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Literature summary for 3.6.4.B10 extracted from

  • Okochi, M.; Matsuzaki, H.; Nomura, T.; Ishii, N.; Yohda, M.
    Molecular characterization of the group II chaperonin from the hyperthermophilic archaeum Pyrococcus horikoshii OT3 (2004), Extremophiles, 9, 127-134.
    View publication on PubMed
Search for more literature for 3.6.4.B10

Activating Compound

Activating Compound Comment Organism Structure
prefoldin the enzyme is not effective in the refolding of isopropylmalate dehydrogenase, the refolding efficiency is enhanced by the cooperation of the enzyme with Pyrococcus prefoldin Pyrococcus horikoshii

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Pyrococcus horikoshii

Organism

Organism UniProt Comment Textmining
Pyrococcus horikoshii O57762
-
-
Pyrococcus horikoshii OT-3 O57762
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Pyrococcus horikoshii

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O the enzyme exists as a homooligomer in a double-ring structure, which captures non-native proteins in a central cavity to promote correct folding in an ATP-dependent manner. It protects the citrate synthase of a porcine heart from thermal aggregation at 45°C, and does the same on the isopropylmalate dehydrogenase of Thermus thermophilus HB8, at 90°C. It enhances the refolding of green fluorescent protein, which has been unfolded by low pH, in an ATP-dependent manner. It is not effective in the refolding of isopropylmalate dehydrogenase, the refolding efficiency is enhanced by the cooperation of the enzyme with Pyrococcus prefoldin Pyrococcus horikoshii ADP + phosphate
-
 ?
ATP + H2O the enzyme exists as a homooligomer in a double-ring structure, which captures non-native proteins in a central cavity to promote correct folding in an ATP-dependent manner. It protects the citrate synthase of a porcine heart from thermal aggregation at 45°C, and does the same on the isopropylmalate dehydrogenase of Thermus thermophilus HB8, at 90°C. It enhances the refolding of green fluorescent protein, which has been unfolded by low pH, in an ATP-dependent manner. It is not effective in the refolding of isopropylmalate dehydrogenase, the refolding efficiency is enhanced by the cooperation of the enzyme with Pyrococcus prefoldin Pyrococcus horikoshii OT-3 ADP + phosphate
-
 ?

Subunits

Subunits Comment Organism
hexadecamer homooligomer, double-ring structure Pyrococcus horikoshii

Synonyms

Synonyms Comment Organism
group II chaperonin Pyrococcus species contain only one chaperonin gene per whole genome Pyrococcus horikoshii
PhCPN
-
 Pyrococcus horikoshii
PhCPN Pyrococcus species contain only one chaperonin gene per whole genome Pyrococcus horikoshii

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
90
-
-
 Pyrococcus horikoshii

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
70 95 70°C: about 70% of maximal activity, 95°C: about 50% of maximal activity Pyrococcus horikoshii