<p>Kinetic parameters for human wild-type and nucleotide-binding mutant variants of c-NADP-ME.</p
<p>Data represent means ± SEM of 3 separate enzyme expressions each tested in duplicate. Note that t...
<p>Kinetic parameters are provided for wild-type and variant forms of <i>Cp</i>Arap27 acting on thre...
<p>Kinetic parameters for “wild type” Tgt and mutated Tgt variants.<sup><a href="http://www.plosone....
<p>Kinetic parameters of the M36 mutant with respect to dC, gemcitabine and AraC.</p
<p>Steady state kinetic parameters for HtrA2 wild type, variants and mutants with β-casein as the su...
<p>W, wild type UGT74S1; UDP-gluc, UDP-glucose.</p><p>Kinetic parameters of wild type and mutant UGT...
<p>Kinetic parameters of LmbC, CcbC and selected CcbC mutants for various substrates.</p
a<p>Residual enzyme activity by inhibition at 3 mM ATP.</p>b<p>using NAD<sup>+</sup> or NADP<sup>+</...
<p>Steady state kinetic parameters for mutants of PMM/PGM in the conversion of glucose 1-phosphate t...
<p>Specific activities were measured in 50 mM phosphate buffer (pH 8.0) at 75°C using <i>p</i>NPC4 a...
<p>Kinetic parameters for the substrate hydrolysis by the wild-type and mutant Sfβgly.</p
<p>Comparison of the kinetic parameters for the α-KG reduction activity of the mutant IDHs.</p
<p>AMP influence on the kinetic properties of Fru-1,6-Pase. Relative (initial) velocity to AMP conce...
<p>Note: The values are expressed as means ± standard deviations of the results of three independent...
<p>Kinetic parameters of OPH mutants in the DFP hydrolysis with or without triethanolamine (TEA).</p
<p>Data represent means ± SEM of 3 separate enzyme expressions each tested in duplicate. Note that t...
<p>Kinetic parameters are provided for wild-type and variant forms of <i>Cp</i>Arap27 acting on thre...
<p>Kinetic parameters for “wild type” Tgt and mutated Tgt variants.<sup><a href="http://www.plosone....
<p>Kinetic parameters of the M36 mutant with respect to dC, gemcitabine and AraC.</p
<p>Steady state kinetic parameters for HtrA2 wild type, variants and mutants with β-casein as the su...
<p>W, wild type UGT74S1; UDP-gluc, UDP-glucose.</p><p>Kinetic parameters of wild type and mutant UGT...
<p>Kinetic parameters of LmbC, CcbC and selected CcbC mutants for various substrates.</p
a<p>Residual enzyme activity by inhibition at 3 mM ATP.</p>b<p>using NAD<sup>+</sup> or NADP<sup>+</...
<p>Steady state kinetic parameters for mutants of PMM/PGM in the conversion of glucose 1-phosphate t...
<p>Specific activities were measured in 50 mM phosphate buffer (pH 8.0) at 75°C using <i>p</i>NPC4 a...
<p>Kinetic parameters for the substrate hydrolysis by the wild-type and mutant Sfβgly.</p
<p>Comparison of the kinetic parameters for the α-KG reduction activity of the mutant IDHs.</p
<p>AMP influence on the kinetic properties of Fru-1,6-Pase. Relative (initial) velocity to AMP conce...
<p>Note: The values are expressed as means ± standard deviations of the results of three independent...
<p>Kinetic parameters of OPH mutants in the DFP hydrolysis with or without triethanolamine (TEA).</p
<p>Data represent means ± SEM of 3 separate enzyme expressions each tested in duplicate. Note that t...
<p>Kinetic parameters are provided for wild-type and variant forms of <i>Cp</i>Arap27 acting on thre...
<p>Kinetic parameters for “wild type” Tgt and mutated Tgt variants.<sup><a href="http://www.plosone....
DOI
Add to ORKG