Protein Variants | Comment | Organism |
---|---|---|
A109C | the mutant is defective in ring separation and exchange | Escherichia coli |
A109S | the mutant shows mixed-ring formation like the wild type enzyme | Escherichia coli |
D155A | the mutant preserves negative inter-ring cooperativity and forms mixed-ring complexes in the presence of cofactor GroES/ATP with an efficiency similar to the wild type enzyme | Escherichia coli |
D155A/R197A | the double mutant preserves negative inter-ring cooperativity and forms mixed-ring complexes in the presence of cofactor GroES/ATP with an efficiency similar to the wild type enzyme | Escherichia coli |
D398A | the mutant enzyme binds ATP but hydrolyzes it at a very slow rate of less than 2% of the wild type enzyme | Escherichia coli |
D87K | the mutant enzyme does not bind nucleotide | Escherichia coli |
E461K | the mutant enzyme shows no mixed-ring formation | Escherichia coli |
Y203E/G337S/I349E | the mutant enzyme is ATPase active but unable to bind substrate protein and the cofactor GroES | Escherichia coli |
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 | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | P0A6F5 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + H2O + a folded polypeptide | - |
Escherichia coli | ADP + phosphate + an unfolded polypeptide | - |
? |
Subunits | Comment | Organism |
---|---|---|
tetradecamer | 14 * 57000, SDS-PAGE | Escherichia coli |
Synonyms | Comment | Organism |
---|---|---|
chaperonin | - |
Escherichia coli |
GroEl | - |
Escherichia coli |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
GroES | - |
Escherichia coli |