EC Number   |
KM Value [mM] |
KM Value Maximum [mM] |
Substrate |
Reference |
|---|
    2.7.7.27 | -999 |
- |
more |
- |
643155 |
| 2.7.7.27 | -999 |
- |
more |
comparison of Km of alpha-D-glucose 1-phosphate at different ATP concentrations, at two levels of 3-phosphoglycerate and in aqueous or by polyethylenglycol crowded medium, comparison of Km of ATP at different alpha-D-glucose 1-phosphate concentrations, at two levels of 3-phosphoglycerate and in aqueous or by polyethylenglycol crowded medium |
643159 |
| 2.7.7.27 | -999 |
- |
more |
comparison of Km of proteolyzed and non-proteolyzed enzyme at pH 7.4 and pH 6.8 |
643120 |
| 2.7.7.27 | -999 |
- |
more |
effect of activators on substrate kinetic parameters of bacterial enzymes |
643144 |
| 2.7.7.27 | -999 |
- |
more |
kinetic parameters |
643135, 643148 |
| 2.7.7.27 | -999 |
- |
more |
kinetic study |
643116, 643120, 643135, 643136, 643144 |
| 2.7.7.27 | -999 |
- |
more |
kinetics of wild-type and mutant large subunits, overview |
693217 |
| 2.7.7.27 | -999 |
- |
more |
kinetics wild-type and mutant enzymes, photoaffinity labeling of the AGPase heterotetramers, overview |
676387 |
| 2.7.7.27 | -999 |
- |
more |
KM-values for mosaic AGPases derived from protein motifs normally expressed in the Zea mays endosperm and the Solanum tuberosum tuber |
663141 |
| 2.7.7.27 | -999 |
- |
more |
ordered kinetic mechanism, regulation of AGPase by effectors, detailed overview |
694714 |
