Mammalian thioltransferase (glutaredoxin) and protein disulfide isomerase have dehydroascorbate reductase activity.
Identifieur interne : 001317 ( Main/Exploration ); précédent : 001316; suivant : 001318Mammalian thioltransferase (glutaredoxin) and protein disulfide isomerase have dehydroascorbate reductase activity.
Auteurs : W W Wells [États-Unis] ; D P Xu ; Y F Yang ; P A RocqueSource :
- The Journal of biological chemistry [ 0021-9258 ] ; 1990.
Descripteurs français
- KwdFr :
- Animaux (MeSH), Bovins (MeSH), Femelle (MeSH), Foie (enzymologie), Glutarédoxines (MeSH), Grossesse (MeSH), Humains (MeSH), Isomerases (métabolisme), Masse moléculaire (MeSH), Oxidoreductases (métabolisme), Placenta (enzymologie), Protein Disulfide-Isomerases (MeSH), Protéines (métabolisme), Protéines recombinantes (métabolisme), Suidae (MeSH), Thiorédoxines (isolement et purification), Thiorédoxines (métabolisme), Thymus (glande) (enzymologie).
- MESH :
- enzymologie : Foie, Placenta, Thymus (glande).
- isolement et purification : Thiorédoxines.
- métabolisme : Isomerases, Oxidoreductases, Protéines, Protéines recombinantes, Thiorédoxines.
- Animaux, Bovins, Femelle, Glutarédoxines, Grossesse, Humains, Masse moléculaire, Protein Disulfide-Isomerases, Suidae.
English descriptors
- KwdEn :
- Animals (MeSH), Cattle (MeSH), Female (MeSH), Glutaredoxins (MeSH), Humans (MeSH), Isomerases (metabolism), Liver (enzymology), Molecular Weight (MeSH), Oxidoreductases (metabolism), Placenta (enzymology), Pregnancy (MeSH), Protein Disulfide-Isomerases (MeSH), Proteins (metabolism), Recombinant Proteins (metabolism), Swine (MeSH), Thioredoxins (isolation & purification), Thioredoxins (metabolism), Thymus Gland (enzymology).
- MESH :
- chemical , isolation & purification : Thioredoxins.
- chemical , metabolism : Isomerases, Oxidoreductases, Proteins, Recombinant Proteins, Thioredoxins.
- chemical : Glutaredoxins, Protein Disulfide-Isomerases.
- enzymology : Liver, Placenta, Thymus Gland.
- Animals, Cattle, Female, Humans, Molecular Weight, Pregnancy, Swine.
Abstract
Homogeneous native and recombinant porcine liver thioltransferase (glutaredoxin), bovine thymus and human placenta thioltransferase (glutaredoxin) were examined for dehydroascorbate reductase activity (EC 1.8.5.1) involving the direct catalytic reduction of dehydroascorbic acid (DHA) by glutathione. Each enzyme had substantial activity with apparent Km and Vmax for dehydroascorbate between 0.2 and 2.2 mM and 6-27 nmol min-1, respectively, and for gluathione between 1.6 and 8.7 mM and 11-30 nmol min-1, respectively. In the presence of purified bovine liver thioredoxin reductase, homogeneous bovine liver thioredoxin failed to reduce DHA to ascorbic acid as measured by NADPH oxidation. Highly purified bovine liver protein disulfide isomerase (PDI) reacted directly with DHA and GSH to catalyze the reduction of DHA to ascorbic acid. The apparent Km for DHA was 1.0 mM and the Vmax was 8 nmol min-1, and for GSH were 3.9 mM and 14 nmol min-1, respectively. These results suggest that thioltransferase and PDI contribute to the regeneration of oxidized ascorbic acid in mammalian cells, and based on their cellular location, thioltransferase is proposed to be the major cytoplasmic activity, whereas interaction of DHA with microsomal membrane PDI may catalyze regeneration of ascorbic acid and initiate oxidation of intralumenal protein thiols to disulfides.
