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Enzymatic activity characterization of SARS coronavirus 3C-like protease by fluorescence resonance energy transfer technique.

Identifieur interne : 002930 ( PubMed/Curation ); précédent : 002929; suivant : 002931

Enzymatic activity characterization of SARS coronavirus 3C-like protease by fluorescence resonance energy transfer technique.

Auteurs : Shuai Chen [République populaire de Chine] ; Li-Li Chen ; Hai-Bin Luo ; Tao Sun ; Jing Chen ; Fei Ye ; Jian-Hua Cai ; Jing-Kang Shen ; Xu Shen ; Hua-Liang Jiang

Source :

Acta pharmacologica Sinica [ 1671-4083 ] ; 2005.

RBID : pubmed:15659121

Descripteurs français

English descriptors

KwdEn :
- Alanine (genetics), Amino Acid Substitution (genetics), Cysteine (genetics), Cysteine Endopeptidases, Endopeptidases (chemistry), Endopeptidases (genetics), Fluorescence Resonance Energy Transfer (methods), Histidine (genetics), Hydrogen-Ion Concentration, Kinetics, Methionine (genetics), Mutagenesis, Site-Directed, SARS Virus (enzymology), SARS Virus (genetics), Substrate Specificity (genetics), Temperature, Viral Proteins (chemistry), Viral Proteins (genetics).
MESH :
- chemical , chemistry : Endopeptidases, Viral Proteins.
- chemical , genetics : Alanine, Cysteine, Endopeptidases, Histidine, Methionine, Viral Proteins.
- enzymology : SARS Virus.
- genetics : Amino Acid Substitution, SARS Virus, Substrate Specificity.
- methods : Fluorescence Resonance Energy Transfer.
- chemical : Cysteine Endopeptidases, Hydrogen-Ion Concentration, Kinetics, Mutagenesis, Site-Directed, Temperature.

Abstract

To characterize enzymatic activity of severe acute respiratory syndrome (SARS) coronavirus (CoV) 3C-like protease (3CL(pro)) and its four site-directed mutants.

