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Literature summary 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

Activating Compound

EC Number Activating Compound Comment Organism Structure
3.6.4.B10 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)

EC Number Cloned (Comment) Organism
3.6.4.B10 expression in Escherichia coli Pyrococcus horikoshii

Organism

EC Number Organism UniProt Comment Textmining
3.6.4.B10 Pyrococcus horikoshii O57762
-
-
3.6.4.B10 Pyrococcus horikoshii OT-3 O57762
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.6.4.B10
-
 Pyrococcus horikoshii

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.6.4.B10 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
-
 ?
3.6.4.B10 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

EC Number Subunits Comment Organism
3.6.4.B10 hexadecamer homooligomer, double-ring structure Pyrococcus horikoshii

Synonyms

EC Number Synonyms Comment Organism
3.6.4.B10 group II chaperonin Pyrococcus species contain only one chaperonin gene per whole genome Pyrococcus horikoshii
3.6.4.B10 PhCPN
-
 Pyrococcus horikoshii
3.6.4.B10 PhCPN Pyrococcus species contain only one chaperonin gene per whole genome Pyrococcus horikoshii

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.6.4.B10 90
-
-
 Pyrococcus horikoshii

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
3.6.4.B10 70 95 70°C: about 70% of maximal activity, 95°C: about 50% of maximal activity Pyrococcus horikoshii