Literature summary for 3.6.4.10 extracted from

Nagy, M.; Wu, H.C.; Liu, Z.; Kedzierska-Mieszkowska, S.; Zolkiewski, M.
Walker-A threonine couples nucleotide occupancy with the chaperone activity of the AAA+ ATPase ClpB (2009), Protein Sci., 18, 287-293.

Search for more literature for 3.6.4.10

Cloned(Commentary)

Cloned (Comment)	Organism
-	Escherichia coli

Protein Variants

Protein Variants	Comment	Organism
T213N	mutation in Walker A motif	Escherichia coli
T213N/T612N	mutations in Walker A motif	Escherichia coli
T612N	mutation in Walker A motif	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Escherichia coli

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg]	Specific Activity Maximum [µmol/min/mg]	Comment	Organism
additional information	-	mutation T213N or T612N produce a ca. 50% decrease in the ATPase activity, in mutant T213N/T612N the ATPase activity was approximately sevenfold lower than that of wild type ClpB, the ATPase of all ClpB variants is activated by soluble pseudosubstrates (casein and poly-lysine)	Escherichia coli

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ATP + H2O	-	Escherichia coli	ADP + phosphate	-	?

Subunits

Subunits	Comment	Organism
homohexamer	-	Escherichia coli

Synonyms

Synonyms	Comment	Organism
ATPase ClpB	-	Escherichia coli

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Release 2023.1 (January 2023)