Abstract
ATP sulfurylase, which catalyzes the first step on the sulfate activation, was purified to apparent homogeneity from Bacillus stearothermophilus, with ammonium sulfate fractionation and successive column chromatography. The enzyme had an apparent molecular mass of 100 kDa, consisting of two equal-sized-44 kDa subunits. The optimum pH was about 8.5–8.7. Divalent cations such as Mn2+, Mg2+, and Co2+ were required for its activity. Apparent Km values for ATP and were 0.045 mM and 0.2 mM, respectively. The enzyme can use deoxyadenosine 5′-triphosphate as a substrate. The enzyme was thermostable and did not show significant loss of activity for 15 min of incubation up to 70°C, suggesting a practical use for a continuous reaction.
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