A dithiol glutaredoxin cDNA from sweet potato (Ipomoea batatas [L.] Lam): enzyme properties and kinetic studies.
Identifieur interne : 002C24 ( Main/Exploration ); précédent : 002C23; suivant : 002C25A dithiol glutaredoxin cDNA from sweet potato (Ipomoea batatas [L.] Lam): enzyme properties and kinetic studies.
Auteurs : X-W Chi [Taïwan] ; C-T Lin ; Y-C Jiang ; L. Wen ; C-T LinSource :
- Plant biology (Stuttgart, Germany) [ 1438-8677 ] ; 2012.
Descripteurs français
- KwdFr :
- ADN complémentaire (génétique), Cinétique (MeSH), Clonage moléculaire (MeSH), Données de séquences moléculaires (MeSH), Glutarédoxines (composition chimique), Glutarédoxines (génétique), Ipomoea batatas (enzymologie), Ipomoea batatas (génétique), Modèles moléculaires (MeSH), Séquence d'acides aminés (MeSH).
- MESH :
- composition chimique : Glutarédoxines.
- enzymologie : Ipomoea batatas.
- génétique : ADN complémentaire, Glutarédoxines, Ipomoea batatas.
- Cinétique, Clonage moléculaire, Données de séquences moléculaires, Modèles moléculaires, Séquence d'acides aminés.
English descriptors
- KwdEn :
- MESH :
- chemical , chemistry : Glutaredoxins.
- chemical , genetics : DNA, Complementary, Glutaredoxins.
- enzymology : Ipomoea batatas.
- genetics : Ipomoea batatas.
- Amino Acid Sequence, Cloning, Molecular, Kinetics, Models, Molecular, Molecular Sequence Data.
Abstract
Glutaredoxins (Grx) play an important role in reduction of protein glutathione mixed disulphides. An IbGrx cDNA (561 bp, EF362614) encoding a putative dithiol Grx was cloned from sweet potato (Ipomoea batatas [L.] Lam). The deduced amino acid sequence is conserved among the reported dithiol Grx, having a CGYC dithiol motif at the active site. A 3-D structural model was created based on the known crystal structure of a poplar Grx (GrxC1). To characterise the IbGrx protein, the coding region was subcloned into an expression vector and transformed into Escherichia coli. The recombinant His(6) -tagged IbGrx was expressed and purified by metal affinity chromatography. The purified enzyme showed a monomeric band, as demonstrated with 15% SDS-PAGE. The Michaelis constant (K(M) ) for ß-hydroxyethyl disulphide (HED) was 0.50 ± 0.08 Mm. The enzyme retained 60% activity at 80 °C for 16 min. The enzyme was active over a broad pH range from 6.0 to 11.0, and in the presence of imidazole up to 0.4 M. The enzyme was susceptible to protease.
DOI: 10.1111/j.1438-8677.2011.00544.x
PubMed: 22288388
Affiliations:
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Wen</name></author><author><name sortKey="Lin, C T" sort="Lin, C T" uniqKey="Lin C" first="C-T" last="Lin">C-T Lin</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2012">2012</date><idno type="RBID">pubmed:22288388</idno><idno type="pmid">22288388</idno><idno type="doi">10.1111/j.1438-8677.2011.00544.x</idno><idno type="wicri:Area/Main/Corpus">002B52</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">002B52</idno><idno type="wicri:Area/Main/Curation">002B52</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">002B52</idno><idno type="wicri:Area/Main/Exploration">002B52</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">A dithiol glutaredoxin cDNA from sweet potato (Ipomoea batatas [L.] Lam): enzyme properties and kinetic studies.</title><author><name sortKey="Chi, X W" sort="Chi, X W" uniqKey="Chi X" first="X-W" last="Chi">X-W Chi</name><affiliation wicri:level="1"><nlm:affiliation>Institute of Bioscience and Biotechnology and Center of Excellence for Marine Bioenvironment and Biotechnology, National Taiwan Ocean University, 2 Pei-Ning Rd, Keelung, Taiwan.