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Literature summary extracted from
- A mutant chaperonin that is functional at lower temperatures enables hyperthermophilic Archaea to grow under cold-stress conditions (2015), J. Bacteriol., 197, 2642-2652.
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 3.6.4.B10 | recombinant expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3) RIL | Thermococcus kodakarensis |
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 3.6.4.B10 | D545G | site-directed mutagenesis, the mutant shows a stabilities similar to the wild-type CpkA | Thermococcus kodakarensis |
| 3.6.4.B10 | D545M | site-directed mutagenesis, the mutant shows slightly higher stabilities than that of wild-type CpkA | Thermococcus kodakarensis |
| 3.6.4.B10 | E530G | site-directed mutagenesis, the mutant strain DA4 shows increased ATPase activity. The CpkA-E530G mutation prevents cold denaturation of proteins under cold-stress conditions, thereby enabling cells to grow in cooler environments | Thermococcus kodakarensis |
| 3.6.4.B10 | E530M | site-directed mutagenesis, the mutant shows a stabilities similar to the wild-type CpkA | Thermococcus kodakarensis |
| 3.6.4.B10 | P538G | site-directed mutagenesis, the mutant shows slightly higher stabilities than that of wild-type CpkA | Thermococcus kodakarensis |
| 3.6.4.B10 | P538M | site-directed mutagenesis, the mutant shows a stabilities similar to the wild-type CpkA | Thermococcus kodakarensis |
| 3.6.4.B10 | Q533G | site-directed mutagenesis | Thermococcus kodakarensis |
| 3.6.4.B10 | Q533M | site-directed mutagenesis, the mutant shows a stabilities similar to the wild-type CpkA | Thermococcus kodakarensis |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.6.4.B10 | Mg2+ | required | Thermococcus kodakarensis |  |
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 3.6.4.B10 | 60000 | - |
x * 60000, about, SDS-PAGE | Thermococcus kodakarensis |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.6.4.B10 | ATP + H2O | Thermococcus kodakarensis | - |
ADP + phosphate | - |
? | |
| 3.6.4.B10 | ATP + H2O | Thermococcus kodakarensis KU216 | - |
ADP + phosphate | - |
? | |
| 3.6.4.B10 | additional information | Thermococcus kodakarensis | denatured indole-3-glycerol-phosphate synthase of Thermococcus kodakarensis is a CpkA target in vitro, mutant CpkA-E530G is more effective than wild-type enzyme CpkA at facilitating the refolding of chemically unfolded substrate | ? | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.6.4.B10 | Thermococcus kodakarensis | P61111 | gene CPKA | - |
| 3.6.4.B10 | Thermococcus kodakarensis | Q52500 | gene CPKB | - |
| 3.6.4.B10 | Thermococcus kodakarensis KU216 | Q52500 | gene CPKB | - |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 3.6.4.B10 | recombinant wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) RIL by heat treatment at 85°C for 30 min, anion exchange chromatography, and gel filtration | Thermococcus kodakarensis |
Source Tissue
| EC Number | Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|---|
| 3.6.4.B10 | additional information | Thermococcus kodakarensis grows optimally at 85°C, the mutant strain DA4 (pyrF cpkA-E530G) grows as well as the parental KU216 (pyrF) strain at 60°C, clear correlation between the CpkA-type chaperonin gene copy number and growth temperature | Thermococcus kodakarensis | - |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.6.4.B10 | ATP + H2O | - |
Thermococcus kodakarensis | ADP + phosphate | - |
? | |
| 3.6.4.B10 | ATP + H2O | - |
Thermococcus kodakarensis KU216 | ADP + phosphate | - |
? | |
| 3.6.4.B10 | additional information | denatured indole-3-glycerol-phosphate synthase of Thermococcus kodakarensis is a CpkA target in vitro, mutant CpkA-E530G is more effective than wild-type enzyme CpkA at facilitating the refolding of chemically unfolded substrate | Thermococcus kodakarensis | ? | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 3.6.4.B10 | ? | x * 60000, about, SDS-PAGE | Thermococcus kodakarensis |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.6.4.B10 | cPKA | - |
Thermococcus kodakarensis |
| 3.6.4.B10 | CpkB | - |
Thermococcus kodakarensis |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.6.4.B10 | 50 | - |
mutants Q533G and E530G | Thermococcus kodakarensis |
| 3.6.4.B10 | 60 | - |
mutant D545G | Thermococcus kodakarensis |
| 3.6.4.B10 | 60 | 70 | wild-type enzyme and mutant P538G | Thermococcus kodakarensis |
| 3.6.4.B10 | 70 | - |
mutants P533M, D545M, and E530M | Thermococcus kodakarensis |
| 3.6.4.B10 | 80 | - |
mutant Q533M | Thermococcus kodakarensis |
Temperature Range [°C]
| EC Number | Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.6.4.B10 | 30 | 90 | activity range of wild-type and mutant enzymes, profiles overview | Thermococcus kodakarensis |
Temperature Stability [°C]
| EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.6.4.B10 | additional information | - |
thermal unfolding plots for recombinant wild-type and mutant enzymes. The thermal unfolding plots for mutants E530M, Q533M, P538M, and D545G are very similar to that for wild-type CpkA. CpkA mutants E530G and Q533M show slightly lower thermal stabilities, while CpkA mutants P538G and D545M show slightly higher stabilities than that of wild-type CpkA | Thermococcus kodakarensis |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.6.4.B10 | 7.5 | - |
assay at | Thermococcus kodakarensis |
Expression
| EC Number | Organism | Comment | Expression |
|---|---|---|---|
| 3.6.4.B10 | Thermococcus kodakarensis | possesses two chaperonins, cold-inducible CpkA and heat-inducible CpkB, which are involved in adaptation to low and high temperatures, respectively | up |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 3.6.4.B10 | malfunction | introduction of single mutations into the CpkA C-terminal region show that a single base substitution E530G allows the organism to adapt to a lower temperature | Thermococcus kodakarensis |
| 3.6.4.B10 | additional information | possesses two chaperonins, cold-inducible CpkA and heat-inducible CpkB, which are involved in adaptation to low and high temperatures, respectively | Thermococcus kodakarensis |
| 3.6.4.B10 | additional information | possesses two chaperonins, cold-inducible CpkA and heat-inducible CpkB, which are involved in adaptation to low and high temperatures, respectively. Clear correlation between the CpkA-type chaperonin gene copy number and growth temperature | Thermococcus kodakarensis |
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Release 2023.1 (January 2023)
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