EC Number   |
KM Value [mM] |
KM Value Maximum [mM] |
Substrate |
Reference |
|---|
   1.1.3.4 | -999 |
- |
more |
- |
389828, 655711 |
| 1.1.3.4 | -999 |
- |
more |
choline, glucose, myo-inositol, methanol, ethanol, 1-pentanol, benzyl alcohol, 2-phenylethanol, cholesterol or lauryl alcohol tested as potential substrates, recombinant protein devoid of either oxidase or dehydrogenase activity |
684268 |
| 1.1.3.4 | -999 |
- |
more |
enzyme thermodynamics and kinetics |
743775 |
| 1.1.3.4 | -999 |
- |
more |
kinetic limitations of a bioelectrochemical electrode using carbon nanotube-attached glucose oxidase for biofuel cells. Carbon nanotube-supported glucose oxidase is examined in the presence of 1,4-benzoquinone. The intrinsic Michaelis parameters of the reaction catalyzed by carbon nanotube-glucose-oxidase are very close to those of native enzyme. However, the Nafion entrapment of carbon nanotube-glucose-oxidase for an electrode results in a much lower activity due to the limited availability of the embedded enzyme. Kinetic studies reveal that the biofuel cell employing such an enzyme electrode only generate a power density equivalent to less than 40% of the reaction capability of the enzyme on electrode. Factors such as electron and proton transfer resistances can be more overwhelming than the heterogeneous reaction kinetics in limiting the power generation of such biofuel cells |
747341 |
| 1.1.3.4 | -999 |
- |
more |
kinetics |
671400 |
| 1.1.3.4 | -999 |
- |
more |
kinetics of enzyme-pentacyanoferrate(III)-nucleophilic ligands-complex interactions, detailed overview |
672508 |
| 1.1.3.4 | -999 |
- |
more |
KM-value of immunoaffinity-layered glucose oxidase preparations remains unaltered |
655079 |
| 1.1.3.4 | -999 |
- |
more |
Michaelis-Menten kinetics |
725789, 741479, 742129, 743744 |
| 1.1.3.4 | -999 |
- |
more |
Michaelis-Menten kinetics of immobilized enzyme GOx and free enzyme GOx |
743105 |
| 1.1.3.4 | -999 |
- |
more |
Michaelis-Menten kinetics, overview |
723947 |
