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ATP5O — TYR

Text-mined interactions from Literome

Liu et al., Proc Natl Acad Sci U S A 2006 : Tyr-53 phosphorylation does not affect the ability of filamentous actin to activate myosin ATPase
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
Higashi et al., J Biol Chem 2010 : Leu ( 110 ) and Tyr ( 261 ) in PotB and Asp ( 108 ), Asp ( 198 ), and Asp ( 199 ) in PotC were involved in the recognition of spermidine, and Trp ( 100 ) and Tyr ( 261 ) in PotB and Asp ( 108 ), Glu ( 169 ), and Asp ( 198 ) in PotC were involved in ATPase activity of PotA ... Accordingly, Trp ( 100 ) in PotB was involved in both PotD recognition and ATPase activity, Leu ( 110 ) in PotB was involved in both PotD and spermidine recognition, and Tyr ( 261 ) in PotB was involved in both spermidine recognition and ATPase activity
Kurella et al., Biochim Biophys Acta 1995 : VP-16/tyrosinase caused inhibition of Na+/K ( + ) -ATPase which was dependent on the incubation time and concentration of tyrosinase