<p>Determination of the kinetic parameters of PepN for the substrate H-Ala-<i>p</i>NA according to Michaelis-Menten analysis (A) and Lineweaver-Burk linearization (B) (each point represents the average of triplicate measurements; the standard deviation was <5%).</p
Several approaches for determining an enzyme’s kinetic parameter K$_m$ (Michaelis constant) from pro...
<p>All compounds were characterized by a combination of specific velocity plots (upper panels) and t...
<p>Kinetic parameters for <i>Lm</i>TK are means of two or more independent experiments.</p><p>N.D. N...
<p>Lineweaver-Burk linearization of PepX inhibition by H-L-Phe-L-Pro-OH (H-Ala-Pro-<i>p</i>NA as sub...
<p>Michaelis-Menten kinetic parameters of endomannanases for LBG-mannan substrate.</p
<p>Determination of kinetic parameters of Sare0718 for L-Ala by Michaelis-Menten analysis using nonl...
1<p>Protein concentration of the enzyme solution: 2.61 mg mL<sup>−1</sup>.</p>2<p>Substrate for the ...
<p>Michaelis-Menten parameters from steady-state kinetics with 2-deoxy-d-ribose-5-phosphate (D5P) as...
<p>Comparison of the kinetic parameters (K<sub>m</sub>, k<sub>cat</sub>, k<sub>cat</sub>/K<sub>m</su...
The statistical implications of the direct linear plot for enzyme kinetic data, described in the pre...
<p>* based on historical values [<a href="http://www.plosone.org/article/info:doi/10.1371/journal.po...
<p>*Initial rate at each substrate concentration was fitted into Michaelis-Menten equation to determ...
<p>Michaelis-Menten kinetic parameters of Zn-peptide complexes of variants derived for the hydrolysi...
A novel method of estimating enzyme kinetic parameters is presented using the Lambert ω function cou...
<p>Each experiment was repeated three times.</p><p>Kinetic parameters for hydrolytic substrates of l...
Several approaches for determining an enzyme’s kinetic parameter K$_m$ (Michaelis constant) from pro...
<p>All compounds were characterized by a combination of specific velocity plots (upper panels) and t...
<p>Kinetic parameters for <i>Lm</i>TK are means of two or more independent experiments.</p><p>N.D. N...
<p>Lineweaver-Burk linearization of PepX inhibition by H-L-Phe-L-Pro-OH (H-Ala-Pro-<i>p</i>NA as sub...
<p>Michaelis-Menten kinetic parameters of endomannanases for LBG-mannan substrate.</p
<p>Determination of kinetic parameters of Sare0718 for L-Ala by Michaelis-Menten analysis using nonl...
1<p>Protein concentration of the enzyme solution: 2.61 mg mL<sup>−1</sup>.</p>2<p>Substrate for the ...
<p>Michaelis-Menten parameters from steady-state kinetics with 2-deoxy-d-ribose-5-phosphate (D5P) as...
<p>Comparison of the kinetic parameters (K<sub>m</sub>, k<sub>cat</sub>, k<sub>cat</sub>/K<sub>m</su...
The statistical implications of the direct linear plot for enzyme kinetic data, described in the pre...
<p>* based on historical values [<a href="http://www.plosone.org/article/info:doi/10.1371/journal.po...
<p>*Initial rate at each substrate concentration was fitted into Michaelis-Menten equation to determ...
<p>Michaelis-Menten kinetic parameters of Zn-peptide complexes of variants derived for the hydrolysi...
A novel method of estimating enzyme kinetic parameters is presented using the Lambert ω function cou...
<p>Each experiment was repeated three times.</p><p>Kinetic parameters for hydrolytic substrates of l...
Several approaches for determining an enzyme’s kinetic parameter K$_m$ (Michaelis constant) from pro...
<p>All compounds were characterized by a combination of specific velocity plots (upper panels) and t...
<p>Kinetic parameters for <i>Lm</i>TK are means of two or more independent experiments.</p><p>N.D. N...