<p>Steady state kinetics experiments of RM.BpuSI cleavage activity were carried out by incubating 200 nM of purified RM.BpuSI protein with 1.25 to 25 μM of FAM-labeled sub01 at 37°C for 1 h in the presence or absence of 160 μM of SAM or SIN. The initial rate (v) for each substrate concentration was plotted against substrate concentration. K<sub>m</sub> and V<sub>max</sub> values were obtained by fitting the data points to the Michaelis-Menten equation. Error bars indicate the standard deviation of the fitting of the initial linear rate of each data point.</p
<p>(<b>A</b>) Steady-state kinetic analysis of GTP stimulated hydrolysis of TTP, by SAMHD1 (115–626)...
<p>(A) Fluorescence spectra of WT and N406A RM.BpuSI. The high similarity of the two spectra indicat...
<p>[A] <i>v versus</i> [APS] in the ATP synthesis reaction at 1 mM pyrophosphate. [B] <i>v versus</i...
<p>Rate of cleavage (k<sub>app</sub>) of pSu1 and pATSer variants at 10 mM Mg<sup>2+</sup>.</p
<p>Concentration dependence of RsASML activity towards (a) pNPP, (b) pNPPC, (c) pNP-TMP. All reactio...
<p>The concentration of indicated protease fragments and the substrates xLC3B-MBP (left) or xGATE16-...
<p>Example data set showing the decrease of substrate concentration in time in for a range of PA-Nte...
<p>HK (200 µg/ml) was incubated with (<b>A</b>) kallikrein (0.5 µg/ml), (<b>B</b>) rMASP-1 (50 µg/ml...
<p>(A) The initial enzyme velocity of caspase-6 was plotted against the indicated concentration of (...
<p>Assays were performed using 10 µM enzyme and 0–10 mM MSmB in 50 mM HEPES (pH 7.5) at 37°C.</p><p>...
<p>A, cleavage kinetics of collagens by MMP1 in molecules with Cys for α1(I) Gly or Cys for α1(I) Ar...
<p>The rate of substrate Suc-LLVY-AMC hydrolysis (a release of AMC molecule) with control and inhibi...
<p>Kinetic constants for cleavage of pATSerUG with RPR variants at 800 mM Mg<sup>2+</sup> as indicat...
AbstractThe kinetics of AMP-aminohydrolase, which under steady state conditions shows a typical sigm...
<p>Aβ1<b>–</b>40 cleavage activity was determined at 0.4<b>–</b>50<b> µ</b>M substrate with 40<b> </...
<p>(<b>A</b>) Steady-state kinetic analysis of GTP stimulated hydrolysis of TTP, by SAMHD1 (115–626)...
<p>(A) Fluorescence spectra of WT and N406A RM.BpuSI. The high similarity of the two spectra indicat...
<p>[A] <i>v versus</i> [APS] in the ATP synthesis reaction at 1 mM pyrophosphate. [B] <i>v versus</i...
<p>Rate of cleavage (k<sub>app</sub>) of pSu1 and pATSer variants at 10 mM Mg<sup>2+</sup>.</p
<p>Concentration dependence of RsASML activity towards (a) pNPP, (b) pNPPC, (c) pNP-TMP. All reactio...
<p>The concentration of indicated protease fragments and the substrates xLC3B-MBP (left) or xGATE16-...
<p>Example data set showing the decrease of substrate concentration in time in for a range of PA-Nte...
<p>HK (200 µg/ml) was incubated with (<b>A</b>) kallikrein (0.5 µg/ml), (<b>B</b>) rMASP-1 (50 µg/ml...
<p>(A) The initial enzyme velocity of caspase-6 was plotted against the indicated concentration of (...
<p>Assays were performed using 10 µM enzyme and 0–10 mM MSmB in 50 mM HEPES (pH 7.5) at 37°C.</p><p>...
<p>A, cleavage kinetics of collagens by MMP1 in molecules with Cys for α1(I) Gly or Cys for α1(I) Ar...
<p>The rate of substrate Suc-LLVY-AMC hydrolysis (a release of AMC molecule) with control and inhibi...
<p>Kinetic constants for cleavage of pATSerUG with RPR variants at 800 mM Mg<sup>2+</sup> as indicat...
AbstractThe kinetics of AMP-aminohydrolase, which under steady state conditions shows a typical sigm...
<p>Aβ1<b>–</b>40 cleavage activity was determined at 0.4<b>–</b>50<b> µ</b>M substrate with 40<b> </...
<p>(<b>A</b>) Steady-state kinetic analysis of GTP stimulated hydrolysis of TTP, by SAMHD1 (115–626)...
<p>(A) Fluorescence spectra of WT and N406A RM.BpuSI. The high similarity of the two spectra indicat...
<p>[A] <i>v versus</i> [APS] in the ATP synthesis reaction at 1 mM pyrophosphate. [B] <i>v versus</i...