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ARG2 — ATP5O

Text-mined interactions from Literome

Nadanaciva et al., Biochemistry 1999 : The role of beta-Arg-182 , an essential catalytic site residue in Escherichia coli F1-ATPase
da Silva et al., Brain Res 1999 : Considering that some GC are epileptogenic and cause a decrease in membrane fluidity and that Na+, K ( + ) -ATPase, a membrane bound enzyme, is essential for cellular excitability and is decreased in experimental and human epilepsy, in the present study we determined the in vitro effects of Arg , N-acetylarginine ( NAA ), argininic acid ( AA ) and homoarginine ( HA ) on the activity of Na+, K ( + ) -ATPase in the synaptic plasma membrane from cerebral cortex of young rats in the hope to identify a possible mechanism for the brain damage in hyperargininemia
Hishida et al., Proc Natl Acad Sci U S A 2004 : This study presents direct evidence that Arg-174 of RuvB allosterically stimulates the ATPase of the adjacent subunit in a RuvB hexamer
Wang et al., J Biol Chem 2005 : Moreover, when the ATPase-defective mutant R635A or R638A is mixed with the Walker A mutant of D2, the ATPase activity is partially restored, suggesting that Arg ( 635 ) and Arg ( 638 ) can stimulate the ATPase activity of the neighboring protomer
Toustrup-Jensen et al., J Biol Chem 2009 : Tyr ( 1017 ), Tyr ( 1018 ), and Arg ( 935 ) are furthermore indispensable to Na ( + ) interaction on the extracellular side of the membrane, as revealed by inability of high Na ( + ) concentrations to drive the transition from E ( 1 ) P to E ( 2 ) P backwards toward E ( 1 ) P and inhibit Na ( + ) -ATPase activity in mutants