Glutaredoxins catalyze the reduction of glutathione by dihydrolipoamide with high efficiency.
Identifieur interne : 000F85 ( Main/Exploration ); précédent : 000F84; suivant : 000F86Glutaredoxins catalyze the reduction of glutathione by dihydrolipoamide with high efficiency.
Auteurs : Pablo Porras [Espagne] ; José R. Pedrajas ; Emilia Martínez-Galisteo ; C Alicia Padilla ; Catrine Johansson ; Arne Holmgren ; J Antonio BárcenaSource :
- Biochemical and biophysical research communications [ 0006-291X ] ; 2002.
Descripteurs français
- KwdFr :
- MESH :
- analogues et dérivés : Acide lipoïque.
- métabolisme : Acide lipoïque, Glutathion, Protéines, Protéines recombinantes.
- Animaux, Catalyse, Escherichia coli, Glutarédoxines, Oxidoreductases, Oxydoréduction, Rats.
English descriptors
- KwdEn :
- MESH :
- chemical , analogs & derivatives : Thioctic Acid.
- chemical , metabolism : Glutathione, Proteins, Recombinant Proteins, Thioctic Acid.
- chemical : Glutaredoxins, Oxidoreductases.
- Animals, Catalysis, Escherichia coli, Oxidation-Reduction, Rats.
Abstract
Glutaredoxins (Grx) are small (approximately 12kDa) proteins which catalyze thiol disulfide oxidoreductions involving glutathione (GSH) and disulfides in proteins or small molecules. Here, we present data which demonstrate the ability of glutaredoxins to catalyze the reduction of oxidized glutathione (GSSG) by dihydrolipoamide (DHL), an important biological redox catalyst and synthetic antioxidant. We have designed a new assay method to quantify the rate of reduction of GSSG and other disulfides by reduced lipoamide and have tested a set of eight recombinant Grx from human, rat, yeast, and E. coli. Lipoamide dependent activity is highest with the large atypical E. coli Grx2 (k(cat)=3.235 min(-1)) and lowest for human mitochondrial Grx2a (k(cat)=96 min(-1)) covering a wider range than k(cat) for the standard reduction of hydroxyethyldisulfide (HED) by GSH (290-2.851 min(-1)). The lipoamide/HED activity ratio was highest for yeast Grx2 (1.25) and E. coli Grx2 and lowest for E. coli Grx1 (0.13). These results suggest a new role for Grxs as ancillary proteins that could shunt reducing equivalents from main catabolic pathways to recycling of GSSG via a lipoyl group, thus serving biochemical functions which involve GSH but without NAD(P)H consumption.
DOI: 10.1016/s0006-291x(02)00771-4
PubMed: 12135599
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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Pedrajas</name></author><author><name sortKey="Martinez Galisteo, Emilia" sort="Martinez Galisteo, Emilia" uniqKey="Martinez Galisteo E" first="Emilia" last="Martínez-Galisteo">Emilia Martínez-Galisteo</name></author><author><name sortKey="Padilla, C Alicia" sort="Padilla, C Alicia" uniqKey="Padilla C" first="C Alicia" last="Padilla">C Alicia Padilla</name></author><author><name sortKey="Johansson, Catrine" sort="Johansson, Catrine" uniqKey="Johansson C" first="Catrine" last="Johansson">Catrine Johansson</name></author><author><name sortKey="Holmgren, Arne" sort="Holmgren, Arne" uniqKey="Holmgren A" first="Arne" last="Holmgren">Arne Holmgren</name></author><author><name sortKey="Barcena, J Antonio" sort="Barcena, J Antonio" uniqKey="Barcena J" first="J Antonio" last="Bárcena">J Antonio Bárcena</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2002">2002</date><idno type="RBID">pubmed:12135599</idno><idno type="pmid">12135599</idno><idno type="doi">10.1016/s0006-291x(02)00771-4</idno><idno type="wicri:Area/Main/Corpus">000F72</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000F72</idno><idno type="wicri:Area/Main/Curation">000F72</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">000F72</idno><idno type="wicri:Area/Main/Exploration">000F72</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Glutaredoxins catalyze the reduction of glutathione by dihydrolipoamide with high efficiency.