DOI: 10.1111/j.1745-7254.2005.00010.x
PubMed: 15659121

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Le document en format XML

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<term>Cysteine Endopeptidases</term>
<term>Endopeptidases (chemistry)</term>
<term>Endopeptidases (genetics)</term>
<term>Fluorescence Resonance Energy Transfer (methods)</term>
<term>Histidine (genetics)</term>
<term>Hydrogen-Ion Concentration</term>
<term>Kinetics</term>
<term>Methionine (genetics)</term>
<term>Mutagenesis, Site-Directed</term>
<term>SARS Virus (enzymology)</term>
<term>SARS Virus (genetics)</term>
<term>Substrate Specificity (genetics)</term>
<term>Temperature</term>
<term>Viral Proteins (chemistry)</term>
<term>Viral Proteins (genetics)</term>
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<term>Cinétique</term>
<term>Concentration en ions d'hydrogène</term>
<term>Cysteine endopeptidases</term>
<term>Cystéine (génétique)</term>
<term>Endopeptidases ()</term>
<term>Endopeptidases (génétique)</term>
<term>Histidine (génétique)</term>
<term>Mutagenèse dirigée</term>
<term>Méthionine (génétique)</term>
<term>Protéines virales ()</term>
<term>Protéines virales (génétique)</term>
<term>Spécificité du substrat (génétique)</term>
<term>Substitution d'acide aminé (génétique)</term>
<term>Température</term>
<term>Transfert d'énergie par résonance de fluorescence ()</term>
<term>Virus du SRAS (enzymologie)</term>
<term>Virus du SRAS (génétique)</term>
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<term>Viral Proteins</term>
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<term>Cysteine</term>
<term>Endopeptidases</term>
<term>Histidine</term>
<term>Methionine</term>
<term>Viral Proteins</term>
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<keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Virus du SRAS</term>
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<keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>SARS Virus</term>
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<keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Amino Acid Substitution</term>
<term>SARS Virus</term>
<term>Substrate Specificity</term>
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<keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Alanine</term>
<term>Cystéine</term>
<term>Endopeptidases</term>
<term>Histidine</term>
<term>Méthionine</term>
<term>Protéines virales</term>
<term>Spécificité du substrat</term>
<term>Substitution d'acide aminé</term>
<term>Virus du SRAS</term>
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<keywords scheme="MESH" qualifier="methods" xml:lang="en"><term>Fluorescence Resonance Energy Transfer</term>
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<keywords scheme="MESH" type="chemical" xml:lang="en"><term>Cysteine Endopeptidases</term>
<term>Hydrogen-Ion Concentration</term>
<term>Kinetics</term>
<term>Mutagenesis, Site-Directed</term>
<term>Temperature</term>
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<term>Concentration en ions d'hydrogène</term>
<term>Cysteine endopeptidases</term>
<term>Endopeptidases</term>
<term>Mutagenèse dirigée</term>
<term>Protéines virales</term>
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<front><div type="abstract" xml:lang="en">To characterize enzymatic activity of severe acute respiratory syndrome (SARS) coronavirus (CoV) 3C-like protease (3CL(pro)) and its four site-directed mutants.</div>
</front>
</TEI>
<pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">15659121</PMID>
<DateCompleted><Year>2005</Year>
<Month>06</Month>
<Day>16</Day>
</DateCompleted>
<DateRevised><Year>2020</Year>
<Month>03</Month>
<Day>25</Day>
</DateRevised>
<Article PubModel="Print"><Journal><ISSN IssnType="Print">1671-4083</ISSN>
<JournalIssue CitedMedium="Print"><Volume>26</Volume>
<Issue>1</Issue>
<PubDate><Year>2005</Year>
<Month>Jan</Month>
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<Title>Acta pharmacologica Sinica</Title>
<ISOAbbreviation>Acta Pharmacol. Sin.</ISOAbbreviation>
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<ArticleTitle>Enzymatic activity characterization of SARS coronavirus 3C-like protease by fluorescence resonance energy transfer technique.</ArticleTitle>
<Pagination><MedlinePgn>99-106</MedlinePgn>
</Pagination>
<Abstract><AbstractText Label="AIM" NlmCategory="OBJECTIVE">To characterize enzymatic activity of severe acute respiratory syndrome (SARS) coronavirus (CoV) 3C-like protease (3CL(pro)) and its four site-directed mutants.</AbstractText>
<AbstractText Label="METHODS" NlmCategory="METHODS">Based on the fluorescence resonance energy transfer (FRET) principle using 5-[(2'-aminoethyl)-amino] naphthelenesulfonic acid (EDANS) and 4-[[4-(dimethylamino) phenyl] azo] benzoic acid (Dabcyl) as the energy transfer pair, one fluorogenic substrate was designed for the evaluation of SARS-CoV 3CL(pro) proteolytic activity.</AbstractText>
<AbstractText Label="RESULTS" NlmCategory="RESULTS">The kinetic parameters of the fluorogenic substrate have been determined as Km=404 micromol.L(-1), kcat=1.08 min(-1), and kcat/Km=2.7 mmol(-1).L.min(-1). SARS-CoV 3CL(pro) showed substantial pH and temperature-triggered activity switches, and site-directed mutagenesis analysis of SARS-CoV 3CL(pro) revealed that substitutions of His41, Cys145, and His163 resulted in complete loss of enzymatic activity, while replacement of Met162 with Ala caused strongly increased activity.</AbstractText>
<AbstractText Label="CONCLUSION" NlmCategory="CONCLUSIONS">This present work has provided valuable information for understanding the catalytic mechanism of SARS-CoV 3CL(pro). This FRET-based assay might supply an ideal approach for the exploration SARS-CoV 3CL(pro) putative inhibitors.</AbstractText>
</Abstract>
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<ForeName>Shuai</ForeName>
<Initials>S</Initials>
<AffiliationInfo><Affiliation>Drug Discovery and Design Center, Shanghai Institute of Materia Medica, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, Graduate School of the Chinese Academy of Sciences, Shanghai 201203, China.</Affiliation>
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<ForeName>Li-li</ForeName>
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<ForeName>Tao</ForeName>
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<Author ValidYN="Y"><LastName>Chen</LastName>
<ForeName>Jing</ForeName>
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<ForeName>Fei</ForeName>
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<ForeName>Jian-hua</ForeName>
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<ForeName>Jing-kang</ForeName>
<Initials>JK</Initials>
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<Author ValidYN="Y"><LastName>Shen</LastName>
<ForeName>Xu</ForeName>
<Initials>X</Initials>
</Author>
<Author ValidYN="Y"><LastName>Jiang</LastName>
<ForeName>Hua-liang</ForeName>
<Initials>HL</Initials>
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<Language>eng</Language>
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<PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType>
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Enzymatic activity characterization of SARS coronavirus 3C-like protease by fluorescence resonance energy transfer technique.

Enzymatic activity characterization of SARS coronavirus 3C-like protease by fluorescence resonance energy transfer technique.

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