New thioredoxins and glutaredoxins as electron donors of 3'-phosphoadenylylsulfate reductase.
Identifieur interne : 001098 ( Main/Exploration ); précédent : 001097; suivant : 001099New thioredoxins and glutaredoxins as electron donors of 3'-phosphoadenylylsulfate reductase.
Auteurs : C H Lillig [Allemagne] ; A. Prior ; J D Schwenn ; F. Aslund ; D. Ritz ; A. Vlamis-Gardikas ; A. HolmgrenSource :
- The Journal of biological chemistry [ 0021-9258 ] ; 1999.
Descripteurs français
- KwdFr :
- MESH :
English descriptors
- KwdEn :
- MESH :
- chemical , metabolism : Oxidoreductases, Proteins, Ribonucleotides, Sulfates, Thioredoxins.
- chemical : Glutaredoxins.
- metabolism : Escherichia coli.
- Electron Transport, Kinetics, Substrate Specificity.
Abstract
Reduction of inorganic sulfate to sulfite in prototrophic bacteria occurs with 3'-phosphoadenylylsulfate (PAPS) as substrate for PAPS reductase and is the first step leading to reduced sulfur for cellular biosynthetic reactions. The relative efficiency as reductants of homogeneous highly active PAPS reductase of the newly identified second thioredoxin (Trx2) and glutaredoxins (Grx1, Grx2, Grx3, and a mutant Grx1C14S) was compared with the well known thioredoxin (Trx1) from Escherichia coli. Trx1, Trx2, and Grx1 supported virtually identical rates of sulfite formation with a Vmax ranging from 6.6 units mg-1 (Trx1) to 5.1 units mg-1 (Grx1), whereas Grx1C14S was only marginally active, and Grx2 and Grx3 had no activity. The structural difference between active reductants had no effect upon Km PAPS (22.5 microM). Grx1 effectively replaced Trx1 with essentially identical Km-values: Km trx1 (13.7 microM), Km grx1 (14.9 microM), whereas the Km trx2 was considerably higher (34.2 microM). The results agree with previous in vivo data suggesting that Trx1 or Grx1 is essential for sulfate reduction but not for ribonucleotide reduction in E. coli.
DOI: 10.1074/jbc.274.12.7695
PubMed: 10075658
Affiliations:
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Prior</name></author><author><name sortKey="Schwenn, J D" sort="Schwenn, J D" uniqKey="Schwenn J" first="J D" last="Schwenn">J D Schwenn</name></author><author><name sortKey="Aslund, F" sort="Aslund, F" uniqKey="Aslund F" first="F" last="Aslund">F. Aslund</name></author><author><name sortKey="Ritz, D" sort="Ritz, D" uniqKey="Ritz D" first="D" last="Ritz">D. Ritz</name></author><author><name sortKey="Vlamis Gardikas, A" sort="Vlamis Gardikas, A" uniqKey="Vlamis Gardikas A" first="A" last="Vlamis-Gardikas">A. Vlamis-Gardikas</name></author><author><name sortKey="Holmgren, A" sort="Holmgren, A" uniqKey="Holmgren A" first="A" last="Holmgren">A. Holmgren</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="1999">1999</date><idno type="RBID">pubmed:10075658</idno><idno type="pmid">10075658</idno><idno type="doi">10.1074/jbc.274.12.7695</idno><idno type="wicri:Area/Main/Corpus">001114</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">001114</idno><idno type="wicri:Area/Main/Curation">001114</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">001114</idno><idno type="wicri:Area/Main/Exploration">001114</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">New thioredoxins and glutaredoxins as electron donors of 3'-phosphoadenylylsulfate reductase.</title><author><name sortKey="Lillig, C H" sort="Lillig, C H" uniqKey="Lillig C" first="C H" last="Lillig">C H Lillig</name><affiliation wicri:level="1"><nlm:affiliation>Biochemistry of Plants, Faculty of Biology, Ruhr-University, 44780 Bochum, Germany.</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>Biochemistry of Plants, Faculty of Biology, Ruhr-University, 44780 Bochum</wicri:regionArea><wicri:noRegion>44780 Bochum</wicri:noRegion><wicri:noRegion>44780 Bochum</wicri:noRegion><wicri:noRegion>44780 Bochum</wicri:noRegion></affiliation></author><author><name sortKey="Prior, A" sort="Prior, A" uniqKey="Prior A" first="A" last="Prior">A. Prior</name></author><author><name sortKey="Schwenn, J D" sort="Schwenn, J D" uniqKey="Schwenn J" first="J D" last="Schwenn">J D Schwenn</name></author><author><name sortKey="Aslund, F" sort="Aslund, F" uniqKey="Aslund F" first="F" last="Aslund">F. Aslund</name></author><author><name sortKey="Ritz, D" sort="Ritz, D" uniqKey="Ritz D" first="D" last="Ritz">D. Ritz</name></author><author><name sortKey="Vlamis Gardikas, A" sort="Vlamis Gardikas, A" uniqKey="Vlamis Gardikas