</title><author><name sortKey="Porras, Pablo" sort="Porras, Pablo" uniqKey="Porras P" first="Pablo" last="Porras">Pablo Porras</name><affiliation wicri:level="2"><nlm:affiliation>Department of Biochemistry and Molecular Biology, Campus de Rabanales, Edificio Severo Ochoa, 1(a) planta, University of Córdoba, 14071 Córdoba, Spain.</nlm:affiliation><country xml:lang="fr">Espagne</country><wicri:regionArea>Department of Biochemistry and Molecular Biology, Campus de Rabanales, Edificio Severo Ochoa, 1(a) planta, University of Córdoba, 14071 Córdoba</wicri:regionArea><placeName><region nuts="2" type="communauté">Andalousie</region></placeName></affiliation></author><author><name sortKey="Pedrajas, Jose R" sort="Pedrajas, Jose R" uniqKey="Pedrajas J" first="José R" last="Pedrajas">José R. Pedrajas</name></author><author><name sortKey="Martinez Galisteo, Emilia" sort="Martinez Galisteo, Emilia" uniqKey="Martinez Galisteo E" first="Emilia" last="Martínez-Galisteo">Emilia Martínez-Galisteo</name></author><author><name sortKey="Padilla, C Alicia" sort="Padilla, C Alicia" uniqKey="Padilla C" first="C Alicia" last="Padilla">C Alicia Padilla</name></author><author><name sortKey="Johansson, Catrine" sort="Johansson, Catrine" uniqKey="Johansson C" first="Catrine" last="Johansson">Catrine Johansson</name></author><author><name sortKey="Holmgren, Arne" sort="Holmgren, Arne" uniqKey="Holmgren A" first="Arne" last="Holmgren">Arne Holmgren</name></author><author><name sortKey="Barcena, J Antonio" sort="Barcena, J Antonio" uniqKey="Barcena J" first="J Antonio" last="Bárcena">J Antonio Bárcena</name></author></analytic><series><title level="j">Biochemical and biophysical research communications</title><idno type="ISSN">0006-291X</idno><imprint><date when="2002" type="published">2002</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals (MeSH)</term><term>Catalysis (MeSH)</term><term>Escherichia coli (MeSH)</term><term>Glutaredoxins (MeSH)</term><term>Glutathione (metabolism)</term><term>Oxidation-Reduction (MeSH)</term><term>Oxidoreductases (MeSH)</term><term>Proteins (metabolism)</term><term>Rats (MeSH)</term><term>Recombinant Proteins (metabolism)</term><term>Thioctic Acid (analogs & derivatives)</term><term>Thioctic Acid (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Acide lipoïque (analogues et dérivés)</term><term>Acide lipoïque (métabolisme)</term><term>Animaux (MeSH)</term><term>Catalyse (MeSH)</term><term>Escherichia coli (MeSH)</term><term>Glutarédoxines (MeSH)</term><term>Glutathion (métabolisme)</term><term>Oxidoreductases (MeSH)</term><term>Oxydoréduction (MeSH)</term><term>Protéines (métabolisme)</term><term>Protéines recombinantes (métabolisme)</term><term>Rats (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="analogs & derivatives" xml:lang="en"><term>Thioctic Acid</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Glutathione</term><term>Proteins</term><term>Recombinant Proteins</term><term>Thioctic Acid</term></keywords><keywords scheme="MESH" type="chemical" xml:lang="en"><term>Glutaredoxins</term><term>Oxidoreductases</term></keywords><keywords scheme="MESH" qualifier="analogues et dérivés" xml:lang="fr"><term>Acide lipoïque</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Acide lipoïque</term><term>Glutathion</term><term>Protéines</term><term>Protéines recombinantes</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Catalysis</term><term>Escherichia coli</term><term>Oxidation-Reduction</term><term>Rats</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Catalyse</term><term>Escherichia coli</term><term>Glutarédoxines</term><term>Oxidoreductases</term><term>Oxydoréduction</term><term>Rats</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Glutaredoxins (Grx) are small (approximately 12kDa) proteins which catalyze thiol disulfide oxidoreductions involving glutathione (GSH) and disulfides in proteins or small molecules. Here, we present data which demonstrate the ability of glutaredoxins to catalyze the reduction of oxidized