Literature summary for 3.4.21.53 extracted from

Thomas, J.; Fishovitz, J.; Lee, I.
Utilization of positional isotope exchange experiments to evaluate reversibility of ATP hydrolysis catalyzed by Escherichia coli Lon protease (2010), Biochem. Cell Biol., 88, 119-128.

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Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	Lon possesses an intrinsic ATPase activity that is stimulated by protein and certain peptide substrates. The ATPase reaction catalyzed by Lon in the presence and absence of peptide substrate that stimulates the enzyme's ATPase activity is irreversible. The half-site ATPase reactivity of Lon can be used to account for the kinetic mechanism of the ATP-dependent peptidase activity of the enzyme	Escherichia coli	?	-	?

General Information

General Information	Comment	Organism
physiological function	Lon possesses an intrinsic ATPase activity that is stimulated by protein and certain peptide substrates. The ATPase reaction catalyzed by Lon in the presence and absence of peptide substrate that stimulates the enzyme's ATPase activity is irreversible	Escherichia coli

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Release 2023.1 (January 2023)