<p>The kinetic parameters (n = 3) were determined for the fluorogenic substrates <b>1</b> and <b>5</b>–<b>14</b> (measured using substrate range of 0.1–8 μM) with caspase-3 and caspase-7. Substrate <b>4</b> or the d-amino acids containing <b>15</b>–<b>24</b> were not cleaved by either enzyme.</p
<p>Enzyme assays were performed in 50 mM phosphate buffer (pH 8.0) at 75°C using <i>p</i>NPC4 as the...
A protease can be defined as an enzyme capable of hydrolyzing peptide bonds. Thus, characterization ...
<p>The kinetic parameters, Km and Vm, measured at 5μM and 100μM PLP for ClACS7, W<sup>364</sup>, K<s...
<p>All compounds were characterized by a combination of specific velocity plots (upper panels) and t...
*<p>FheCL3 kinetic parameters were taken from Corvo <i>et al</i>, 2009 <a href="http://www.plosntds....
<p>Steady-state kinetics parameters for Fluor-de-Lys substrate with KDAC8 in assay buffer 2.</p
<p>Where, pept represents the αDG(613–651) peptide, <sup><i>0</i></sup><i>k</i><sub><i>cat</i></sub>...
a<p>Vmax is expressed in pmol AMC/min/<i>µ</i>g enzyme.</p>b<p>Value from Cortesio and Jiang <a href...
<p>Enzyme kinetics parameter value represents mean ± SE from three independent experiments performed...
<p>8325–4 WT and <i>srtA</i> KO strains were incubated in the presence of (A) either 1 mM of substra...
<p>H3K9me2 vs. H3K9me3 peptide substrate analogues, depicting the different <i>k</i><sub>cat</sub>/<...
Contains fulltext : 161454.pdf (publisher's version ) (Open Access)Radboud Univers...
<p>The kinetic parameters (<i>Km</i>, <i>Vmax</i>, and <i>Kcat</i>) values were determined from Mich...
<p>Kinetic parameters of the β-lactamases IMP-1 and IMP-34 with various substrates.</p
<p>Each experiment was repeated three times.</p><p>Kinetic parameters for hydrolytic substrates of l...
<p>Enzyme assays were performed in 50 mM phosphate buffer (pH 8.0) at 75°C using <i>p</i>NPC4 as the...
A protease can be defined as an enzyme capable of hydrolyzing peptide bonds. Thus, characterization ...
<p>The kinetic parameters, Km and Vm, measured at 5μM and 100μM PLP for ClACS7, W<sup>364</sup>, K<s...
<p>All compounds were characterized by a combination of specific velocity plots (upper panels) and t...
*<p>FheCL3 kinetic parameters were taken from Corvo <i>et al</i>, 2009 <a href="http://www.plosntds....
<p>Steady-state kinetics parameters for Fluor-de-Lys substrate with KDAC8 in assay buffer 2.</p
<p>Where, pept represents the αDG(613–651) peptide, <sup><i>0</i></sup><i>k</i><sub><i>cat</i></sub>...
a<p>Vmax is expressed in pmol AMC/min/<i>µ</i>g enzyme.</p>b<p>Value from Cortesio and Jiang <a href...
<p>Enzyme kinetics parameter value represents mean ± SE from three independent experiments performed...
<p>8325–4 WT and <i>srtA</i> KO strains were incubated in the presence of (A) either 1 mM of substra...
<p>H3K9me2 vs. H3K9me3 peptide substrate analogues, depicting the different <i>k</i><sub>cat</sub>/<...
Contains fulltext : 161454.pdf (publisher's version ) (Open Access)Radboud Univers...
<p>The kinetic parameters (<i>Km</i>, <i>Vmax</i>, and <i>Kcat</i>) values were determined from Mich...
<p>Kinetic parameters of the β-lactamases IMP-1 and IMP-34 with various substrates.</p
<p>Each experiment was repeated three times.</p><p>Kinetic parameters for hydrolytic substrates of l...
<p>Enzyme assays were performed in 50 mM phosphate buffer (pH 8.0) at 75°C using <i>p</i>NPC4 as the...
A protease can be defined as an enzyme capable of hydrolyzing peptide bonds. Thus, characterization ...
<p>The kinetic parameters, Km and Vm, measured at 5μM and 100μM PLP for ClACS7, W<sup>364</sup>, K<s...