Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Gao, L.; Imanaka, T.; Fujiwara, S.
    A mutant chaperonin that is functional at lower temperatures enables hyperthermophilic archaea to grow under cold-stress conditions (2015), J. Bacteriol., 197, 2642-2652 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
5.6.1.7 mutant enzyme E350G is expressed in Escherichia coli BL21(DE3) RIL cells and in Thermococcus kodakarensis strain DA4 Thermococcus kodakarensis

Protein Variants

EC Number Protein Variants Comment Organism
5.6.1.7 D545G the mutant shows its highest activity at 60°C, with a value equal to that of wild type isoform CpkA Thermococcus kodakarensis
5.6.1.7 D545M the optimal activity of the mutant is at 70°C, with a value equal to that of wild type isoform CpkA Thermococcus kodakarensis
5.6.1.7 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
5.6.1.7 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
5.6.1.7 P533M the mutant shows optimal activity at 70°C, with a value similar to that of wild type isoform CpkA Thermococcus kodakarensis
5.6.1.7 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
5.6.1.7 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
5.6.1.7 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

EC Number Organism UniProt Comment Textmining
5.6.1.7 Thermococcus kodakarensis
-
-
-
5.6.1.7 Thermococcus kodakarensis KU216
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
5.6.1.7 MonoQ column chromatography and Superdex 200 gel filtration Thermococcus kodakarensis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5.6.1.7 ATP + H2O + folded indole-3-glycerol-phosphate synthase
-
 Thermococcus kodakarensis ADP + phosphate + unfolded indole-3-glycerol-phosphate synthase
-
 ?
5.6.1.7 ATP + H2O + folded indole-3-glycerol-phosphate synthase
-
 Thermococcus kodakarensis KU216 ADP + phosphate + unfolded indole-3-glycerol-phosphate synthase
-
 ?

Subunits

EC Number Subunits Comment Organism
5.6.1.7 ? x * 60000, SDS-PAGE Thermococcus kodakarensis

Synonyms

EC Number Synonyms Comment Organism
5.6.1.7 chaperonin
-
 Thermococcus kodakarensis
5.6.1.7 cPKA isoform Thermococcus kodakarensis

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
5.6.1.7 60 70 isoform CpkA has its highest ATPase activity at 60-70°C Thermococcus kodakarensis