Literature summary for 5.6.1.7 extracted from

Chapman, E.; Farr, G.W.; Fenton, W.A.; Johnson, S.M.; Horwich, A.L.
Requirement for binding multiple ATPs to convert a GroEL ring to the folding-active state (2008), Proc. Natl. Acad. Sci. USA, 105, 19205-19210.

Search for more literature for 5.6.1.7

Activating Compound

Activating Compound	Comment	Organism	Structure
additional information	binding of ADP to at least 2 subunits of a ring is regquired for GroES binding, ATP binding to at least 4 subunits is required to drive productive refolding	Escherichia coli

Protein Variants

Protein Variants	Comment	Organism
I493C	normal ATP hydrolysis in absence of inhibitor	Escherichia coli

Inhibitors

Inhibitors	Comment	Organism	Structure
N-[4-(4-amino-1-tert-butyl-1H-pyrazolo[3,4-d]pyrimidin-3-yl)phenyl]cyclopentanecarboxamide	specifically blocks ATP binding and hydrolysis	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ATP + H2O + a folded polypeptide	assay at pH 7.4, 23°C, 5 min	Escherichia coli	ADP + phosphate + an unfolded polypeptide	-	?
ATP + H2O + a folded polypeptide	rhodanese	Escherichia coli	ADP + phosphate + an unfolded polypeptide	-	?

Synonyms

Synonyms	Comment	Organism
GroEl	-	Escherichia coli

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
23	-	assay at	Escherichia coli

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
7.4	-	assay at	Escherichia coli

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Release 2023.1 (January 2023)