A" first="A" last="Vlamis-Gardikas">A. Vlamis-Gardikas</name></author><author><name sortKey="Holmgren, A" sort="Holmgren, A" uniqKey="Holmgren A" first="A" last="Holmgren">A. Holmgren</name></author></analytic><series><title level="j">The Journal of biological chemistry</title><idno type="ISSN">0021-9258</idno><imprint><date when="1999" type="published">1999</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Electron Transport (MeSH)</term><term>Escherichia coli (metabolism)</term><term>Glutaredoxins (MeSH)</term><term>Kinetics (MeSH)</term><term>Oxidoreductases (metabolism)</term><term>Proteins (metabolism)</term><term>Ribonucleotides (metabolism)</term><term>Substrate Specificity (MeSH)</term><term>Sulfates (metabolism)</term><term>Thioredoxins (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Cinétique (MeSH)</term><term>Escherichia coli (métabolisme)</term><term>Glutarédoxines (MeSH)</term><term>Oxidoreductases (métabolisme)</term><term>Protéines (métabolisme)</term><term>Ribonucléotides (métabolisme)</term><term>Spécificité du substrat (MeSH)</term><term>Sulfates (métabolisme)</term><term>Thiorédoxines (métabolisme)</term><term>Transport d'électrons (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Oxidoreductases</term><term>Proteins</term><term>Ribonucleotides</term><term>Sulfates</term><term>Thioredoxins</term></keywords><keywords scheme="MESH" type="chemical" xml:lang="en"><term>Glutaredoxins</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>Oxidoreductases</term><term>Protéines</term><term>Ribonucléotides</term><term>Sulfates</term><term>Thiorédoxines</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Electron Transport</term><term>Kinetics</term><term>Substrate Specificity</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Cinétique</term><term>Glutarédoxines</term><term>Spécificité du substrat</term><term>Transport d'électrons</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Reduction of inorganic sulfate to sulfite in prototrophic bacteria occurs with 3'-phosphoadenylylsulfate (PAPS) as substrate for PAPS reductase and is the first step leading to reduced sulfur for cellular biosynthetic reactions. The relative efficiency as reductants of homogeneous highly active PAPS reductase of the newly identified second thioredoxin (Trx2) and glutaredoxins (Grx1, Grx2, Grx3, and a mutant Grx1C14S) was compared with the well known thioredoxin (Trx1) from Escherichia coli. Trx1, Trx2, and Grx1 supported virtually identical rates of sulfite formation with a Vmax ranging from 6.6 units mg-1 (Trx1) to 5.1 units mg-1 (Grx1), whereas Grx1C14S was only marginally active, and Grx2 and Grx3 had no activity. The structural difference between active reductants had no effect upon Km PAPS (22.5 microM). Grx1 effectively replaced Trx1 with essentially identical Km-values: Km trx1 (13.7 microM), Km grx1 (14.9 microM), whereas the Km trx2 was considerably higher (34.2 microM). The results agree with previous in vivo data suggesting that Trx1 or Grx1 is essential for sulfate reduction but not for ribonucleotide reduction in E. coli.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">10075658</PMID><DateCompleted><Year>1999</Year><Month>04</Month><Day>15</Day></DateCompleted><DateRevised><Year>2019</Year><Month>05</Month><Day>08</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0021-9258</ISSN><JournalIssue CitedMedium="Print"><Volume>274</Volume><Issue>12</Issue><PubDate><Year>1999</Year><Month>Mar</Month><Day>19</Day></PubDate></JournalIssue><Title>The Journal of biological chemistry</Title><ISOAbbreviation>J Biol Chem</ISOAbbreviation></Journal><ArticleTitle>New thioredoxins and glutaredoxins as electron donors of 3'-phosphoadenylylsulfate reductase.</ArticleTitle><Pagination><MedlinePgn>7695-8</MedlinePgn></Pagination><Abstract><AbstractText>Reduction of inorganic sulfate to sulfite in prototrophic bacteria occurs with 3'-phosphoadenylylsulfate (PAPS) as substrate for PAPS reductase and is the first step leading to reduced sulfur for cellular biosynthetic reactions. The relative efficiency as reductants of homogeneous highly active PAPS reductase of the newly identified second thioredoxin (Trx2) and glutaredoxins (Grx1, Grx2, Grx3, and a mutant Grx1C14S) was compared with the well known thioredoxin (Trx1) from Escherichia coli. Trx1, Trx2, and Grx1 supported virtually identical rates of sulfite formation with a Vmax ranging from 6.6 units mg-1 (Trx1) to 5.1 units mg-1 (Grx1), whereas Grx1C14S was only marginally active, and Grx2 and Grx3 had no activity. The structural difference between active reductants had no effect upon Km PAPS (22.5 microM). Grx1 effectively replaced Trx1 with essentially identical Km-values: Km trx1 (13.7 microM), Km grx1 (14.9 microM), whereas the Km trx2 was considerably higher (34.2 microM). The results agree with previous in vivo data suggesting that Trx1 or Grx1 is essential for sulfate reduction but not for ribonucleotide reduction in E. coli.