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Literature summary for 5.6.1.7 extracted from
- Asp-52 in combination with Asp-398 plays a critical role in ATP hydrolysis of chaperonin GroEL (2014), J. Biol. Chem., 289, 30005-30011.
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| D398A | site-directed mutagenesis, the mutant shows reduced ATPase activity compared to the wild-type enzyme | Escherichia coli |
| D52A | site-directed mutagenesis, ATPase activity of the mutant is 80% reduced compared to the wild-type GroEL | Escherichia coli |
| D52A/D398A | site-directed mutagenesis, the mutant forms a stable symmetric GroEL-GroES complex with a half-life of 150 h, but has no ATPase activity | Escherichia coli |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Mg2+ | required | Escherichia coli |  |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + H2O + a folded polypeptide | Escherichia coli | - |
ADP + phosphate + an unfolded polypeptide | - |
? | |
| additional information | Escherichia coli | malate dehydrogenase and rhodanase are substrate proteins for GroEl refolding | ? | - |
? | |
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 | - |
Escherichia coli | ADP + phosphate + an unfolded polypeptide | - |
? | |
| additional information | malate dehydrogenase and rhodanase are substrate proteins for GroEl refolding | Escherichia coli | ? | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| chaperonin GroEL | - |
Escherichia coli |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 25 | - |
refolding and ATPase assay at | Escherichia coli |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.4 | - |
refolding and ATPase assay at | Escherichia coli |
General Information
| General Information | Comment | Organism |
|---|---|---|
| additional information | enzyme residues Asp398 and Asp52 play a critical role for ATP hydrolysis of GroEL | Escherichia coli |
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