</nlm:affiliation><country xml:lang="fr">Taïwan</country><wicri:regionArea>Institute of Bioscience and Biotechnology and Center of Excellence for Marine Bioenvironment and Biotechnology, National Taiwan Ocean University, 2 Pei-Ning Rd, Keelung</wicri:regionArea><wicri:noRegion>Keelung</wicri:noRegion></affiliation></author><author><name sortKey="Lin, C T" sort="Lin, C T" uniqKey="Lin C" first="C-T" last="Lin">C-T Lin</name></author><author><name sortKey="Jiang, Y C" sort="Jiang, Y C" uniqKey="Jiang Y" first="Y-C" last="Jiang">Y-C Jiang</name></author><author><name sortKey="Wen, L" sort="Wen, L" uniqKey="Wen L" first="L" last="Wen">L. Wen</name></author><author><name sortKey="Lin, C T" sort="Lin, C T" uniqKey="Lin C" first="C-T" last="Lin">C-T Lin</name></author></analytic><series><title level="j">Plant biology (Stuttgart, Germany)</title><idno type="eISSN">1438-8677</idno><imprint><date when="2012" type="published">2012</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence (MeSH)</term><term>Cloning, Molecular (MeSH)</term><term>DNA, Complementary (genetics)</term><term>Glutaredoxins (chemistry)</term><term>Glutaredoxins (genetics)</term><term>Ipomoea batatas (enzymology)</term><term>Ipomoea batatas (genetics)</term><term>Kinetics (MeSH)</term><term>Models, Molecular (MeSH)</term><term>Molecular Sequence Data (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>ADN complémentaire (génétique)</term><term>Cinétique (MeSH)</term><term>Clonage moléculaire (MeSH)</term><term>Données de séquences moléculaires (MeSH)</term><term>Glutarédoxines (composition chimique)</term><term>Glutarédoxines (génétique)</term><term>Ipomoea batatas (enzymologie)</term><term>Ipomoea batatas (génétique)</term><term>Modèles moléculaires (MeSH)</term><term>Séquence d'acides aminés (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Glutaredoxins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>DNA, Complementary</term><term>Glutaredoxins</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Glutarédoxines</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Ipomoea batatas</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Ipomoea batatas</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Ipomoea batatas</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>ADN complémentaire</term><term>Glutarédoxines</term><term>Ipomoea batatas</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Cloning, Molecular</term><term>Kinetics</term><term>Models, Molecular</term><term>Molecular Sequence Data</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Cinétique</term><term>Clonage moléculaire</term><term>Données de séquences moléculaires</term><term>Modèles moléculaires</term><term>Séquence d'acides aminés</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Glutaredoxins (Grx) play an important role in reduction of protein glutathione mixed disulphides. An IbGrx cDNA (561 bp, EF362614) encoding a putative dithiol Grx was cloned from sweet potato (Ipomoea batatas [L.] Lam). The deduced amino acid sequence is conserved among the reported dithiol Grx, having a CGYC dithiol motif at the active site. A 3-D structural model was created based on the known crystal structure of a poplar Grx (GrxC1). To characterise the IbGrx protein, the coding region was subcloned into an expression vector and transformed into Escherichia coli. The recombinant His(6) -tagged IbGrx was expressed and purified by metal affinity chromatography. The purified enzyme showed a monomeric band, as demonstrated with 15% SDS-PAGE. The Michaelis constant (K(M) ) for ß-hydroxyethyl disulphide (HED) was 0.50 ± 0.08 Mm. The enzyme retained 60% activity at 80 °C for 16 min. The enzyme was active over a broad pH range from 6.0 to 11.0, and in the presence of imidazole up to 0.4 M. The enzyme was susceptible to protease.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">22288388</PMID><DateCompleted><Year>2012</Year><Month>10</Month><Day>12</Day></DateCompleted><DateRevised><Year>2012</Year><Month>06</Month><Day>12</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1438-8677</ISSN><JournalIssue CitedMedium="Internet"><Volume>14</Volume><Issue>4</Issue><PubDate><Year>2012</Year><Month>Jul</Month></PubDate></JournalIssue><Title>Plant biology (Stuttgart, Germany)</Title><ISOAbbreviation>Plant Biol (Stuttg)</ISOAbbreviation></Journal><ArticleTitle>A dithiol glutaredoxin cDNA from sweet potato (Ipomoea batatas [L.] Lam): enzyme properties and kinetic studies.