EC Number   |
KM Value [mM] |
KM Value Maximum [mM] |
Substrate |
Reference |
|---|
   5.6.1.7 | -999 |
- |
more |
cooperative effect in ATP hydrolysis, Hill coefficient is estimated at 3.56 |
654810 |
| 5.6.1.7 | -999 |
- |
more |
cooperativity in GroEL, an allosteric enzyme complex, kinetic analysis, overview. Structural basis of negative cooperativity between rings. GroES is an allosteric effector of ATP hydrolysis |
734473 |
| 5.6.1.7 | -999 |
- |
more |
GroEL:GroES stoichiometry calculation. The GroEL/ES system is allosterically regulated with positive cooperativity of ATP binding and hydrolysis within rings and negative cooperativity between rings |
734487 |
| 5.6.1.7 | -999 |
- |
more |
kinetic model for allosteric transitions in GroEL and substrate protein folding and aggregation |
699525 |
| 5.6.1.7 | -999 |
- |
more |
positive intraring cooperativity of ATP is suggested |
655574 |
| 5.6.1.7 | 0.007 |
- |
ATP |
50 mM K+ |
289236 |
| 5.6.1.7 | 0.015 |
- |
ATP |
wild type enzyme, with rhamnose dehydrogenase as protein substrate, at pH 7.5 and 55°C |
750509 |
| 5.6.1.7 | 0.082 |
- |
ATP |
mutant enzyme D94A, with rhamnose dehydrogenase as protein substrate, at pH 7.5 and 55°C |
750509 |
| 5.6.1.7 | 0.1 |
- |
ATP |
- |
289227 |
| 5.6.1.7 | 0.115 |
- |
ATP |
- |
289225 |
