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EC Number KM Value [mM] KM Value Maximum [mM] Substrate Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 3.6.4.B10-999 - more chaperonins are machines driven by cycles of ATP binding and hydrolysis, and they all show strong interring negative cooperativity, meaning that the rings are generally in alternative states. Binding cooperativity is positive when the presence of an already bound ligand enhances the binding of another to the macromolecule. Within the CCT rings, there is weak positive cooperativity which may be concerted or sequential, and this aspect of the cooperativity effect is very difficult to distinguish kinetically using Hill coefficients of ATPase kinetics 749858
Display the word mapDisplay the reaction diagram Show all sequences 3.6.4.B10-999 - more kinetic analysis, stopped-flow fluorometry and stopped-flow small-angle X-ray scattering and ATP dissociation constants of wild-type and mutant enzymes. Allosteric communication in the group II chaperonins lies only in the intra-ring contact regions, which are located entirely within the equatorial domains. No cooperativity in ATP binding 734484
Display the word mapDisplay the reaction diagram Show all sequences 3.6.4.B10-999 - more transient kinetic analysis of ATP hydrolysis by chaperonin CCT/TRiC, stopped-flow measurements. Two burst phases are observed, followed by a lag phase and then a linear steady-state phase of ATP hydrolysis. The burst phases are found to decrease with increasing ATP and K+ concentrations, thereby indicating that the apo state of CCT/TRiC is in equilibrium between several conformations and that conformational selection by ATP takes place before hydrolysis. The amplitude of the lag phase, which follows, decreases with increasing ATP concentrations, thus indicating that it reflects a transition between states with low affinity for ATP and a state with high affinity for ATP that is predominant under steady-state conditions. A kinetic model based on the data is suggested, in which CCT/TRiC is in equilibrium between a relatively large number of states that are distinguished kinetically, in agreement with its proposed sequential allosteric mechanism, overview 751330
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