Selenoglutaredoxin as a glutathione peroxidase mimic.
Identifieur interne : 000B68 ( Main/Exploration ); précédent : 000B67; suivant : 000B69Selenoglutaredoxin as a glutathione peroxidase mimic.
Auteurs : Giulio Casi [Suisse] ; Gerard Roelfes ; Donald HilvertSource :
- Chembiochem : a European journal of chemical biology [ 1439-7633 ] ; 2008.
Descripteurs français
- KwdFr :
- Catalyse (MeSH), Cinétique (MeSH), Dichroïsme circulaire (MeSH), Escherichia coli (métabolisme), Fragments peptidiques (MeSH), Glutarédoxines (composition chimique), Glutarédoxines (métabolisme), Glutathione peroxidase (métabolisme), Protéines Escherichia coli (métabolisme), Protéines recombinantes (composition chimique), Protéines recombinantes (métabolisme), Sélénium (MeSH), Sélénocystéine (métabolisme), Séquence d'acides aminés (MeSH).
- MESH :
- composition chimique : Glutarédoxines, Protéines recombinantes.
- métabolisme : Escherichia coli, Glutarédoxines, Glutathione peroxidase, Protéines Escherichia coli, Protéines recombinantes, Sélénocystéine.
- Catalyse, Cinétique, Dichroïsme circulaire, Fragments peptidiques, Sélénium, Séquence d'acides aminés.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Catalysis (MeSH), Circular Dichroism (MeSH), Escherichia coli (metabolism), Escherichia coli Proteins (metabolism), Glutaredoxins (chemistry), Glutaredoxins (metabolism), Glutathione Peroxidase (metabolism), Kinetics (MeSH), Peptide Fragments (MeSH), Recombinant Proteins (chemistry), Recombinant Proteins (metabolism), Selenium (MeSH), Selenocysteine (metabolism).
- MESH :
- chemical , chemistry : Glutaredoxins, Recombinant Proteins.
- chemical , metabolism : Escherichia coli Proteins, Glutaredoxins, Glutathione Peroxidase, Recombinant Proteins, Selenocysteine.
- metabolism : Escherichia coli.
- Amino Acid Sequence, Catalysis, Circular Dichroism, Kinetics, Peptide Fragments, Selenium.
Abstract
Glutaredoxin (Grx1) from Escherichia coli is a monomeric, 85-amino-acid-long, disulfide-containing redox protein. A Grx1 variant in which the redox-active disulfide was replaced with a selenocysteine (C11U/C14S) was prepared by native chemical ligation from three fragments as a potential mimic of the natural selenoenzyme glutathione peroxidase (Gpx). Selenoglutaredoxin, like the analogous C14S Grx1 variant, shows weak peroxidase activity. The selenol provides a 30-fold advantage over the thiol, but its activity is four orders of magnitude lower than that of bovine Gpx. In contrast, selenoglutaredoxin is an excellent catalyst for thiol-disulfide exchange reactions; it promotes the reduction of beta-hydroxyethyldisulfide by glutathione with a specific activity of 130 units mg(-1). This value is 1.8 times greater than that of C14S Grx1 under identical conditions, and >10(4) greater than the peroxidase activity of either enzyme. Given the facile reduction of the glutathionyl-selenoglutaredoxin adduct by glutathione, oxidation of the selenol by the alkyl hydroperoxide substrate likely limits catalytic turnover and will have to be optimized to create more effective Gpx mimics. These results highlight the challenge of generating Gpx activity in a small, generic protein scaffold, despite the presence of a well-defined glutathione binding site and the intrinsic advantage of selenium over sulfur derivatives.
