GSH-dependent peroxidase activity of the rice (Oryza sativa) glutaredoxin, a thioltransferase.
Identifieur interne : 000F70 ( Main/Corpus ); précédent : 000F69; suivant : 000F71GSH-dependent peroxidase activity of the rice (Oryza sativa) glutaredoxin, a thioltransferase.
Auteurs : Kyun Oh Lee ; Jung Ro Lee ; Ji Young Yoo ; Ho Hee Jang ; Jeong Chan Moon ; Bae Gyo Jung ; Yong Hun Chi ; Soo Kwon Park ; Seung Sik Lee ; Chae Oh Lim ; Dae-Jin Yun ; Moo Je Cho ; Sang Yeol LeeSource :
- Biochemical and biophysical research communications [ 0006-291X ] ; 2002.
English descriptors
- KwdEn :
- Antioxidants (metabolism), Cysteine (genetics), Electrophoresis, Polyacrylamide Gel (MeSH), Glutaredoxins (MeSH), Glutathione (physiology), Kinetics (MeSH), Mutation (MeSH), Oryza (enzymology), Oxidoreductases (genetics), Oxidoreductases (metabolism), Peroxidase (genetics), Peroxidase (metabolism), Protein Disulfide Reductase (Glutathione) (MeSH), Substrate Specificity (MeSH).
- MESH :
- chemical , genetics : Cysteine, Oxidoreductases, Peroxidase.
- chemical , metabolism : Antioxidants, Oxidoreductases, Peroxidase.
- chemical , physiology : Glutathione.
- enzymology : Oryza.
- Electrophoresis, Polyacrylamide Gel, Glutaredoxins, Kinetics, Mutation, Protein Disulfide Reductase (Glutathione), Substrate Specificity.
Abstract
Glutaredoxin (Grx) is a 12-kDa thioltransferase that reduces disulfide bonds of other proteins and maintains the redox potential of cells. In addition to its oxidoreductase activity, we report here that a rice Grx (OsGrx) can also function as a GSH-dependent peroxidase. Because of this antioxidant activity, OsGrx protects glutamine synthetase from oxidative damage. Individually replacing the conserved Cys residues in OsGrx with Ser shows that Cys(23), but not Cys(26), is essential for the thioltransferase and GSH-dependent peroxidase activities. Kinetic characterization of OsGrx reveals that the maximal catalytic efficiency (V(max)/K(m)) is obtained with cumene hydroperoxide rather than H(2)O(2) or t-butyl hydroperoxide.
DOI: 10.1016/s0006-291x(02)02047-8
PubMed: 12207894
Links to Exploration step
pubmed:12207894Le document en format XML
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last="Moon">Jeong Chan Moon</name></author><author><name sortKey="Jung, Bae Gyo" sort="Jung, Bae Gyo" uniqKey="Jung B" first="Bae Gyo" last="Jung">Bae Gyo Jung</name></author><author><name sortKey="Chi, Yong Hun" sort="Chi, Yong Hun" uniqKey="Chi Y" first="Yong Hun" last="Chi">Yong Hun Chi</name></author><author><name sortKey="Park, Soo Kwon" sort="Park, Soo Kwon" uniqKey="Park S" first="Soo Kwon" last="Park">Soo Kwon Park</name></author><author><name sortKey="Lee, Seung Sik" sort="Lee, Seung Sik" uniqKey="Lee S" first="Seung Sik" last="Lee">Seung Sik Lee</name></author><author><name sortKey="Lim, Chae Oh" sort="Lim, Chae Oh" uniqKey="Lim C" first="Chae Oh" last="Lim">Chae Oh Lim</name></author><author><name sortKey="Yun, Dae Jin" sort="Yun, Dae Jin" uniqKey="Yun D" first="Dae-Jin" last="Yun">Dae-Jin Yun</name></author><author><name sortKey="Cho, Moo Je" sort="Cho, Moo Je" uniqKey="Cho M" first="Moo Je" last="Cho">Moo Je Cho</name></author><author><name sortKey="Lee, Sang Yeol" 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sortKey="Lee, Seung Sik" sort="Lee, Seung Sik" uniqKey="Lee S" first="Seung Sik" last="Lee">Seung Sik Lee</name></author><author><name sortKey="Lim, Chae Oh" sort="Lim, Chae Oh" uniqKey="Lim C" first="Chae Oh" last="Lim">Chae Oh Lim</name></author><author><name sortKey="Yun, Dae Jin" sort="Yun, Dae Jin" uniqKey="Yun D" first="Dae-Jin" last="Yun">Dae-Jin Yun</name></author><author><name sortKey="Cho, Moo Je" sort="Cho, Moo Je" uniqKey="Cho M" first="Moo Je" last="Cho">Moo Je Cho</name></author><author><name sortKey="Lee, Sang Yeol" sort="Lee, Sang Yeol" uniqKey="Lee S" first="Sang