</ArticleTitle><Pagination><MedlinePgn>659-65</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1111/j.1438-8677.2011.00544.x</ELocationID><Abstract><AbstractText>Glutaredoxins (Grx) play an important role in reduction of protein glutathione mixed disulphides. An IbGrx cDNA (561 bp, EF362614) encoding a putative dithiol Grx was cloned from sweet potato (Ipomoea batatas [L.] Lam). The deduced amino acid sequence is conserved among the reported dithiol Grx, having a CGYC dithiol motif at the active site. A 3-D structural model was created based on the known crystal structure of a poplar Grx (GrxC1). To characterise the IbGrx protein, the coding region was subcloned into an expression vector and transformed into Escherichia coli. The recombinant His(6) -tagged IbGrx was expressed and purified by metal affinity chromatography. The purified enzyme showed a monomeric band, as demonstrated with 15% SDS-PAGE. The Michaelis constant (K(M) ) for ß-hydroxyethyl disulphide (HED) was 0.50 ± 0.08 Mm. The enzyme retained 60% activity at 80 °C for 16 min. The enzyme was active over a broad pH range from 6.0 to 11.0, and in the presence of imidazole up to 0.4 M. The enzyme was susceptible to protease.</AbstractText><CopyrightInformation>© 2012 German Botanical Society and The Royal Botanical Society of the Netherlands.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Chi</LastName><ForeName>X-W</ForeName><Initials>XW</Initials><AffiliationInfo><Affiliation>Institute of Bioscience and Biotechnology and Center of Excellence for Marine Bioenvironment and Biotechnology, National Taiwan Ocean University, 2 Pei-Ning Rd, Keelung, Taiwan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Lin</LastName><ForeName>C-T</ForeName><Initials>CT</Initials></Author><Author ValidYN="Y"><LastName>Jiang</LastName><ForeName>Y-C</ForeName><Initials>YC</Initials></Author><Author ValidYN="Y"><LastName>Wen</LastName><ForeName>L</ForeName><Initials>L</Initials></Author><Author ValidYN="Y"><LastName>Lin</LastName><ForeName>C-T</ForeName><Initials>CT</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>2012</Year><Month>01</Month><Day>30</Day></ArticleDate></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>Plant Biol (Stuttg)</MedlineTA><NlmUniqueID>101148926</NlmUniqueID><ISSNLinking>1435-8603</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D018076">DNA, Complementary</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D054477">Glutaredoxins</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D003001" MajorTopicYN="N">Cloning, Molecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D018076" MajorTopicYN="N">DNA, Complementary</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D054477" MajorTopicYN="N">Glutaredoxins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D027723" MajorTopicYN="N">Ipomoea batatas</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D007700" MajorTopicYN="N">Kinetics</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008958" MajorTopicYN="N">Models, Molecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="entrez"><Year>2012</Year><Month>2</Month><Day>1</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2012</Year><Month>2</Month><Day>1</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2012</Year><Month>10</Month><Day>13</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">22288388</ArticleId><ArticleId IdType="doi">10.1111/j.1438-8677.2011.00544.x</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Taïwan</li></country></list><tree><noCountry><name sortKey="Jiang, Y C" sort="Jiang, Y C" uniqKey="Jiang Y" first="Y-C" last="Jiang">Y-C Jiang</name><name sortKey="Lin, C T" sort="Lin, C T" uniqKey="Lin C" first="C-T" last="Lin">C-T Lin</name><name sortKey="Lin, C T" sort="Lin, C T" uniqKey="Lin C" first="C-T" last="Lin">C-T Lin</name><name sortKey="Wen, L" sort="Wen, L" uniqKey="Wen L" first="L" last="Wen">L. Wen</name></noCountry><country name="Taïwan"><noRegion><name sortKey="Chi, X W" sort="Chi, X W" uniqKey="Chi X" first="X-W" last="Chi">X-W Chi</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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