DOI: 10.1002/cbic.200700745
PubMed: 18548475
Affiliations:
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Hilvert</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2008">2008</date><idno type="RBID">pubmed:18548475</idno><idno type="pmid">18548475</idno><idno type="doi">10.1002/cbic.200700745</idno><idno type="wicri:Area/Main/Corpus">000B81</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000B81</idno><idno type="wicri:Area/Main/Curation">000B81</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">000B81</idno><idno type="wicri:Area/Main/Exploration">000B81</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Selenoglutaredoxin as a glutathione peroxidase mimic.</title><author><name sortKey="Casi, Giulio" sort="Casi, Giulio" uniqKey="Casi G" first="Giulio" last="Casi">Giulio Casi</name><affiliation wicri:level="1"><nlm:affiliation>Laboratorium für Organische Chemie, ETH Zürich, Hönggerberg HCI F339, 8093 Zürich, Switzerland.</nlm:affiliation><country xml:lang="fr">Suisse</country><wicri:regionArea>Laboratorium für Organische Chemie, ETH Zürich, Hönggerberg HCI F339, 8093 Zürich</wicri:regionArea><placeName><settlement type="city">Zurich</settlement><region nuts="3" type="region">Canton de Zurich</region></placeName></affiliation></author><author><name sortKey="Roelfes, Gerard" sort="Roelfes, Gerard" uniqKey="Roelfes G" first="Gerard" last="Roelfes">Gerard Roelfes</name></author><author><name sortKey="Hilvert, Donald" sort="Hilvert, Donald" uniqKey="Hilvert D" first="Donald" last="Hilvert">Donald Hilvert</name></author></analytic><series><title level="j">Chembiochem : a European journal of chemical biology</title><idno type="eISSN">1439-7633</idno><imprint><date when="2008" type="published">2008</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence (MeSH)</term><term>Catalysis (MeSH)</term><term>Circular Dichroism (MeSH)</term><term>Escherichia coli (metabolism)</term><term>Escherichia coli Proteins (metabolism)</term><term>Glutaredoxins (chemistry)</term><term>Glutaredoxins (metabolism)</term><term>Glutathione Peroxidase (metabolism)</term><term>Kinetics (MeSH)</term><term>Peptide Fragments (MeSH)</term><term>Recombinant Proteins (chemistry)</term><term>Recombinant Proteins (metabolism)</term><term>Selenium (MeSH)</term><term>Selenocysteine (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Catalyse (MeSH)</term><term>Cinétique (MeSH)</term><term>Dichroïsme circulaire (MeSH)</term><term>Escherichia coli (métabolisme)</term><term>Fragments peptidiques (MeSH)</term><term>Glutarédoxines (composition chimique)</term><term>Glutarédoxines (métabolisme)</term><term>Glutathione peroxidase (métabolisme)</term><term>Protéines Escherichia coli (métabolisme)</term><term>Protéines recombinantes (composition chimique)</term><term>Protéines recombinantes (métabolisme)</term><term>Sélénium (MeSH)</term><term>Sélénocystéine (métabolisme)</term><term>Séquence d'acides aminés (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Glutaredoxins</term><term>Recombinant Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Escherichia coli Proteins</term><term>Glutaredoxins</term><term>Glutathione Peroxidase</term><term>Recombinant Proteins</term><term>Selenocysteine</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Glutarédoxines</term><term>Protéines recombinantes</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Escherichia coli</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Escherichia coli</term><term>Glutarédoxines</term><term>Glutathione peroxidase</term><term>Protéines Escherichia coli</term><term>Protéines recombinantes</term><term>Sélénocystéine</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Catalysis</term><term>Circular Dichroism</term><term>Kinetics</term><term>Peptide Fragments</term><term>Selenium</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Catalyse</term><term>Cinétique</term><term>Dichroïsme circulaire</term><term>Fragments peptidiques</term><term>Sélénium</term><term>Séquence d'acides aminés</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Glutaredoxin (Grx1) from Escherichia coli is a monomeric, 85-amino-acid-long, disulfide-containing redox protein. A Grx1 variant in which the redox-active disulfide was replaced with a selenocysteine (C11U/C14S) was prepared by native chemical ligation from three fragments as a potential mimic of the natural selenoenzyme glutathione peroxidase (Gpx). Selenoglutaredoxin, like the analogous C14S Grx1 variant, shows weak peroxidase activity. The selenol provides a 30-fold advantage over the thiol, but its activity is four orders of magnitude lower than that of bovine Gpx. In contrast, selenoglutaredoxin is an excellent catalyst for thiol-disulfide exchange reactions; it promotes the reduction of beta-hydroxyethyldisulfide by glutathione with a specific activity of 130 units mg(-1). This value is 1.8 times greater than that of C14S Grx1 under identical conditions, and >10(4) greater than the peroxidase activity of either enzyme. Given the facile reduction of the glutathionyl-selenoglutaredoxin adduct by glutathione, oxidation of the selenol by the alkyl hydroperoxide substrate likely limits catalytic turnover and will have to be optimized to create more effective Gpx mimics. These results highlight the challenge of generating Gpx activity in a small, generic protein scaffold, despite the presence of a well-defined glutathione binding site and the intrinsic advantage of selenium over sulfur derivatives.