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Lillig</LastName><ForeName>C H</ForeName><Initials>CH</Initials><AffiliationInfo><Affiliation>Biochemistry of Plants, Faculty of Biology, Ruhr-University, 44780 Bochum, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Prior</LastName><ForeName>A</ForeName><Initials>A</Initials></Author><Author ValidYN="Y"><LastName>Schwenn</LastName><ForeName>J D</ForeName><Initials>JD</Initials></Author><Author ValidYN="Y"><LastName>Aslund</LastName><ForeName>F</ForeName><Initials>F</Initials></Author><Author ValidYN="Y"><LastName>Ritz</LastName><ForeName>D</ForeName><Initials>D</Initials></Author><Author ValidYN="Y"><LastName>Vlamis-Gardikas</LastName><ForeName>A</ForeName><Initials>A</Initials></Author><Author ValidYN="Y"><LastName>Holmgren</LastName><ForeName>A</ForeName><Initials>A</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>J Biol Chem</MedlineTA><NlmUniqueID>2985121R</NlmUniqueID><ISSNLinking>0021-9258</ISSNLinking></MedlineJournalInfo><ChemicalList><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="D012265">Ribonucleotides</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D013431">Sulfates</NameOfSubstance></Chemical><Chemical><RegistryNumber>52500-60-4</RegistryNumber><NameOfSubstance UI="D013879">Thioredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.-</RegistryNumber><NameOfSubstance UI="D010088">Oxidoreductases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.8.4.-</RegistryNumber><NameOfSubstance UI="C052449">3'-phosphoadenylyl-5'-phosphosulfate reductase</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D004579" MajorTopicYN="N">Electron Transport</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004926" MajorTopicYN="N">Escherichia coli</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D054477" MajorTopicYN="N">Glutaredoxins</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007700" MajorTopicYN="N">Kinetics</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010088" MajorTopicYN="N">Oxidoreductases</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011506" MajorTopicYN="N">Proteins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D012265" MajorTopicYN="N">Ribonucleotides</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013379" MajorTopicYN="N">Substrate Specificity</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013431" MajorTopicYN="N">Sulfates</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013879" MajorTopicYN="N">Thioredoxins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>1999</Year><Month>3</Month><Day>13</Day></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>1999</Year><Month>3</Month><Day>13</Day><Hour>0</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>1999</Year><Month>3</Month><Day>13</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">10075658</ArticleId><ArticleId IdType="doi">10.1074/jbc.274.12.7695</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Allemagne</li></country></list><tree><noCountry><name sortKey="Aslund, F" sort="Aslund, F" uniqKey="Aslund F" first="F" last="Aslund">F. Aslund</name><name sortKey="Holmgren, A" sort="Holmgren, A" uniqKey="Holmgren A" first="A" last="Holmgren">A. Holmgren</name><name sortKey="Prior, A" sort="Prior, A" uniqKey="Prior A" first="A" last="Prior">A. Prior</name><name sortKey="Ritz, D" sort="Ritz, D" uniqKey="Ritz D" first="D" last="Ritz">D. Ritz</name><name sortKey="Schwenn, J D" sort="Schwenn, J D" uniqKey="Schwenn J" first="J D" last="Schwenn">J D Schwenn</name><name sortKey="Vlamis Gardikas, A" sort="Vlamis Gardikas, A" uniqKey="Vlamis Gardikas A" first="A" last="Vlamis-Gardikas">A. Vlamis-Gardikas</name></noCountry><country name="Allemagne"><noRegion><name sortKey="Lillig, C H" sort="Lillig, C H" uniqKey="Lillig C" first="C H" last="Lillig">C H Lillig</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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