EC Number   |
Turnover Number Minimum [1/s] |
Turnover Number Maximum [1/s] |
Substrate |
Reference |
|---|
    2.7.1.1 | -999 |
- |
more |
- |
662159, 676293 |
| 2.7.1.1 | -999 |
- |
more |
6000/min, wild-type and nonaggregating interface mutant hexokinase I |
640258 |
| 2.7.1.1 | -999 |
- |
more |
as the temperature is raised from 30°C to 47.5°C kcat decreases, falling to about 10 per sec (by 80%) at 50°C |
674421 |
| 2.7.1.1 | -999 |
- |
more |
kinetic parameters of hexokinase activity in wine yeast strains |
684622 |
| 2.7.1.1 | -999 |
- |
more |
natural hexokinase: 68160/min, recombinant hexokinase expressed in Escherichia coli XL-1 Blue: 18913/min, at pH 7.5 |
640265 |
| 2.7.1.1 | -999 |
- |
more |
osmolytes decrease kcat/KM in the order ofedecreasing efficiency NaCl, urea, trimethylamine N-oxide/glycerol, betains. For the organic osmolytes this order correlates with the degree of exclusion from protein/water interfaces |
673148 |
| 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 |
| 2.7.1.1 | 0.00091 |
- |
D-glucose |
mutant enzyme D205A, kcat less than 0.00091 s-1 |
702320 |
| 2.7.1.1 | 0.007 |
- |
D-glucose |
mutant T228M, 37°C, pH not specified in the puclication |
722237 |
| 2.7.1.1 | 0.02 |
- |
D-fructose |
pH 7.5, temperature not specified in the publication |
739618 |
