Literature summary for 5.6.1.7 extracted from

Guagliardi, A.; Cerchia, L.; Rossi, M.
Prevention of in vitro protein thermal aggregation by the Sulfolobus solfataricus chaperonin. Evidence for nonequivalent binding surfaces on the chaperonin molecule (1995), J. Biol. Chem., 270, 28126-28132.

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Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
additional information	Saccharolobus solfataricus	study on aggregation and inactivation of monomeric model proteins chicken egg white lysozyme and yeast alpha-glucosidase, and tetrameric model proteins chicken liver malic enzyme, and yeast alcohol dehydrogenase. The chaperonin has nonequivalent surfaces for the binding of the model proteins upon heating: the thermal denaturation intermediates of the single-chain proteins share surfaces I, while the thermal denaturation intermediates of the tetrameric proteins share surfaces II. ATP binding to the chaperonin induces a conformation that lacks surfaces I and carries surfaces II. Enzyme shows two mechanistically distinct strategies, one being ATP-dependent and the other ATP-independent	?	-	?

Organism

Organism	UniProt	Comment	Textmining
Saccharolobus solfataricus	-	-	-

Source Tissue

Source Tissue	Comment	Organism	Textmining

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	study on aggregation and inactivation of monomeric model proteins chicken egg white lysozyme and yeast alpha-glucosidase, and tetrameric model proteins chicken liver malic enzyme, and yeast alcohol dehydrogenase. The chaperonin has nonequivalent surfaces for the binding of the model proteins upon heating: the thermal denaturation intermediates of the single-chain proteins share surfaces I, while the thermal denaturation intermediates of the tetrameric proteins share surfaces II. ATP binding to the chaperonin induces a conformation that lacks surfaces I and carries surfaces II. Enzyme shows two mechanistically distinct strategies, one being ATP-dependent and the other ATP-independent	Saccharolobus solfataricus	?	-	?

Subunits

Subunits	Comment	Organism
More	study on aggregation and inactivation of monomeric model proteins chicken egg white lysozyme and yeast alpha-glucosidase, and tetrameric model proteins chicken liver malic enzyme, and yeast alcohol dehydrogenase. The chaperonin has nonequivalent surfaces for the binding of the model proteins upon heating: the thermal denaturation intermediates of the single-chain proteins share surfaces I, while the thermal denaturation intermediates of the tetrameric proteins share surfaces II. ATP binding to the chaperonin induces a conformation that lacks surfaces I and carries surfaces II	Saccharolobus solfataricus

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Release 2023.1 (January 2023)