PubMed: 2394726
Affiliations:
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Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Mammalian thioltransferase (glutaredoxin) and protein disulfide isomerase have dehydroascorbate reductase activity.</title><author><name sortKey="Wells, W W" sort="Wells, W W" uniqKey="Wells W" first="W W" last="Wells">W W Wells</name><affiliation wicri:level="4"><nlm:affiliation>Department of Biochemistry, Michigan State University, East Lansing 48824.</nlm:affiliation><orgName type="university">Université d'État du Michigan</orgName><country>États-Unis</country><placeName><settlement type="city">East Lansing</settlement><region type="state">Michigan</region></placeName></affiliation></author><author><name sortKey="Xu, D P" sort="Xu, D P" uniqKey="Xu D" first="D P" last="Xu">D P Xu</name></author><author><name sortKey="Yang, Y F" sort="Yang, Y F" uniqKey="Yang Y" first="Y F" last="Yang">Y F Yang</name></author><author><name sortKey="Rocque, P A" sort="Rocque, P A" uniqKey="Rocque P" first="P A" last="Rocque">P A Rocque</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="1990">1990</date><idno type="RBID">pubmed:2394726</idno><idno type="pmid">2394726</idno><idno type="wicri:Area/Main/Corpus">001311</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">001311</idno><idno type="wicri:Area/Main/Curation">001311</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">001311</idno><idno type="wicri:Area/Main/Exploration">001311</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Mammalian thioltransferase (glutaredoxin) and protein disulfide isomerase have dehydroascorbate reductase activity.</title><author><name sortKey="Wells, W W" sort="Wells, W W" uniqKey="Wells W" first="W W" last="Wells">W W Wells</name><affiliation wicri:level="4"><nlm:affiliation>Department of Biochemistry, Michigan State University, East Lansing 48824.</nlm:affiliation><orgName type="university">Université d'État du Michigan</orgName><country>États-Unis</country><placeName><settlement type="city">East Lansing</settlement><region type="state">Michigan</region></placeName></affiliation></author><author><name sortKey="Xu, D P" sort="Xu, D P" uniqKey="Xu D" first="D P" last="Xu">D P Xu</name></author><author><name sortKey="Yang, Y F" sort="Yang, Y F" uniqKey="Yang Y" first="Y F" last="Yang">Y F Yang</name></author><author><name sortKey="Rocque, P A" sort="Rocque, P A" uniqKey="Rocque P" first="P A" last="Rocque">P A Rocque</name></author></analytic><series><title level="j">The Journal of biological chemistry</title><idno type="ISSN">0021-9258</idno><imprint><date when="1990" type="published">1990</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals (MeSH)</term><term>Cattle (MeSH)</term><term>Female (MeSH)</term><term>Glutaredoxins (MeSH)</term><term>Humans (MeSH)</term><term>Isomerases (metabolism)</term><term>Liver (enzymology)</term><term>Molecular Weight (MeSH)</term><term>Oxidoreductases (metabolism)</term><term>Placenta (enzymology)</term><term>Pregnancy (MeSH)</term><term>Protein Disulfide-Isomerases (MeSH)</term><term>Proteins (metabolism)</term><term>Recombinant Proteins (metabolism)</term><term>Swine (MeSH)</term><term>Thioredoxins (isolation & purification)</term><term>Thioredoxins (metabolism)</term><term>Thymus Gland (enzymology)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Animaux (MeSH)</term><term>Bovins (MeSH)</term><term>Femelle (MeSH)</term><term>Foie (enzymologie)</term><term>Glutarédoxines (MeSH)</term><term>Grossesse (MeSH)</term><term>Humains (MeSH)</term><term>Isomerases (métabolisme)</term><term>Masse moléculaire (MeSH)</term><term>Oxidoreductases (métabolisme)</term><term>Placenta (enzymologie)</term><term>Protein Disulfide-Isomerases (MeSH)</term><term>Protéines (métabolisme)</term><term>Protéines recombinantes (métabolisme)</term><term>Suidae (MeSH)</term><term>Thiorédoxines (isolement et purification)</term><term>Thiorédoxines (métabolisme)</term><term>Thymus (glande) (enzymologie)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="isolation & purification" xml:lang="en"><term>Thioredoxins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Isomerases</term><term>Oxidoreductases</term><term>Proteins</term><term>Recombinant Proteins</term><term>Thioredoxins</term></keywords><keywords