Journal
FEBS LETTERS
Volume 580, Issue 11, Pages 2577-2583Publisher
WILEY
DOI: 10.1016/j.febslet.2006.04.004
Keywords
antiviral agents; fluorogenic substrate; high throughput screening; proteinase; rhodamine; SARS
Funding
- NIAID NIH HHS [AI056480, R56 AI041599, R01 AI041599, AI41599, U01 AI056480] Funding Source: Medline
Ask authors/readers for more resources
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. (c) 2006 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available