[59] Inhibitors of the ATP synthetase systems

Linnett, Paul E.; Beechey, R. B.

doi:10.1016/0076-6879(79)55061-7

Cited by 241 publications

(125 citation statements)

References 173 publications

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“…At concentrations of 0.1 mM and 1.0 mM, respectively, the ATPase activity in both systems was reduced to values around 10ϳ20%. While the structural related V-ATPase inhibitor apicularen A reduced this activity only slightly, the inhibitory values of cruentaren A were in the same concentration range as those measured for the specific F-ATPase inhibitor oligomycin [17].…”

Section: Biological Propertiessupporting

confidence: 66%

Cruentaren, a New Antifungal Salicylate-Type Macrolide from Byssovorax cruenta (Myxobacteria) with Inhibitory Effect on Mitochondrial ATPase Activity

et al. 2006

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The novel macrolide cruentaren A was produced at levels up to 3.2 mg/liter by cultures of the myxobacterium Byssovorax cruenta. The new compound strongly inhibited the growth of yeasts and filamentous fungi and showed high cytotoxicity against L929 mouse fibroblast cells. A minor co-metabolite of cruentaren A, named cruentaren B, and identified as a six-membered lactone isomer of cruentaren A, showed only marginal cytotoxicity and no antifungal activity. Cruentaren A inhibited F 0 F 1 mitochondrial ATP-hydrolysis in submitochondrial particles of yeasts and beef heart.

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Section: Biological Propertiessupporting

confidence: 66%

Cruentaren, a New Antifungal Salicylate-Type Macrolide from Byssovorax cruenta (Myxobacteria) with Inhibitory Effect on Mitochondrial ATPase Activity

et al. 2006

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“…1). Crucial for proton transport are the unique glutamic acid residues, one on each subunit c: binding, e.g., dicyclohexyl-carbodiimide to this glutamic acid blocks both proton transport and ATP hydrolysis (Linnett and Beechey 1979;Wada et al 2000;Perez-Sayans et al 2009), proving that catalysis and transport are strongly coupled . In both enzymes this coupling involves a rotation of the rotor relative to the rest of the protein that can be considered as the stator Fillingame et al 2000;Futai et al 2000;Yasuda et al 2001;Rondelez et al 2005;Ueno et al 2005).…”

Section: Introductionmentioning

confidence: 99%

“…Specific inhibitors of V-ATPase are important because the enzyme is a potential therapeutic target in certain diseases, e.g., osteoporosis, deafness and cancer (Linnett and Beechey 1979;Farina and Gagliardi 1999;Bowman and Bowman 2005;Lu et al 2005;Morimura et al 2008;Otero-Rey et al 2008;Supino et al 2008;Hinton et al 2009;Perez-Sayans et al 2009;McHenry et al 2010;Nishisho et al 2011). The macrolide antibiotics concanamycin A and bafilomycin are the most potent and most selective inhibitors of V-ATPase, with IC 50 values down to the nM region (Bowman et al 1988;Farina and Gagliardi 1999;Gagliardi et al 1999;Huss et al 2002;Dixon et al 2008).…”

Section: Introductionmentioning

confidence: 99%

Estimating the rotation rate in the vacuolar proton-ATPase in native yeast vacuolar membranes

et al. 2012

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The rate of rotation of the rotor of the yeast vacuolar proton-ATPase (V-ATPase), relative to the stator or the steady parts of enzyme, is estimated in native vacuolar membrane vesicles of Saccharomyces cerevisiae under standardised conditions. Membrane vesicles are spontaneously formed after exposing purified yeast vacuoles to osmotic shock. The fraction of the total ATPase activity originating from V-ATPase is determined using the potent and specific inhibitor of the enzyme, concanamycin A. Inorganic phosphate liberated from ATP in the vacuolar membrane vesicle system, during 10 min of ATPase activity at 20 °C, is assayed spectrophotometrically for different concanamycin A concentrations. A fit to the quadratic binding equation, assuming a single concanamycin A binding site on a monomeric V-ATPase (our data is incompatible with models assuming more binding sites) to the inhibitor titration curve determines the concentration of the enzyme. Combining it with the known rotation:ATP stoichiometry of V-ATPase and the assayed concentration of inorganic phosphate liberated by V-ATPase leads to an average rate of ~9.53 Hz of the 360 degrees rotation, which, according to the time-dependence of the activity, extrapolates to ~14.14 Hz for the beginning of the reaction. These are low limit estimates. To our knowledge this is the first report of the rotation rate in a V-ATPase that is not subjected to genetic or chemical modification and it is not fixed on a solid support, instead it is functioning in its native membrane environment.Special Issue: Structure, function, folding and assembly of membrane proteins -Insight from Biophysics.

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“…We describe herein the isolation and structural elucidation of aurovertin E (2). glucose 20 g, KH 2 PO 4 3 g, MgSO 4 1.5 g, citric acid 0.1 g and thiamin hydrochloride 10 mg in 1 liter of deionized water. Reagent bottles were used as flask (size: 500 ml; volume of media: 300 ml).…”

Section: Introductionmentioning

confidence: 99%