EC Number   |
KM Value [mM] |
KM Value Maximum [mM] |
Substrate |
Reference |
|---|
    1.1.5.2 | -999 |
- |
more |
detailed kinetic analysis of wild-type and mutant enzymes, substrate inhibition and cooperativity effects, overview |
725196 |
| 1.1.5.2 | -999 |
- |
more |
electrochemical data and kinetics for quinone derivatives as redocx mediators |
654936 |
| 1.1.5.2 | -999 |
- |
more |
kinetic study, enzyme follows Michaelis-Menten kinetics using artificial electron transfer mediator system based on ruthenium(III) compounds for activity assays |
654780 |
| 1.1.5.2 | -999 |
- |
more |
kinetics |
655097 |
| 1.1.5.2 | -999 |
- |
more |
kinetics, cooperativity in the recombinant chimeric mutant enzyme which possesses only 1 active subunit derived from the wild-type enzyme |
655929 |
| 1.1.5.2 | -999 |
- |
more |
metal binding kinetics, wild-type and mutant enzymes, Km for the different substrates of mutant enzymes with different metal ions bound, overview |
654865 |
| 1.1.5.2 | -999 |
- |
more |
predicted binding energy of wild-type and mutant enzymes |
655127 |
| 1.1.5.2 | 0.000004 |
- |
2-deoxy-D-glucose |
pH 7.5, 70°C, wild-type enzyme |
746918 |
| 1.1.5.2 | 0.00002 |
- |
D-glucosamine |
pH 7.5, 70°C, mutant enzyme Y156A |
746918 |
| 1.1.5.2 | 0.00002 |
- |
D-glucosamine |
pH 7.5, 70°C, mutant enzyme Y156K |
746918 |
