Literature summary for 3.4.24.B17 extracted from

Yang, Y.; Gunasekara, M.; Muhammednazaar, S.; Li, Z.; Hong, H.
Proteolysis mediated by the membrane-integrated ATP-dependent protease FtsH has a unique nonlinear dependence on ATP hydrolysis rates (2019), Protein Sci., 28, 1262-1275 .

Search for more literature for 3.4.24.B17

Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P0AAI3	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
protein GlpG + H2O	helical bundle membrane protein, model membrane substrate	Escherichia coli	?	-	?

General Information

General Information	Comment	Organism
physiological function	dependence of degradation rates on ATP hydrolysis rates is highly nonlinear. At least, about 20 ATP hydrolysis events need to be accumulated per minute for degradation to occur, but once exceeding the threshold, FtsH tightly couples ATP hydrolysis to degradation in a highly cooperative manner (Hill coefficinet for ATP is 4-5). The degradation rates steeply increase and saturate at the ATP hydrolysis rates far below the maxima. During the steep increase, FtsH efficiently utilizes ATP hydrolysis for degradation, consuming only 40-60% of the total ATP cost measured at the maximal ATP hydrolysis rates	Escherichia coli

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Release 2023.1 (January 2023)