glutathione (GSSG) by dihydrolipoamide (DHL), an important biological redox catalyst and synthetic antioxidant. We have designed a new assay method to quantify the rate of reduction of GSSG and other disulfides by reduced lipoamide and have tested a set of eight recombinant Grx from human, rat, yeast, and E. coli. Lipoamide dependent activity is highest with the large atypical E. coli Grx2 (k(cat)=3.235 min(-1)) and lowest for human mitochondrial Grx2a (k(cat)=96 min(-1)) covering a wider range than k(cat) for the standard reduction of hydroxyethyldisulfide (HED) by GSH (290-2.851 min(-1)). The lipoamide/HED activity ratio was highest for yeast Grx2 (1.25) and E. coli Grx2 and lowest for E. coli Grx1 (0.13). These results suggest a new role for Grxs as ancillary proteins that could shunt reducing equivalents from main catabolic pathways to recycling of GSSG via a lipoyl group, thus serving biochemical functions which involve GSH but without NAD(P)H consumption.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">12135599</PMID><DateCompleted><Year>2002</Year><Month>08</Month><Day>22</Day></DateCompleted><DateRevised><Year>2020</Year><Month>02</Month><Day>04</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0006-291X</ISSN><JournalIssue CitedMedium="Print"><Volume>295</Volume><Issue>5</Issue><PubDate><Year>2002</Year><Month>Aug</Month><Day>02</Day></PubDate></JournalIssue><Title>Biochemical and biophysical research communications</Title><ISOAbbreviation>Biochem Biophys Res Commun</ISOAbbreviation></Journal><ArticleTitle>Glutaredoxins catalyze the reduction of glutathione by dihydrolipoamide with high efficiency.</ArticleTitle><Pagination><MedlinePgn>1046-51</MedlinePgn></Pagination><Abstract><AbstractText>Glutaredoxins (Grx) are small (approximately 12kDa) proteins which catalyze thiol disulfide oxidoreductions involving glutathione (GSH) and disulfides in proteins or small molecules. Here, we present data which demonstrate the ability of glutaredoxins to catalyze the reduction of oxidized glutathione (GSSG) by dihydrolipoamide (DHL), an important biological redox catalyst and synthetic antioxidant. We have designed a new assay method to quantify the rate of reduction of GSSG and other disulfides by reduced lipoamide and have tested a set of eight recombinant Grx from human, rat, yeast, and E. coli. Lipoamide dependent activity is highest with the large atypical E. coli Grx2 (k(cat)=3.235 min(-1)) and lowest for human mitochondrial Grx2a (k(cat)=96 min(-1)) covering a wider range than k(cat) for the standard reduction of hydroxyethyldisulfide (HED) by GSH (290-2.851 min(-1)). The lipoamide/HED activity ratio was highest for yeast Grx2 (1.25) and E. coli Grx2 and lowest for E. coli Grx1 (0.13). These results suggest a new role for Grxs as ancillary proteins that could shunt reducing equivalents from main catabolic pathways to recycling of GSSG via a lipoyl group, thus serving biochemical functions which involve GSH but without NAD(P)H consumption.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Porras</LastName><ForeName>Pablo</ForeName><Initials>P</Initials><AffiliationInfo><Affiliation>Department of Biochemistry and Molecular Biology, Campus de Rabanales, Edificio Severo Ochoa, 1(a) planta, University of Córdoba, 14071 Córdoba, Spain.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Pedrajas</LastName><ForeName>José R</ForeName><Initials>JR</Initials></Author><Author ValidYN="Y"><LastName>Martínez-Galisteo</LastName><ForeName>Emilia</ForeName><Initials>E</Initials></Author><Author ValidYN="Y"><LastName>Padilla</LastName><ForeName>C Alicia</ForeName><Initials>CA</Initials></Author><Author ValidYN="Y"><LastName>Johansson</LastName><ForeName>Catrine</ForeName><Initials>C</Initials></Author><Author ValidYN="Y"><LastName>Holmgren</LastName><ForeName>Arne</ForeName><Initials>A</Initials></Author><Author ValidYN="Y"><LastName>Bárcena</LastName><ForeName>J