Enzymatic activity of the SARS coronavirus main proteinase dimer

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 sequen...

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Detalles Bibliográficos
Autores principales: Graziano, Vito, McGrath, William J., DeGruccio, Ann Marie, Dunn, John J., Mangel, Walter F.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: John Wiley and Sons Inc. 2006
Materias:
Short Communications
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7094300/
https://www.ncbi.nlm.nih.gov/pubmed/16647061
http://dx.doi.org/10.1016/j.febslet.2006.04.004
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author Graziano, Vito
McGrath, William J.
DeGruccio, Ann Marie
Dunn, John J.
Mangel, Walter F.
author_facet Graziano, Vito
McGrath, William J.
DeGruccio, Ann Marie
Dunn, John J.
Mangel, Walter F.
author_sort Graziano, Vito
collection PubMed
description 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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spelling pubmed-70943002020-03-25 Enzymatic activity of the SARS coronavirus main proteinase dimer Graziano, Vito McGrath, William J. DeGruccio, Ann Marie Dunn, John J. Mangel, Walter F. FEBS Lett Short Communications 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. John Wiley and Sons Inc. 2006-05-15 2006-04-21 /pmc/articles/PMC7094300/ /pubmed/16647061 http://dx.doi.org/10.1016/j.febslet.2006.04.004 Text en FEBS Letters 580 (2006) 1873-3468 © 2015 Federation of European Biochemical Societies This article is being made freely available through PubMed Central as part of the COVID-19 public health emergency response. It can be used for unrestricted research re-use and analysis in any form or by any means with acknowledgement of the original source, for the duration of the public health emergency.
spellingShingle Short Communications
Graziano, Vito
McGrath, William J.
DeGruccio, Ann Marie
Dunn, John J.
Mangel, Walter F.
Enzymatic activity of the SARS coronavirus main proteinase dimer
title Enzymatic activity of the SARS coronavirus main proteinase dimer
title_full Enzymatic activity of the SARS coronavirus main proteinase dimer
title_fullStr Enzymatic activity of the SARS coronavirus main proteinase dimer
title_full_unstemmed Enzymatic activity of the SARS coronavirus main proteinase dimer
title_short Enzymatic activity of the SARS coronavirus main proteinase dimer
title_sort enzymatic activity of the sars coronavirus main proteinase dimer
topic Short Communications
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7094300/
https://www.ncbi.nlm.nih.gov/pubmed/16647061
http://dx.doi.org/10.1016/j.febslet.2006.04.004
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