Cloned (Comment) | Organism |
---|---|
expression in Escherichia coli | Halobacterium salinarum |
Protein Variants | Comment | Organism |
---|---|---|
G114D | inactive mutant enzyme, dissociates more than wild-type enzyme in low salt buffer | Halobacterium salinarum |
G114K | active mutant enzyme, refolds in 1M NaCl after heat-denaturation, under which the wild-type enzyme and mutant enzyme G114S proteins show no refolding | Halobacterium salinarum |
G114R | once folded, the mutant enzyme is stable even in low salt buffer | Halobacterium salinarum |
G114S | active mutant enzyme, dissociates as extensively as the wild-type enzyme as low salt buffer | Halobacterium salinarum |
General Stability | Organism |
---|---|
mutants with a basic amino acid at residue 114 (G114K, G114R) are resistant against heat inactivation as well as against low salt dissociation | Halobacterium salinarum |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Halobacterium salinarum | P61136 | - |
- |
Halobacterium salinarum JCM 11081 | P61136 | - |
- |
Purification (Comment) | Organism |
---|---|
- |
Halobacterium salinarum |
Subunits | Comment | Organism |
---|---|---|
dimer | G114S mutant behaves similarly to wild-type enzyme, dissociating a dimer | Halobacterium salinarum |
hexamer | G114K mutant has a hexameric structure under low salt concentration of non-denaturing PAGE condition | Halobacterium salinarum |
More | a basic amino acid at residue 114 is responsible for the stabilization of subunit assembly | Halobacterium salinarum |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
additional information | - |
mutants with a basic amino acid at residue 114 (G114K, G114R) are resistant against heat inactivation as well as against low salt dissociation | Halobacterium salinarum |
30 | - |
G114S mutant is stable up to 30°C | Halobacterium salinarum |