Cloned (Comment) | Organism |
---|---|
mutant enzyme E350G is expressed in Escherichia coli BL21(DE3) RIL cells and in Thermococcus kodakarensis strain DA4 | Thermococcus kodakarensis |
Protein Variants | Comment | Organism |
---|---|---|
D545G | the mutant shows its highest activity at 60°C, with a value equal to that of wild type isoform CpkA | Thermococcus kodakarensis |
D545M | the optimal activity of the mutant is at 70°C, with a value equal to that of wild type isoform CpkA | Thermococcus kodakarensis |
E530G | the mutant of isoform CpkA shows increased ATPase and protein refolding activities, with its highest activity at 50°C. The mutation prevents cold denaturation of proteins under cold stress conditions, thereby enabling cells to grow in cooler environments | Thermococcus kodakarensis |
E530M | the mutant enzyme shows the most activity at 70°C, although the value is almost half that of wild type enzyme isoform CpkA. The ATPase activity of the mutant at 50°C is a little lower than that of the wild type enzyme | Thermococcus kodakarensis |
P533M | the mutant shows optimal activity at 70°C, with a value similar to that of wild type isoform CpkA | Thermococcus kodakarensis |
P538G | the mutant shows a temperature-dependent profile similar to that of wild type isoform CpkA, although its ATPase activity is almost 2fold lower | Thermococcus kodakarensis |
Q533G | the mutant enzyme shows the most activity at 50°C, although the value is similar to that of the wild type enzyme isoform CpkA. The ATPase activity of the mutant at 50°C is a little lower than that of the wild type enzyme | Thermococcus kodakarensis |
Q533M | the optimum activity of the enzyme is displayed at 80°C and is 4fold higher than that of wild type isoform CpkA at this temperature | Thermococcus kodakarensis |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Thermococcus kodakarensis | - |
- |
- |
Thermococcus kodakarensis KU216 | - |
- |
- |
Purification (Comment) | Organism |
---|---|
MonoQ column chromatography and Superdex 200 gel filtration | Thermococcus kodakarensis |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + H2O + folded indole-3-glycerol-phosphate synthase | - |
Thermococcus kodakarensis | ADP + phosphate + unfolded indole-3-glycerol-phosphate synthase | - |
? | |
ATP + H2O + folded indole-3-glycerol-phosphate synthase | - |
Thermococcus kodakarensis KU216 | ADP + phosphate + unfolded indole-3-glycerol-phosphate synthase | - |
? |
Subunits | Comment | Organism |
---|---|---|
? | x * 60000, SDS-PAGE | Thermococcus kodakarensis |
Synonyms | Comment | Organism |
---|---|---|
chaperonin | - |
Thermococcus kodakarensis |
cPKA | isoform | Thermococcus kodakarensis |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
60 | 70 | isoform CpkA has its highest ATPase activity at 60-70°C | Thermococcus kodakarensis |