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• W286603286 endingPage "1728" @default.
• W286603286 startingPage "1724" @default.
• W286603286 abstract "Severe acute respiratory syndrome coronavirus (SARS-CoV) helicase separates the double-stranded nucleic acids using the energy from ATP hydrolysis. We have measured ATPase activity of SARS-CoV helicase in the presence of various types of nucleic acids. Steady state ATPase analysis showed that poly(U) has two-times higher turnover number than poly(C) with lower Michaelis constant. When M13 single-stranded DNA is used as substrate, the Michaelis constant was about twenty-times lower than poly(U), whereas turnover numbers were similar. However, stimulation of ATPase activity was not observed in the presence of double-stranded DNA. pH dependent profiles of ATP hydrolysis with the helicase showed that the optimal ATPase activities were in a range of pH 6.2 ~ 6.6. In addition, ATP hydrolysis activity assays performed in the presence of various divalent cations exhibited that <TEX>$Mg^{2+}$</TEX> stimulated the ATPase activity with the highest rate and <TEX>$Mn^{2+}$</TEX> with about 40% rate as compared to the <TEX>$Mg^{2+}$</TEX>." @default.
• W286603286 created "2016-06-24" @default.
• W286603286 date "2009-08-20" @default.
• W286603286 modified "2023-09-30" @default.
• W286603286 title "ATP Hydrolysis Analysis of Severe Acute Respiratory Syndrome (SARS) Coronavirus Helicase" @default.
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• W286603286 doi "https://doi.org/10.5012/bkcs.2009.30.8.1724" @default.
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