Enzymatic activity of the SARS coronavirus main proteinase dimer.
Identifieur interne : 003F04 ( Main/Curation ); précédent : 003F03; suivant : 003F05Enzymatic activity of the SARS coronavirus main proteinase dimer.
Auteurs : Vito Graziano [États-Unis] ; William J. Mcgrath ; Ann Marie Degruccio ; John J. Dunn ; Walter F. MangelSource :
- FEBS letters [ 0014-5793 ] ; 2006.
Descripteurs français
- KwdFr :
- Cinétique, Clonage moléculaire, Concentration en ions d'hydrogène, Concentration osmolaire, Cysteine endopeptidases (), Cysteine endopeptidases (génétique), Cysteine endopeptidases (isolement et purification), Cysteine endopeptidases (métabolisme), Dimérisation, Expression des gènes, Hydrolyse, Peptides (), Peptides (métabolisme), Sensibilité et spécificité, Spécificité du substrat, Structure quaternaire des protéines, Température, Virus du SRAS (enzymologie).
- MESH :
- enzymologie : Virus du SRAS.
- génétique : Cysteine endopeptidases.
- isolement et purification : Cysteine endopeptidases.
- métabolisme : Cysteine endopeptidases, Peptides.
- Cinétique, Clonage moléculaire, Concentration en ions d'hydrogène, Concentration osmolaire, Cysteine endopeptidases, Dimérisation, Expression des gènes, Hydrolyse, Peptides, Sensibilité et spécificité, Spécificité du substrat, Structure quaternaire des protéines, Température.
English descriptors
- KwdEn :
- Cloning, Molecular, Cysteine Endopeptidases (chemistry), Cysteine Endopeptidases (genetics), Cysteine Endopeptidases (isolation & purification), Cysteine Endopeptidases (metabolism), Dimerization, Gene Expression, Hydrogen-Ion Concentration, Hydrolysis, Kinetics, Osmolar Concentration, Peptides (chemistry), Peptides (metabolism), Protein Structure, Quaternary, SARS Virus (enzymology), Sensitivity and Specificity, Substrate Specificity, Temperature.
- MESH :
- chemical , chemistry : Cysteine Endopeptidases, Peptides.
- chemical , genetics : Cysteine Endopeptidases.
- chemical , isolation & purification : Cysteine Endopeptidases.
- chemical , metabolism : Cysteine Endopeptidases, Peptides.
- enzymology : SARS Virus.
- Cloning, Molecular, Dimerization, Gene Expression, Hydrogen-Ion Concentration, Hydrolysis, Kinetics, Osmolar Concentration, Protein Structure, Quaternary, Sensitivity and Specificity, Substrate Specificity, Temperature.
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.
DOI: 10.1016/j.febslet.2006.04.004
PubMed: 16647061
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pubmed:16647061Le document en format XML
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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.</div></front></TEI></record>Pour manipuler ce document sous Unix (Dilib)
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