Literature summary for 4.1.1.18 extracted from

Snider, J.; Gutsche, I.; Lin, M.; Baby, S.; Cox, B.; Butland, G.; Greenblatt, J.; Emili, A.; Houry, W.A.
Formation of a distinctive complex between the inducible bacterial lysine decarboxylase and a novel AAA+ ATPase (2006), J. Biol. Chem., 281, 1532-1546.

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Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-

Subunits

Subunits	Comment	Organism
More	enzyme interacts strongly with regulatory ATPase variant A, RavA, forming a cage-like structure consisting of two enzyme decamers linked by up to five RavA oligomers. Enzyme activity is not affected by binding to RavA, but complex formation results in stimulation of RavA ATPase activity	Escherichia coli

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Release 2023.1 (January 2023)