Yeol" last="Lee">Sang Yeol Lee</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>Antioxidants (metabolism)</term><term>Cysteine (genetics)</term><term>Electrophoresis, Polyacrylamide Gel (MeSH)</term><term>Glutaredoxins (MeSH)</term><term>Glutathione (physiology)</term><term>Kinetics (MeSH)</term><term>Mutation (MeSH)</term><term>Oryza (enzymology)</term><term>Oxidoreductases (genetics)</term><term>Oxidoreductases (metabolism)</term><term>Peroxidase (genetics)</term><term>Peroxidase (metabolism)</term><term>Protein Disulfide Reductase (Glutathione) (MeSH)</term><term>Substrate Specificity (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Cysteine</term><term>Oxidoreductases</term><term>Peroxidase</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Antioxidants</term><term>Oxidoreductases</term><term>Peroxidase</term></keywords><keywords scheme="MESH" type="chemical" qualifier="physiology" xml:lang="en"><term>Glutathione</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Oryza</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Electrophoresis, Polyacrylamide Gel</term><term>Glutaredoxins</term><term>Kinetics</term><term>Mutation</term><term>Protein Disulfide Reductase (Glutathione)</term><term>Substrate Specificity</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Glutaredoxin (Grx) is a 12-kDa thioltransferase that reduces disulfide bonds of other proteins and maintains the redox potential of cells. In addition to its oxidoreductase activity, we report here that a rice Grx (OsGrx) can also function as a GSH-dependent peroxidase. Because of this antioxidant activity, OsGrx protects glutamine synthetase from oxidative damage. Individually replacing the conserved Cys residues in OsGrx with Ser shows that Cys(23), but not Cys(26), is essential for the thioltransferase and GSH-dependent peroxidase activities. Kinetic characterization of OsGrx reveals that the maximal catalytic efficiency (V(max)/K(m)) is obtained with cumene hydroperoxide rather than H(2)O(2) or t-butyl hydroperoxide.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">12207894</PMID><DateCompleted><Year>2002</Year><Month>10</Month><Day>24</Day></DateCompleted><DateRevised><Year>2019</Year><Month>06</Month><Day>12</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0006-291X</ISSN><JournalIssue CitedMedium="Print"><Volume>296</Volume><Issue>5</Issue><PubDate><Year>2002</Year><Month>Sep</Month><Day>06</Day></PubDate></JournalIssue><Title>Biochemical and biophysical research communications</Title><ISOAbbreviation>Biochem Biophys Res Commun</ISOAbbreviation></Journal><ArticleTitle>GSH-dependent peroxidase activity of the rice (Oryza sativa) glutaredoxin, a thioltransferase.</ArticleTitle><Pagination><MedlinePgn>1152-6</MedlinePgn></Pagination><Abstract><AbstractText>Glutaredoxin (Grx) is a 12-kDa thioltransferase that reduces disulfide bonds of other proteins and maintains the redox potential of cells. In addition to its oxidoreductase activity, we report here that a rice Grx (OsGrx) can also function as a GSH-dependent peroxidase. Because of this antioxidant activity, OsGrx protects glutamine synthetase from oxidative damage. Individually replacing the conserved Cys residues in OsGrx with Ser shows that Cys(23), but not Cys(26), is essential for the thioltransferase and GSH-dependent peroxidase activities. Kinetic characterization of OsGrx reveals that the maximal catalytic efficiency (V(max)/K(m)) is obtained with cumene hydroperoxide rather than H(2)O(2) or t-butyl hydroperoxide.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Lee</LastName><ForeName>Kyun Oh</ForeName><Initials>KO</Initials><AffiliationInfo><Affiliation>Division of Applied Life Sciences (BK21 program), Department of Biochemistry, PMBBRC, Gyeongsang National University, 660-701, Chinju, Republic of Korea.