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">18548475</PMID><DateCompleted><Year>2008</Year><Month>08</Month><Day>06</Day></DateCompleted><DateRevised><Year>2013</Year><Month>11</Month><Day>21</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Electronic">1439-7633</ISSN><JournalIssue CitedMedium="Internet"><Volume>9</Volume><Issue>10</Issue><PubDate><Year>2008</Year><Month>Jul</Month><Day>02</Day></PubDate></JournalIssue><Title>Chembiochem : a European journal of chemical biology</Title><ISOAbbreviation>Chembiochem</ISOAbbreviation></Journal><ArticleTitle>Selenoglutaredoxin as a glutathione peroxidase mimic.</ArticleTitle><Pagination><MedlinePgn>1623-31</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1002/cbic.200700745</ELocationID><Abstract><AbstractText>Glutaredoxin (Grx1) from Escherichia coli is a monomeric, 85-amino-acid-long, disulfide-containing redox protein. A Grx1 variant in which the redox-active disulfide was replaced with a selenocysteine (C11U/C14S) was prepared by native chemical ligation from three fragments as a potential mimic of the natural selenoenzyme glutathione peroxidase (Gpx). Selenoglutaredoxin, like the analogous C14S Grx1 variant, shows weak peroxidase activity. The selenol provides a 30-fold advantage over the thiol, but its activity is four orders of magnitude lower than that of bovine Gpx. In contrast, selenoglutaredoxin is an excellent catalyst for thiol-disulfide exchange reactions; it promotes the reduction of beta-hydroxyethyldisulfide by glutathione with a specific activity of 130 units mg(-1). This value is 1.8 times greater than that of C14S Grx1 under identical conditions, and >10(4) greater than the peroxidase activity of either enzyme. Given the facile reduction of the glutathionyl-selenoglutaredoxin adduct by glutathione, oxidation of the selenol by the alkyl hydroperoxide substrate likely limits catalytic turnover and will have to be optimized to create more effective Gpx mimics. These results highlight the challenge of generating Gpx activity in a small, generic protein scaffold, despite the presence of a well-defined glutathione binding site and the intrinsic advantage of selenium over sulfur derivatives.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Casi</LastName><ForeName>Giulio</ForeName><Initials>G</Initials><AffiliationInfo><Affiliation>Laboratorium für Organische Chemie, ETH Zürich, Hönggerberg HCI F339, 8093 Zürich, Switzerland.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Roelfes</LastName><ForeName>Gerard</ForeName><Initials>G</Initials></Author><Author ValidYN="Y"><LastName>Hilvert</LastName><ForeName>Donald</ForeName><Initials>D</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></Article><MedlineJournalInfo><Country>Germany</Country><MedlineTA>Chembiochem</MedlineTA><NlmUniqueID>100937360</NlmUniqueID><ISSNLinking>1439-4227</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D029968">Escherichia coli Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D054477">Glutaredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010446">Peptide Fragments</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011994">Recombinant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0CH9049VIS</RegistryNumber><NameOfSubstance UI="D017279">Selenocysteine</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.11.1.9</RegistryNumber><NameOfSubstance UI="D005979">Glutathione Peroxidase</NameOfSubstance></Chemical><Chemical><RegistryNumber>H6241UJ22B</RegistryNumber><NameOfSubstance UI="D012643">Selenium</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002384" MajorTopicYN="N">Catalysis</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002942" MajorTopicYN="N">Circular Dichroism</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004926" MajorTopicYN="N">Escherichia coli</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D029968" MajorTopicYN="N">Escherichia coli Proteins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D054477" MajorTopicYN="N">Glutaredoxins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005979" MajorTopicYN="N">Glutathione Peroxidase</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D007700" MajorTopicYN="N">Kinetics</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010446" MajorTopicYN="N">Peptide Fragments</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011994" MajorTopicYN="N">Recombinant Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D012643" MajorTopicYN="Y">Selenium</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017279" MajorTopicYN="N">Selenocysteine</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2008</Year><Month>6</Month><Day>13</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2008</Year><Month>8</Month><Day>7</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2008</Year><Month>6</Month><Day>13</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">18548475</ArticleId><ArticleId IdType="doi">10.1002/cbic.200700745</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Suisse</li></country><region><li>Canton de Zurich</li></region><settlement><li>Zurich</li></settlement></list><tree><noCountry><name sortKey="Hilvert, Donald" sort="Hilvert, Donald" uniqKey="Hilvert D" first="Donald" last="Hilvert">Donald Hilvert</name><name sortKey="Roelfes, Gerard" sort="Roelfes, Gerard" uniqKey="Roelfes G" first="Gerard" last="Roelfes">Gerard Roelfes</name></noCountry><country name="Suisse"><region name="Canton de Zurich"><name sortKey="Casi, Giulio" sort="Casi, Giulio" uniqKey="Casi G" first="Giulio" last="Casi">Giulio Casi</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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