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    Molecular analysis of the interaction of anthrax adenylyl cyclase toxin, edema factor, with 2(3)-O-(N-methyl)anthraniloyl)-substituted purine and pyrimidine nucleotides.

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    Abbreviations AC, adenylyl cyclase; ANT, anthraniloyl-; CaM, calmodulin; CyaA, Bordetella pertussis adenylyl cyclase toxin; ESI, electrospray ionization; FRET, fluorescence resonance energy transfer; HPLC, high pressure liquid chromatography; k, capacity factor; mAC, mammalian membranous adenylyl cyclase; MANT, methylanthraniloyl-; MS, mass spectroscopy; MW, molecular weight; NDP, nucleoside 5´-diphosphate; NTP, nucleoside 5´-triphosphate; PMEApp, {9-[2-(phosphonomethoxy)ethyl]adenine diphosphate}; EF, full-length edema factor adenylyl cyclase toxin; EF3, catalytic domain of edema factor adenylyl cyclase toxin; R f , retention factor; R t , retention time; TLC, thin layer chromatography. MOL #52340 3 Abstract Bacillus anthracis causes anthrax disease and exerts its deleterious effects by the release of three exotoxins, i.e. lethal factor, protective antigen and edema factor EF), a highly active calmodulin-dependent adenylyl cyclase (AC). However, conventional antibiotic treatment is ineffective against either toxemia or antibioticresistant strains. Thus, more effective drugs for anthrax treatment are needed. Previous studies from our laboratory showed that mammalian membranous A
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