Abstract
A sulfite-dependent ATPase [EC 3.6.1.3] of Thiobacillus thiooxidans was activated and solubilized by treatment with trypsin [EC 3.4.4.4], and purified 84-fold with a 32% recovery. It required both Mg2+ and SO32− for full activity, and its optimum pH was found at 7.5–8.0. Mn2+, Co2+, and Ca2+ could partially substitute for Mg2+, while SeO32− and CrO42− could partially substitute for SO32−. The enzyme hydrolyzed ATP and deoxy-ATP most rapidly and other phosphate esters were poorer substrates. The apparent Km value for ATP was 0.33 mM. The enzyme activity was strongly inhibited by 0.2 mM NaN3 and 10 mM NaF.
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