scheme="MESH" type="chemical" xml:lang="en"><term>Glutaredoxins</term><term>Protein Disulfide-Isomerases</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Foie</term><term>Placenta</term><term>Thymus (glande)</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Liver</term><term>Placenta</term><term>Thymus Gland</term></keywords><keywords scheme="MESH" qualifier="isolement et purification" xml:lang="fr"><term>Thiorédoxines</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Isomerases</term><term>Oxidoreductases</term><term>Protéines</term><term>Protéines recombinantes</term><term>Thiorédoxines</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Cattle</term><term>Female</term><term>Humans</term><term>Molecular Weight</term><term>Pregnancy</term><term>Swine</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Bovins</term><term>Femelle</term><term>Glutarédoxines</term><term>Grossesse</term><term>Humains</term><term>Masse moléculaire</term><term>Protein Disulfide-Isomerases</term><term>Suidae</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Homogeneous native and recombinant porcine liver thioltransferase (glutaredoxin), bovine thymus and human placenta thioltransferase (glutaredoxin) were examined for dehydroascorbate reductase activity (EC 1.8.5.1) involving the direct catalytic reduction of dehydroascorbic acid (DHA) by glutathione. Each enzyme had substantial activity with apparent Km and Vmax for dehydroascorbate between 0.2 and 2.2 mM and 6-27 nmol min-1, respectively, and for gluathione between 1.6 and 8.7 mM and 11-30 nmol min-1, respectively. In the presence of purified bovine liver thioredoxin reductase, homogeneous bovine liver thioredoxin failed to reduce DHA to ascorbic acid as measured by NADPH oxidation. Highly purified bovine liver protein disulfide isomerase (PDI) reacted directly with DHA and GSH to catalyze the reduction of DHA to ascorbic acid. The apparent Km for DHA was 1.0 mM and the Vmax was 8 nmol min-1, and for GSH were 3.9 mM and 14 nmol min-1, respectively. These results suggest that thioltransferase and PDI contribute to the regeneration of oxidized ascorbic acid in mammalian cells, and based on their cellular location, thioltransferase is proposed to be the major cytoplasmic activity, whereas interaction of DHA with microsomal membrane PDI may catalyze regeneration of ascorbic acid and initiate oxidation of intralumenal protein thiols to disulfides.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">2394726</PMID><DateCompleted><Year>1990</Year><Month>10</Month><Day>11</Day></DateCompleted><DateRevised><Year>2008</Year><Month>11</Month><Day>21</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0021-9258</ISSN><JournalIssue CitedMedium="Print"><Volume>265</Volume><Issue>26</Issue><PubDate><Year>1990</Year><Month>Sep</Month><Day>15</Day></PubDate></JournalIssue><Title>The Journal of biological chemistry</Title><ISOAbbreviation>J Biol Chem</ISOAbbreviation></Journal><ArticleTitle>Mammalian thioltransferase (glutaredoxin) and protein disulfide isomerase have dehydroascorbate reductase activity.</ArticleTitle><Pagination><MedlinePgn>15361-4</MedlinePgn></Pagination><Abstract><AbstractText>Homogeneous native and recombinant porcine liver thioltransferase (glutaredoxin), bovine thymus and human placenta thioltransferase (glutaredoxin) were examined for dehydroascorbate reductase activity (EC 1.8.5.1) involving the direct catalytic reduction of dehydroascorbic acid (DHA) by glutathione. Each enzyme had substantial activity with apparent Km and Vmax for dehydroascorbate between 0.2 and 2.2 mM and 6-27 nmol min-1, respectively, and for gluathione between 1.6 and 8.7 mM and 11-30 nmol min-1, respectively. In the presence of purified bovine liver thioredoxin reductase, homogeneous bovine liver thioredoxin failed to reduce DHA to ascorbic acid as measured by NADPH oxidation. Highly purified bovine liver protein disulfide isomerase (PDI) reacted directly with DHA and GSH to catalyze the reduction of DHA to ascorbic acid. The apparent Km for DHA was 1.0 mM and the Vmax was 8 nmol min-1, and for GSH were 3.9 mM and 14 nmol min-1, respectively. These results suggest that thioltransferase and PDI contribute to the regeneration of oxidized ascorbic acid in mammalian cells, and based on their cellular location, thioltransferase is proposed to be the major cytoplasmic activity, whereas interaction of DHA with microsomal membrane PDI may catalyze regeneration of ascorbic acid and initiate oxidation of intralumenal protein thiols to disulfides.