Evaluation of peptide-aldehyde inhibitors using R188I mutant of SARS 3CL protease as a proteolysis-resistant mutant.
Identifieur interne : 001A54 ( PubMed/Curation ); précédent : 001A53; suivant : 001A55Evaluation of peptide-aldehyde inhibitors using R188I mutant of SARS 3CL protease as a proteolysis-resistant mutant.
Auteurs : Kenichi Akaji [Japon] ; Hiroyuki Konno ; Mari Onozuka ; Ayumi Makino ; Hiroyuki Saito ; Kazuto NosakaSource :
- Bioorganic & medicinal chemistry [ 1464-3391 ] ; 2008.
Descripteurs français
- KwdFr :
- Aldéhydes (pharmacologie), Aldéhydes (synthèse chimique), Conformation des protéines, Cysteine endopeptidases (génétique), Cysteine endopeptidases (métabolisme), Données de séquences moléculaires, Humains, Hydrolyse, Inhibiteurs de protéases (pharmacologie), Inhibiteurs de protéases (synthèse chimique), Maturation post-traductionnelle des protéines, Modèles moléculaires, Mutation (génétique), Protéines virales (antagonistes et inhibiteurs), Protéines virales (génétique), Protéines virales (métabolisme), Sites de fixation, Spectrométrie de masse MALDI, Spécificité du substrat, Structure moléculaire, Syndrome respiratoire aigu sévère (génétique), Séquence d'acides aminés, Virus du SRAS (enzymologie), Virus du SRAS (génétique), Virus du SRAS (métabolisme).
- MESH :
- antagonistes et inhibiteurs : Protéines virales.
- enzymologie : Virus du SRAS.
- génétique : Cysteine endopeptidases, Mutation, Protéines virales, Syndrome respiratoire aigu sévère, Virus du SRAS.
- métabolisme : Cysteine endopeptidases, Protéines virales, Virus du SRAS.
- pharmacologie : Aldéhydes, Inhibiteurs de protéases.
- synthèse chimique : Aldéhydes, Inhibiteurs de protéases.
- Conformation des protéines, Données de séquences moléculaires, Humains, Hydrolyse, Maturation post-traductionnelle des protéines, Modèles moléculaires, Sites de fixation, Spectrométrie de masse MALDI, Spécificité du substrat, Structure moléculaire, Séquence d'acides aminés.
English descriptors
- KwdEn :
- Aldehydes (chemical synthesis), Aldehydes (pharmacology), Amino Acid Sequence, Binding Sites, Cysteine Endopeptidases (genetics), Cysteine Endopeptidases (metabolism), Humans, Hydrolysis, Models, Molecular, Molecular Sequence Data, Molecular Structure, Mutation (genetics), Protease Inhibitors (chemical synthesis), Protease Inhibitors (pharmacology), Protein Conformation, Protein Processing, Post-Translational, SARS Virus (enzymology), SARS Virus (genetics), SARS Virus (metabolism), Severe Acute Respiratory Syndrome (genetics), Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization, Substrate Specificity, Viral Proteins (antagonists & inhibitors), Viral Proteins (genetics), Viral Proteins (metabolism).
- MESH :
- chemical , antagonists & inhibitors : Viral Proteins.
- chemical , chemical synthesis : Aldehydes, Protease Inhibitors.
- chemical , genetics : Cysteine Endopeptidases, Viral Proteins.
- chemical , metabolism : Cysteine Endopeptidases, Viral Proteins.
- chemical , pharmacology : Aldehydes, Protease Inhibitors.
- enzymology : SARS Virus.
- genetics : Mutation, SARS Virus, Severe Acute Respiratory Syndrome.
- metabolism : SARS Virus.
- Amino Acid Sequence, Binding Sites, Humans, Hydrolysis, Models, Molecular, Molecular Sequence Data, Molecular Structure, Protein Conformation, Protein Processing, Post-Translational, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization, Substrate Specificity.
Abstract
The 3C-like (3CL) protease of the severe acute respiratory syndrome (SARS) coronavirus is a key enzyme for the virus maturation. We found for the first time that the mature SARS 3CL protease is subject to degradation at 188Arg/189Gln. Replacing Arg with Ile at position 188 rendered the protease resistant to proteolysis. The R188I mutant digested a conserved undecapeptide substrate with a K(m) of 33.8 microM and k(cat) of 4753 s(-1). Compared with the value reported for the mature protease containing a C-terminal His-tag, the relative activity of the mutant was nearly 10(6). Novel peptide-aldehyde derivatives containing a side-chain-protected C-terminal Gln efficiently inhibited the catalytic activity of the R188I mutant. The results indicated for the first time that the tetrapeptide sequence is enough for inhibitory activities of peptide-aldehyde derivatives.
