Literature summary for 5.6.1.7 extracted from

Jones, H.; Preuss, M.; Wright, M.; Miller, A.D.
The mechanism of GroEL/GroES folding/refolding of protein substrates revisited (2006), Org. Biomol. Chem., 4, 1223-1235.

Search for more literature for 5.6.1.7

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	GroES-assisted refolding of unfolded zinc-cytochrome c takes place by a mechanism that is quite close to the Anfinsen Cage hypothesis for molecular chaperone activity. Even in the presence of ATP, GroEL/GroES-assisted refolding of ZnCyt c takes place at approximately half the rate of refolding of ZnCyt c alone. All forward rate enhancements or reductions could be accounted for in terms of thermodynamic coupling due to binding interactions between GroEL and unfolded protein substrates,driven by thermodynamic considerations. It is proposed that passive kinetic partitioning should be considered the core mechanism of the GroEL/GroES molecular chaperone machinery, wherein the core function is to bind unfolded protein substrates leading to a blockade of aggregation pathways and to increases in molecular flux through productive folding pathways	Escherichia coli	?	-	?

Synonyms

Synonyms	Comment	Organism
GroEL/GroES	-	Escherichia coli

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Release 2023.1 (January 2023)