EC Number   |
KM Value [mM] |
KM Value Maximum [mM] |
Substrate |
Reference |
|---|
    2.7.1.1 | -999 |
- |
more |
- |
640208, 640210, 640212, 640214, 640217, 640222, 640226, 640232, 640245, 661740 |
| 2.7.1.1 | -999 |
- |
more |
kinetic parameters of hexokinase activity in wine yeast strains |
684622 |
| 2.7.1.1 | -999 |
- |
more |
kinetics of isozyme hexokinase 2 |
661772 |
| 2.7.1.1 | -999 |
- |
more |
kinetics, mass spectrometry-based assay, overview, the Mg2+ concentration influence the kinetics |
661952 |
| 2.7.1.1 | -999 |
- |
more |
non-cooperative conditions shows an ordered, ternary-complex mechanism with MgADP- as the last product to be released, hyperbolic kinetics with both 2-deoxyglucose and MgATP2- |
660949 |
| 2.7.1.1 | -999 |
- |
more |
of HXK1 mutants with modified active site |
640266 |
| 2.7.1.1 | -999 |
- |
more |
osmolytes decrease kcat/KM in the order of decreasing efficiency NaCl, urea, trimethylamine N-oxide/glycerol, betaine. For the organic osmolytes this order correlates with the degree of exclusion from protein/water interfaces |
673148 |
| 2.7.1.1 | -999 |
- |
more |
positive cooperation, mechanism, kinetic model |
663409 |
| 2.7.1.1 | -999 |
- |
more |
stopped-flow steady-state kinetics, dissociation constants of the monomer-homodimer equilibria |
662159 |
| 2.7.1.1 | -999 |
- |
more |
the osmolytes decreases kcat/KM in the order: NaCl/urea/trimethylamine-N-oxide dehydrate/glycerol/betaine. For the organic osmolytes this order correlates with the degree of exclusion from protein-water interfaces. Thus, the stronger the exclusion the weaker the perturbing effects on kcat/KM |
673148 |
