Literature summary for 5.6.1.7 extracted from

Viitanen, P.V.; Lubben, T.H.; Reed, J.; Goloubinoff, P.; O'Keefe, D.P.; Lorimer, G.H.
Chaperonin-facilitated refolding of ribulosebisphosphate carboxylase and ATP hydrolysis by chaperonin 60 (groel) are K+ dependent (1990), Biochemistry, 29, 5665-5671.

Search for more literature for 5.6.1.7

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
0.007	-	ATP	50 mM K+	Escherichia coli

Metals/Ions

Metals/Ions	Comment	Organism	Structure
K+	1 mM, 100fold activation in the absence of Cpn10, half-maximal rate at 0.080 mM K+	Escherichia coli
Rb+	-	Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
ATP + H2O + a folded polypeptide	Escherichia coli	-	ADP + phosphate + an unfolded polypeptide	-	?

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	-	Escherichia coli	ADP + phosphate + an unfolded polypeptide	-	?

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
0.1	-	ATP	based on protomers, 1 mM K+	Escherichia coli

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Release 2023.1 (January 2023)