exchanged to alanine and the kinetic ...
<p>All active site and dimerization residues that have been mutated to alanine are represented as st...
<p>n.a. not available; experimental data could not be fitted.</p><p>Initial velocity rates at GAP co...
a<p><i>K</i><sub>m,BAEE</sub>: Michaelis constant for benzoyl-L-arginine ethyl ester (BAEE) as the <...
<p>Kinetic parameters are provided for wild-type and variant forms of <i>Cp</i>Arap27 acting on thre...
<p>All enzymes showed Michaelis-Menten kinetics with the tolerated amino acid substrates. The V<sub>...
<p><b>A)</b> Wild type enzyme (gray bars) exhibited preference for nucleoside diphosphate sugar (NDP...
A common variant of the Michaelis-Menten model of enzyme kinetics involves inhibition by excess subs...
<p>*the best fit values of <i>k<sub>cat</sub></i> and <i>K<sub>M</sub></i> were determined by non-li...
<p>Michaelis-Menten parameters from steady-state kinetics with 2-deoxy-d-ribose-5-phosphate (D5P) as...
<p>Rate constants for model of cooperative enzyme kinetics with substrate input (SBML files F3 and F...
<p>(<b>A</b>) Basal GTPase activities of wild-type DNM1L, DNM1L GG fusion protein and full-length mu...
<p>NADP<sup>+</sup>-dependent activity (black circles) and activity with NAD<sup>+</sup> (white circ...
<p>(A) Domain architecture of dynamin showing the position of point mutation within the GTPase domai...
<p>NADP<sup>+</sup>-dependent activity (black circles) and activity with NAD<sup>+</sup> (white circ...
<p>Identified Chk1 target residues in GST-wt CK1δ (FP449) were exchanged to alanine and the kinetic ...
<p>All active site and dimerization residues that have been mutated to alanine are represented as st...
<p>n.a. not available; experimental data could not be fitted.</p><p>Initial velocity rates at GAP co...
a<p><i>K</i><sub>m,BAEE</sub>: Michaelis constant for benzoyl-L-arginine ethyl ester (BAEE) as the <...
<p>Kinetic parameters are provided for wild-type and variant forms of <i>Cp</i>Arap27 acting on thre...
<p>All enzymes showed Michaelis-Menten kinetics with the tolerated amino acid substrates. The V<sub>...
<p><b>A)</b> Wild type enzyme (gray bars) exhibited preference for nucleoside diphosphate sugar (NDP...
A common variant of the Michaelis-Menten model of enzyme kinetics involves inhibition by excess subs...
<p>*the best fit values of <i>k<sub>cat</sub></i> and <i>K<sub>M</sub></i> were determined by non-li...
<p>Michaelis-Menten parameters from steady-state kinetics with 2-deoxy-d-ribose-5-phosphate (D5P) as...
<p>Rate constants for model of cooperative enzyme kinetics with substrate input (SBML files F3 and F...