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Wells</LastName><ForeName>W W</ForeName><Initials>WW</Initials><AffiliationInfo><Affiliation>Department of Biochemistry, Michigan State University, East Lansing 48824.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Xu</LastName><ForeName>D P</ForeName><Initials>DP</Initials></Author><Author ValidYN="Y"><LastName>Yang</LastName><ForeName>Y F</ForeName><Initials>YF</Initials></Author><Author ValidYN="Y"><LastName>Rocque</LastName><ForeName>P A</ForeName><Initials>PA</Initials></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>CA-51972</GrantID><Acronym>CA</Acronym><Agency>NCI NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>GM-38634</GrantID><Acronym>GM</Acronym><Agency>NIGMS NIH HHS</Agency><Country>United States</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013487">Research Support, U.S. Gov't, P.H.S.</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="D011994">Recombinant Proteins</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 1.8.5.1</RegistryNumber><NameOfSubstance UI="C020666">glutathione dehydrogenase (ascorbate)</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 5.-</RegistryNumber><NameOfSubstance UI="D007535">Isomerases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 5.3.4.1</RegistryNumber><NameOfSubstance UI="D019704">Protein Disulfide-Isomerases</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002417" MajorTopicYN="N">Cattle</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005260" MajorTopicYN="N">Female</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D054477" MajorTopicYN="N">Glutaredoxins</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007535" MajorTopicYN="N">Isomerases</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008099" MajorTopicYN="N">Liver</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008970" MajorTopicYN="N">Molecular Weight</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010088" MajorTopicYN="N">Oxidoreductases</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010920" MajorTopicYN="N">Placenta</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011247" MajorTopicYN="N">Pregnancy</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D019704" MajorTopicYN="N">Protein Disulfide-Isomerases</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011506" MajorTopicYN="N">Proteins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011994" MajorTopicYN="N">Recombinant Proteins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013552" MajorTopicYN="N">Swine</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013879" MajorTopicYN="N">Thioredoxins</DescriptorName><QualifierName UI="Q000302" MajorTopicYN="N">isolation & purification</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013950" MajorTopicYN="N">Thymus Gland</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>1990</Year><Month>9</Month><Day>15</Day></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>1990</Year><Month>9</Month><Day>15</Day><Hour>0</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>1990</Year><Month>9</Month><Day>15</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">2394726</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>États-Unis</li></country><region><li>Michigan</li></region><settlement><li>East Lansing</li></settlement><orgName><li>Université d'État du Michigan</li></orgName></list><tree><noCountry><name sortKey="Rocque, P A" sort="Rocque, P A" uniqKey="Rocque P" first="P A" last="Rocque">P A Rocque</name><name sortKey="Xu, D P" sort="Xu, D P" uniqKey="Xu D" first="D P" last="Xu">D P Xu</name><name sortKey="Yang, Y F" sort="Yang, Y F" uniqKey="Yang Y" first="Y F" last="Yang">Y F Yang</name></noCountry><country name="États-Unis"><region name="Michigan"><name sortKey="Wells, W W" sort="Wells, W W" uniqKey="Wells W" first="W W" last="Wells">W W Wells</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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