High impact information on ATPase

• The ATPase activity is 50% inhibited by 10 microM vanadate, 1 mM N-ethyl maleimide, or 5 mM AMP-PNP; it is enhanced 50% by 0.2% Triton [1].
• Its ATPase activity is stimulated by Ca2+ and EDTA [2].
• The tomato R gene products I-2 and MI-1 are functional ATP binding proteins with ATPase activity [3].
• We also find that thiamine supplementation partially rescues the phenotype of partial loss-of-function mutants of the Na/K ATPase, providing genetic evidence that thiamine absorption, and/or redistribution from the absorbing cells, requires the full activity of this enzyme [4].
• Moreover, the ATP turnover rates (5.5 and 3.1 ATPs per motor domain per second, respectively) are too low to give rise to the observed microtubule gliding velocities, if only a single motor were driving transport with an 8 nm step per ATPase cycle [5].

Biological context of ATPase

• However, the F(1) ATPase inhibitor was up-regulated in both, implying enhanced homeostasis in conditions where mitochondria are stressed [6].

Anatomical context of ATPase

• Vacuoles purified from Saccharomyces cerevisiae bearing the vph1-1 mutation had no detectable bafilomycin-sensitive ATPase activity or ATP-dependent proton pumping [7].

Other interactions of ATPase

• ATPase characteristics of myosin from nematode Caenorhabditis elegans purified by an improved method. Formation of myosin-phosphate-ADP complex and ATP-induced fluorescence enhancement [8].

Analytical, diagnostic and therapeutic context of ATPase

• Thin layer chromatography revealed that both I-2 and Mi-1 exerted ATPase activity [3].

References