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Lee</LastName><ForeName>Jung Ro</ForeName><Initials>JR</Initials></Author><Author ValidYN="Y"><LastName>Yoo</LastName><ForeName>Ji Young</ForeName><Initials>JY</Initials></Author><Author ValidYN="Y"><LastName>Jang</LastName><ForeName>Ho Hee</ForeName><Initials>HH</Initials></Author><Author ValidYN="Y"><LastName>Moon</LastName><ForeName>Jeong Chan</ForeName><Initials>JC</Initials></Author><Author ValidYN="Y"><LastName>Jung</LastName><ForeName>Bae Gyo</ForeName><Initials>BG</Initials></Author><Author ValidYN="Y"><LastName>Chi</LastName><ForeName>Yong Hun</ForeName><Initials>YH</Initials></Author><Author ValidYN="Y"><LastName>Park</LastName><ForeName>Soo Kwon</ForeName><Initials>SK</Initials></Author><Author ValidYN="Y"><LastName>Lee</LastName><ForeName>Seung Sik</ForeName><Initials>SS</Initials></Author><Author ValidYN="Y"><LastName>Lim</LastName><ForeName>Chae Oh</ForeName><Initials>CO</Initials></Author><Author ValidYN="Y"><LastName>Yun</LastName><ForeName>Dae-Jin</ForeName><Initials>DJ</Initials></Author><Author ValidYN="Y"><LastName>Cho</LastName><ForeName>Moo Je</ForeName><Initials>MJ</Initials></Author><Author ValidYN="Y"><LastName>Lee</LastName><ForeName>Sang Yeol</ForeName><Initials>SY</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="D000975">Antioxidants</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D054477">Glutaredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.-</RegistryNumber><NameOfSubstance UI="D010088">Oxidoreductases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.11.1.7</RegistryNumber><NameOfSubstance UI="D009195">Peroxidase</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.8.4.2</RegistryNumber><NameOfSubstance UI="D011490">Protein Disulfide Reductase (Glutathione)</NameOfSubstance></Chemical><Chemical><RegistryNumber>GAN16C9B8O</RegistryNumber><NameOfSubstance UI="D005978">Glutathione</NameOfSubstance></Chemical><Chemical><RegistryNumber>K848JZ4886</RegistryNumber><NameOfSubstance UI="D003545">Cysteine</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000975" MajorTopicYN="N">Antioxidants</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D003545" MajorTopicYN="N">Cysteine</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004591" MajorTopicYN="N">Electrophoresis, Polyacrylamide Gel</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D054477" MajorTopicYN="N">Glutaredoxins</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005978" MajorTopicYN="N">Glutathione</DescriptorName><QualifierName UI="Q000502" MajorTopicYN="Y">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D007700" MajorTopicYN="N">Kinetics</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D009154" MajorTopicYN="N">Mutation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D012275" MajorTopicYN="N">Oryza</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010088" MajorTopicYN="N">Oxidoreductases</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D009195" MajorTopicYN="N">Peroxidase</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011490" MajorTopicYN="Y">Protein Disulfide Reductase (Glutathione)</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013379" MajorTopicYN="N">Substrate Specificity</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2002</Year><Month>9</Month><Day>5</Day><Hour>10</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2002</Year><Month>10</Month><Day>31</Day><Hour>4</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2002</Year><Month>9</Month><Day>5</Day><Hour>10</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">12207894</ArticleId><ArticleId IdType="pii">S0006291X02020478</ArticleId><ArticleId IdType="doi">10.1016/s0006-291x(02)02047-8</ArticleId></ArticleIdList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
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