Enzymatic activity of the SARS coronavirus main proteinase dimer.

FEBS Letters
Vito GrazianoWalter F Mangel

Abstract

The enzymatic activity of the SARS coronavirus main proteinase dimer was characterized by a sensitive, quantitative assay. The new, fluorogenic substrate, (Ala-Arg-Leu-Gln-NH)(2)-Rhodamine, contained a severe acute respiratory syndrome coronavirus (SARS CoV) main proteinase consensus cleavage sequence and Rhodamine 110, one of the most detectable compounds known, as the reporter group. The gene for the enzyme was cloned in the absence of purification tags, expressed in Escherichia coli and the enzyme purified. Enzyme activity from the SARS CoV main proteinase dimer could readily be detected at low pM concentrations. The enzyme exhibited a high K(m), and is unusually sensitive to ionic strength and reducing agents.

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Citations

May 3, 2011·Protein & Cell·Bin Xia, Xue Kang
Apr 28, 2010·Biochemistry·Jennifer BarrilaErnesto Freire
Jul 19, 2011·Future Virology·Dale L Barnard, Yohichi Kumaki
May 29, 2013·FEBS Letters·William J McGrathWalter F Mangel
May 17, 2013·The Journal of Physical Chemistry. B·Amir MazouchiClaudiu C Gradinaru
Feb 15, 2014·Journal of Biomolecular Screening·Nenggang ZhangDebananda Pati
Oct 20, 2020·Frontiers in Immunology·Narasimha M BeerakaGjumrakch Aliev
Mar 28, 2021·European Journal of Clinical Pharmacology·Suzy HuijghebaertGuido Vanham
Dec 23, 2020·Journal of Proteome Research·Mostafa JamalanFathollah Gholami-Borujeni

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Methods Mentioned

BETA
ISS
electrophoresis
proteinase assay
enzyme assay
fluorescence
FRET

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