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Literature summary for 5.6.1.7 extracted from
- ATP-triggered ADP release from the asymmetric chaperonin GroEL/GroES/ADP7 is not the rate-limiting step of the GroEL/GroES reaction cycle (2010), FEBS Lett., 584, 951-953.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
- |
Escherichia coli |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| D398A | to measure the rate of ADP release from an asymmetric GroEL/GroES/ADP7 complex, D398A mutant is employed. The mutant hydrolyzes ATP at a rate 2% that of wild-type GroEL, and thus effectively allows study of a single turnover of the reaction | Escherichia coli |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Escherichia coli |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + H2O + a folded polypeptide | the GroEL/GroES protein folding chamber is formed and dissociated by ATP binding and hydrolysis. ATP hydrolysis in the GroES-bound (cis) ring gates entry of ATP into the opposite unoccupied trans ring, which allosterically ejects cis ligands. ADP release from the cis ring is not the rate-limiting step of the GroEL/GroES reaction cycle | Escherichia coli | ADP + phosphate + an unfolded polypeptide | - |
? |  |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| GroEl | - |
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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