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http://dx.doi.org/10.5012/bkcs.2009.30.8.1724

ATP Hydrolysis Analysis of Severe Acute Respiratory Syndrome (SARS) Coronavirus Helicase  

Lee, Na-Ra (Department of Bio and Nanochemistry, Kookmin University)
Lee, A-Ram (Department of Bio and Nanochemistry, Kookmin University)
Lee, Bok-Hui (Department of Bioscience and Biotechnology, Konkuk University)
Kim, Dong-Eun (Department of Bioscience and Biotechnology, Konkuk University)
Jeong, Yong-Joo (Department of Bio and Nanochemistry, Kookmin University)
Publication Information
Bulletin of the Korean Chemical Society / v.30, no.8, 2009 , pp. 1724-1728 More about this Journal
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 $Mg^{2+}$ stimulated the ATPase activity with the highest rate and $Mn^{2+}$ with about 40% rate as compared to the $Mg^{2+}$.
Keywords
Severe acute respiratory syndrome coronavirus helicase; ATP hydrolysis; Single-stranded nucleicNacids; pH-Dependence profile; Divalent cations;
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