Antonio</ForeName><Initials>JA</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>United States</Country><MedlineTA>Biochem Biophys Res Commun</MedlineTA><NlmUniqueID>0372516</NlmUniqueID><ISSNLinking>0006-291X</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C516005">GLRX protein, human</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C516008">GLRX2 protein, human</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C516007">Glrx protein, rat</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C516010">Glrx2 protein, rat</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D054477">Glutaredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011506">Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011994">Recombinant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>3884-47-7</RegistryNumber><NameOfSubstance UI="C007409">dihydrolipoamide</NameOfSubstance></Chemical><Chemical><RegistryNumber>73Y7P0K73Y</RegistryNumber><NameOfSubstance UI="D008063">Thioctic Acid</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.-</RegistryNumber><NameOfSubstance UI="D010088">Oxidoreductases</NameOfSubstance></Chemical><Chemical><RegistryNumber>GAN16C9B8O</RegistryNumber><NameOfSubstance UI="D005978">Glutathione</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002384" MajorTopicYN="N">Catalysis</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004926" MajorTopicYN="N">Escherichia coli</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D054477" MajorTopicYN="N">Glutaredoxins</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005978" MajorTopicYN="N">Glutathione</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010084" MajorTopicYN="N">Oxidation-Reduction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010088" MajorTopicYN="Y">Oxidoreductases</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011506" MajorTopicYN="N">Proteins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D051381" MajorTopicYN="N">Rats</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011994" MajorTopicYN="N">Recombinant Proteins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008063" MajorTopicYN="N">Thioctic Acid</DescriptorName><QualifierName UI="Q000031" MajorTopicYN="Y">analogs & derivatives</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2002</Year><Month>7</Month><Day>24</Day><Hour>10</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2002</Year><Month>8</Month><Day>23</Day><Hour>10</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2002</Year><Month>7</Month><Day>24</Day><Hour>10</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">12135599</ArticleId><ArticleId IdType="pii">S0006291X02007714</ArticleId><ArticleId IdType="doi">10.1016/s0006-291x(02)00771-4</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Espagne</li></country><region><li>Andalousie</li></region></list><tree><noCountry><name sortKey="Barcena, J Antonio" sort="Barcena, J Antonio" uniqKey="Barcena J" first="J Antonio" last="Bárcena">J Antonio Bárcena</name><name sortKey="Holmgren, Arne" sort="Holmgren, Arne" uniqKey="Holmgren A" first="Arne" last="Holmgren">Arne Holmgren</name><name sortKey="Johansson, Catrine" sort="Johansson, Catrine" uniqKey="Johansson C" first="Catrine" last="Johansson">Catrine Johansson</name><name sortKey="Martinez Galisteo, Emilia" sort="Martinez Galisteo, Emilia" uniqKey="Martinez Galisteo E" first="Emilia" last="Martínez-Galisteo">Emilia Martínez-Galisteo</name><name sortKey="Padilla, C Alicia" sort="Padilla, C Alicia" uniqKey="Padilla C" first="C Alicia" last="Padilla">C Alicia Padilla</name><name sortKey="Pedrajas, Jose R" sort="Pedrajas, Jose R" uniqKey="Pedrajas J" first="José R" last="Pedrajas">José R. Pedrajas</name></noCountry><country name="Espagne"><region name="Andalousie"><name sortKey="Porras, Pablo" sort="Porras, Pablo" uniqKey="Porras P" first="Pablo" last="Porras">Pablo Porras</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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