DOI: 10.1016/j.bmc.2008.09.057
PubMed: 18845442
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maturation. We found for the first time that the mature SARS 3CL protease is subject to degradation at 188Arg/189Gln. Replacing Arg with Ile at position 188 rendered the protease resistant to proteolysis. The R188I mutant digested a conserved undecapeptide substrate with a K(m) of 33.8 microM and k(cat) of 4753 s(-1). Compared with the value reported for the mature protease containing a C-terminal His-tag, the relative activity of the mutant was nearly 10(6). Novel peptide-aldehyde derivatives containing a side-chain-protected C-terminal Gln efficiently inhibited the catalytic activity of the R188I mutant. The results indicated for the first time that the tetrapeptide sequence is enough for inhibitory activities of peptide-aldehyde derivatives.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">18845442</PMID><DateCompleted><Year>2009</Year><Month>02</Month><Day>19</Day></DateCompleted><DateRevised><Year>2020</Year><Month>04</Month><Day>09</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1464-3391</ISSN><JournalIssue CitedMedium="Internet"><Volume>16</Volume><Issue>21</Issue><PubDate><Year>2008</Year><Month>Nov</Month><Day>01</Day></PubDate></JournalIssue><Title>Bioorganic & medicinal chemistry</Title><ISOAbbreviation>Bioorg. Med. Chem.</ISOAbbreviation></Journal><ArticleTitle>Evaluation of peptide-aldehyde inhibitors using R188I mutant of SARS 3CL protease as a proteolysis-resistant mutant.</ArticleTitle><Pagination><MedlinePgn>9400-8</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.bmc.2008.09.057</ELocationID><Abstract><AbstractText>The 3C-like (3CL) protease of the severe acute respiratory syndrome (SARS) coronavirus is a key enzyme for the virus maturation. We found for the first time that the mature SARS 3CL protease is subject to degradation at 188Arg/189Gln. Replacing Arg with Ile at position 188 rendered the protease resistant to proteolysis. The R188I mutant digested a conserved undecapeptide substrate with a K(m) of 33.8 microM and k(cat) of 4753 s(-1). Compared with the value reported for the mature protease containing a C-terminal His-tag, the relative activity of the mutant was nearly 10(6). Novel peptide-aldehyde derivatives containing a side-chain-protected C-terminal Gln efficiently inhibited the catalytic activity of the R188I mutant. The results indicated for the first time that the tetrapeptide sequence is enough for inhibitory activities of peptide-aldehyde derivatives.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Akaji</LastName><ForeName>Kenichi</ForeName><Initials>K</Initials><AffiliationInfo><Affiliation>Department of Chemistry, Graduate School of Medical Science, Kyoto Prefectural University of Medicine, Kita-ku, Kyoto 603-8334, Japan. akaji@koto.kpu-m.ac.jp</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Konno</LastName><ForeName>Hiroyuki</ForeName><Initials>H</Initials></Author><Author ValidYN="Y"><LastName>Onozuka</LastName><ForeName>Mari</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Makino</LastName><ForeName>Ayumi</ForeName><Initials>A</Initials></Author><Author ValidYN="Y"><LastName>Saito</LastName><ForeName>Hiroyuki</ForeName><Initials>H</Initials></Author><Author ValidYN="Y"><LastName>Nosaka</LastName><ForeName>Kazuto</ForeName><Initials>K</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2008</Year><Month>09</Month><Day>26</Day></ArticleDate></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>Bioorg Med Chem</MedlineTA><NlmUniqueID>9413298</NlmUniqueID><ISSNLinking>0968-0896</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D000447">Aldehydes</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011480">Protease Inhibitors</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D014764">Viral Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.22.-</RegistryNumber><NameOfSubstance UI="C099456">3C-like proteinase, Coronavirus</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.22.-</RegistryNumber><NameOfSubstance UI="D003546">Cysteine Endopeptidases</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000447" MajorTopicYN="N">Aldehydes</DescriptorName><QualifierName UI="Q000138" MajorTopicYN="N">chemical synthesis</QualifierName><QualifierName UI="Q000494" MajorTopicYN="Y">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D001665" MajorTopicYN="N">Binding Sites</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D003546" MajorTopicYN="N">Cysteine Endopeptidases</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006868" MajorTopicYN="N">Hydrolysis</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008958" MajorTopicYN="N">Models, Molecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D015394" MajorTopicYN="N">Molecular Structure</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D009154" MajorTopicYN="N">Mutation</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011480" MajorTopicYN="N">Protease Inhibitors</DescriptorName><QualifierName UI="Q000138" MajorTopicYN="N">chemical synthesis</QualifierName><QualifierName UI="Q000494" MajorTopicYN="Y">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011487" MajorTopicYN="N">Protein Conformation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011499" MajorTopicYN="N">Protein Processing, Post-Translational</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D045473" MajorTopicYN="N">SARS Virus</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D045169" MajorTopicYN="N">Severe Acute Respiratory Syndrome</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D019032" MajorTopicYN="N">Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013379" MajorTopicYN="N">Substrate Specificity</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D014764" MajorTopicYN="N">Viral Proteins</DescriptorName><QualifierName UI="Q000037" MajorTopicYN="Y">antagonists & inhibitors</QualifierName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2008</Year><Month>08</Month><Day>19</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2008</Year><Month>09</Month><Day>22</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2008</Year><Month>09</Month><Day>23</Day></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2008</Year><Month>10</Month><Day>11</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate 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