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Literature summary for 5.6.1.7 extracted from
- Dissecting a bimolecular process of MgATP2- binding to the chaperonin GroEL (2011), J. Mol. Biol., 410, 343-356.
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| Y485W | mutant is used in this study to monitor the MgATP2-binding process to unliganded apo GroEL in the absence of K+ at pH 7.5 and 5.1°C. Under these conditions ATP exists mostly as MgATP2- and [MgATP2-] | Escherichia coli |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| K+ | essential for hydrolysis of ATP, ATPase activity is barely retained in the absence of K+ | Escherichia coli |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + H2O + a folded polypeptide | the equilibrium and kinetics of MgATP2- binding to GroEL mutant Y485W is studied via isothermal titration calorimetry (ITC) and stopped-flow fluorescence spectroscopy. Comparison of the kinetics in the absence and presence of K+ clearly demonstrate that the first fluorescence-increasing phase corresponds to bimolecular MgATP2- binding to GroEL | Escherichia coli | ADP + phosphate + an unfolded polypeptide | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| GroEl | - |
Escherichia coli |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 5 | - |
assay at | Escherichia coli |
| 25 | - |
assay at | Escherichia coli |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.5 | - |
assay at | Escherichia coli |
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Release 2023.1 (January 2023)
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