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Literature summary for 3.6.4.B10 extracted from
- Transient kinetic analysis of ATP hydrolysis by the CCT/TRiC chaperonin (2016), J. Mol. Biol., 428, 4520-4527 .
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| G345D | site-directed mutagenesis in subunit CCT4 decreases cooperativity in ATP binding compared to wild-type | Saccharomyces cerevisiae |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | 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 | Saccharomyces cerevisiae |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Mg2+ | required | Saccharomyces cerevisiae |  |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + H2O | Saccharomyces cerevisiae | - |
ADP + phosphate | - |
? | |
| ATP + H2O | Saccharomyces cerevisiae ATCC 204508 | - |
ADP + phosphate | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Saccharomyces cerevisiae | P12612 AND P39076 AND P39077 AND P39078 AND P40413 AND P39079 AND P42943 AND P47079 | genes CCT1-8 encoding subunits CCT-alpha, CCT-beta, CCT-gamma, CCT-delta, CCT-epsilon, CCT-zeta, CCT-eta, and CCT-theta | - |
| Saccharomyces cerevisiae ATCC 204508 | P12612 AND P39076 AND P39077 AND P39078 AND P40413 AND P39079 AND P42943 AND P47079 | genes CCT1-8 encoding subunits CCT-alpha, CCT-beta, CCT-gamma, CCT-delta, CCT-epsilon, CCT-zeta, CCT-eta, and CCT-theta | - |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| native enzyme by calmodulin affinity chromatography and gel filtration | Saccharomyces cerevisiae |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + H2O | - |
Saccharomyces cerevisiae | ADP + phosphate | - |
? | |
| ATP + H2O | - |
Saccharomyces cerevisiae ATCC 204508 | ADP + phosphate | - |
? | |
| additional information | CCT/TRiC is mixed rapidly with different concentrations of ATP, and the amount of phosphate formed upon ATP hydrolysis is measured as a function of time using the coumarin-labeled phosphate-binding protein method. Two burst phases are observed, followed by a lag phase and then a linear steady-state phase of ATP hydrolysis | Saccharomyces cerevisiae | ? | - |
- |
|
| additional information | CCT/TRiC is mixed rapidly with different concentrations of ATP, and the amount of phosphate formed upon ATP hydrolysis is measured as a function of time using the coumarin-labeled phosphate-binding protein method. Two burst phases are observed, followed by a lag phase and then a linear steady-state phase of ATP hydrolysis | Saccharomyces cerevisiae ATCC 204508 | ? | - |
- |
|
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| CCT | - |
Saccharomyces cerevisiae |
| CCT/TRiC chaperonin | - |
Saccharomyces cerevisiae |
| chaperonin-containing t-complex polypeptide 1 | - |
Saccharomyces cerevisiae |
| TCP-1 | - |
Saccharomyces cerevisiae |
| TriC | - |
Saccharomyces cerevisiae |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 25 | - |
assay at | Saccharomyces cerevisiae |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.5 | - |
assay at | Saccharomyces cerevisiae |
General Information
| General Information | Comment | Organism |
|---|---|---|
| additional information | determination of kinetic intermediates in the sequential allosteric pathway of CCT/TRiC, kinetic mechanism and model, overview | Saccharomyces cerevisiae |
| physiological function | the chaperonin-containing t-complex polypeptide 1 (CCT or TRiC) assists protein folding in an ATP-dependent manner. CCT/TRiC has been found to mediate the folding of beta-actin, alpha- and beta-tubulin, and several hundred other proteins in addition to several clinically important proteins such as p53 and the oncoprotein AML1-ETO | Saccharomyces cerevisiae |
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Release 2023.1 (January 2023)
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