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Literature summary for 5.6.1.7 extracted from

  • An, Y.J.; Rowland, S.E.; Na, J.H.; Spigolon, D.; Hong, S.K.; Yoon, Y.J.; Lee, J.H.; Robb, F.T.; Cha, S.S.
    Structural and mechanistic characterization of an archaeal-like chaperonin from a thermophilic bacterium (2017), Nat. Commun., 8, 827 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 5.6.1.7

Protein Variants

Protein Variants Comment Organism
D373A the thermostability of the mutant is compromised as it retains 4.7% of the basal ATPase activity of the wild type enzyme after 1 h incubation at 65°C Carboxydothermus hydrogenoformans
L439A the thermostability of the mutant is compromised as it retains about 20% of the basal ATPase activity of the wild type enzyme after 1 h incubation at 65°C Carboxydothermus hydrogenoformans
R155E the mutant has severely diminished activity compared to the wild type enzyme Carboxydothermus hydrogenoformans
R155K the mutant enzyme has about wild type activity Carboxydothermus hydrogenoformans
R155L the mutant has severely diminished activity compared to the wild type enzyme Carboxydothermus hydrogenoformans

Organism

Organism UniProt Comment Textmining
Carboxydothermus hydrogenoformans
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O + folded malate dehydrogenase
-
 Carboxydothermus hydrogenoformans ADP + phosphate + unfolded malate dehydrogenase
-
 ?

Synonyms

Synonyms Comment Organism
chaperonin
-
 Carboxydothermus hydrogenoformans
CPN
-
 Carboxydothermus hydrogenoformans

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
65
-
-
 Carboxydothermus hydrogenoformans