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• W2000413656 endingPage "27164" @default.
• W2000413656 startingPage "27160" @default.
• W2000413656 abstract "Excess ATP is known to enhance Ca2+-ATPase activity and, among other effects, to accelerate the Ca2+ binding reaction. In previous work, we studied the pH dependence of this reaction and proposed a 33H+/2Ca2+ exchange at the transport sites, in agreement with the H+/Ca2+ counter transport. Here we studied the effect of ADP and nonhydrolyzable ATP analogues on the Ca2+ binding reaction at various pH values.At pH 6, where Ca2+ binding is monophasic and slow, ADP, adenosine 5′-(β,γ-methylene)triphosphate (AMPPCP), or adenyl-5′-yl imidodiphosphate (AMPPNP) increased the Ca2+ binding rate constant 20-fold. At pH 7 and 8, where Ca2+ binding is biphasic, the nucleotides induce fast and monophasic Ca2+ binding. At pH 7, AMPPCP accelerated Ca2+ binding with an apparent dissociation constant of 10 μM.At acidic pH, ADP, AMPPCP, or AMPPNP increased the equilibrium affinity of Ca2+ for ATPase, whereas at alkaline pH, these nucleotides had no effect. At pH 5.5, AMPPCP increased equilibrium Ca2+ binding with an apparent dissociation constant of 1 μM. Excess ATP is known to enhance Ca2+-ATPase activity and, among other effects, to accelerate the Ca2+ binding reaction. In previous work, we studied the pH dependence of this reaction and proposed a 33H+/2Ca2+ exchange at the transport sites, in agreement with the H+/Ca2+ counter transport. Here we studied the effect of ADP and nonhydrolyzable ATP analogues on the Ca2+ binding reaction at various pH values. At pH 6, where Ca2+ binding is monophasic and slow, ADP, adenosine 5′-(β,γ-methylene)triphosphate (AMPPCP), or adenyl-5′-yl imidodiphosphate (AMPPNP) increased the Ca2+ binding rate constant 20-fold. At pH 7 and 8, where Ca2+ binding is biphasic, the nucleotides induce fast and monophasic Ca2+ binding. At pH 7, AMPPCP accelerated Ca2+ binding with an apparent dissociation constant of 10 μM. At acidic pH, ADP, AMPPCP, or AMPPNP increased the equilibrium affinity of Ca2+ for ATPase, whereas at alkaline pH, these nucleotides had no effect. At pH 5.5, AMPPCP increased equilibrium Ca2+ binding with an apparent dissociation constant of 1 μM." @default.
• W2000413656 created "2016-06-24" @default.
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• W2000413656 date "1995-11-01" @default.
• W2000413656 modified "2023-09-27" @default.
• W2000413656 title "The Modulation of Ca2+ Binding to Sarcoplasmic Reticulum ATPase by ATP Analogues Is pH-dependent" @default.
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• W2000413656 doi "https://doi.org/10.1074/jbc.270.45.27160" @default.
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