Identification of the dehydroascorbic acid reductase and thioltransferase (Glutaredoxin) activities of bovine erythrocyte glutathione peroxidase.
Identifieur interne : 001105 ( Main/Exploration ); précédent : 001104; suivant : 001106Identification of the dehydroascorbic acid reductase and thioltransferase (Glutaredoxin) activities of bovine erythrocyte glutathione peroxidase.
Auteurs : M P Washburn [États-Unis] ; W W WellsSource :
- Biochemical and biophysical research communications [ 0006-291X ] ; 1999.
Descripteurs français
- KwdFr :
- Acide déhydroascorbique (métabolisme), Animaux (MeSH), Bovins (MeSH), Cinétique (MeSH), Cystéine (analogues et dérivés), Cystéine (métabolisme), Foie (enzymologie), Glutarédoxines (MeSH), Glutathion (métabolisme), Glutathione peroxidase (isolement et purification), Glutathione peroxidase (métabolisme), Humains (MeSH), Masse moléculaire (MeSH), Oxidoreductases (métabolisme), Protein-disulfide reductase (glutathione) (MeSH), Suidae (MeSH), Électrophorèse sur gel de polyacrylamide (MeSH), Érythrocytes (enzymologie).
- MESH :
- analogues et dérivés : Cystéine.
- enzymologie : Foie, Érythrocytes.
- isolement et purification : Glutathione peroxidase.
- métabolisme : Acide déhydroascorbique, Cystéine, Glutathion, Glutathione peroxidase, Oxidoreductases.
- Animaux, Bovins, Cinétique, Glutarédoxines, Humains, Masse moléculaire, Protein-disulfide reductase (glutathione), Suidae, Électrophorèse sur gel de polyacrylamide.
English descriptors
- KwdEn :
- Animals (MeSH), Cattle (MeSH), Cysteine (analogs & derivatives), Cysteine (metabolism), Dehydroascorbic Acid (metabolism), Electrophoresis, Polyacrylamide Gel (MeSH), Erythrocytes (enzymology), Glutaredoxins (MeSH), Glutathione (metabolism), Glutathione Peroxidase (isolation & purification), Glutathione Peroxidase (metabolism), Humans (MeSH), Kinetics (MeSH), Liver (enzymology), Molecular Weight (MeSH), Oxidoreductases (metabolism), Protein Disulfide Reductase (Glutathione) (MeSH), Swine (MeSH).
- MESH :
- chemical , analogs & derivatives : Cysteine.
- chemical , isolation & purification : Glutathione Peroxidase.
- chemical , metabolism : Cysteine, Dehydroascorbic Acid, Glutathione, Glutathione Peroxidase, Oxidoreductases.
- enzymology : Erythrocytes, Liver.
- Animals, Cattle, Electrophoresis, Polyacrylamide Gel, Glutaredoxins, Humans, Kinetics, Molecular Weight, Protein Disulfide Reductase (Glutathione), Swine.
Abstract
Bovine erythrocyte glutathione (GSH) peroxidase (GPX, EC 1.11.1.9) was examined for GSH-dependent dehydroascorbate (DHA) reductase (EC 1.8.5.1) and thioltransferase (EC 1.8.4.1) activities. Using the direct assay method for GSH-dependent DHA reductase activity, GPX had a kcat (app) of 140 +/- 9 min-1 and specificity constants (kcat/Km(app)) of 5.74 +/- 0.78 x 10(2) M-1s-1 for DHA and 1.18 +/- 0.17 x 10(3) M-1s-1 for GSH based on the monomer Mr of 22,612. Using the coupled assay method for thioltransferase activity, GPX had a kcat (app) of 186 +/- 9 min-1 and specificity constants (app) of 1. 49 +/- 0.14 x 10(3) M-1s-1 for S-sulfocysteine and 1.51 +/- 0.18 x 10(3) M-1s-1 for GSH based on the GPX monomer molecular weight. GPX has a higher specificity constant for S-sulfocysteine than DHA, and both assay systems gave nearly identical specificity constants for GSH. The DHA reductase and thioltransferase activities of GPX adds to the repertoire of functions of this enzyme as an important protector against cellular oxidative stress.
DOI: 10.1006/bbrc.1999.0508
PubMed: 10198252
Affiliations:
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Biochemistry, Michigan State University, East Lansing, Michigan, 48824, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Biochemistry, Michigan State University, East Lansing, Michigan, 48824</wicri:regionArea><orgName type="university">Université d'État du Michigan</orgName><placeName><settlement type="city">East Lansing</settlement><region type="state">Michigan</region></placeName></affiliation></author><author><name sortKey="Wells, W W" sort="Wells, W W" uniqKey="Wells W" first="W W" last="Wells">W W Wells</name></author></analytic><series><title level="j">Biochemical and biophysical research communications</title><idno type="ISSN">0006-291X</idno><imprint><date when="1999" type="published">1999</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals (MeSH)</term><term>Cattle (MeSH)</term><term>Cysteine (analogs & derivatives)</term><term>Cysteine (metabolism)</term><term>Dehydroascorbic Acid (metabolism)</term><term>Electrophoresis, Polyacrylamide Gel (MeSH)</term><term>Erythrocytes (enzymology)</term><term>Glutaredoxins (MeSH)</term><term>Glutathione (metabolism)</term><term>Glutathione Peroxidase (isolation & purification)</term><term>Glutathione Peroxidase (metabolism)</term><term>Humans (MeSH)</term><term>Kinetics (MeSH)</term><term>Liver (enzymology)</term><term>Molecular Weight (MeSH)</term><term>Oxidoreductases (metabolism)</term><term>Protein Disulfide Reductase (Glutathione) (MeSH)</term><term>Swine (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Acide déhydroascorbique (métabolisme)</term><term>Animaux (MeSH)</term><term>Bovins (MeSH)</term><term>Cinétique (MeSH)</term><term>Cystéine (analogues et dérivés)</term><term>Cystéine (métabolisme)</term><term>Foie (enzymologie)</term><term>Glutarédoxines (MeSH)</term><term>Glutathion (métabolisme)</term><term>Glutathione peroxidase (isolement et purification)</term><term>Glutathione peroxidase (métabolisme)</term><term>Humains (MeSH)</term><term>Masse moléculaire (MeSH)</term><term>Oxidoreductases (métabolisme)</term><term>Protein-disulfide reductase (glutathione) (MeSH)</term><term>Suidae (MeSH)</term><term>Électrophorèse sur gel de polyacrylamide (MeSH)</term><term>Érythrocytes (enzymologie)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="analogs & derivatives" xml:lang="en"><term>Cysteine</term></keywords><keywords scheme="MESH" type="chemical" qualifier="isolation & purification" xml:lang="en"><term>Glutathione Peroxidase</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Cysteine</term><term>Dehydroascorbic Acid</term><term>Glutathione</term><term>Glutathione Peroxidase</term><term>Oxidoreductases</term></keywords><keywords scheme="MESH" qualifier="analogues et dérivés" xml:lang="fr"><term>Cystéine</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Foie</term><term>Érythrocytes</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Erythrocytes</term><term>Liver</term></keywords><keywords scheme="MESH" qualifier="isolement et purification" xml:lang="fr"><term>Glutathione peroxidase</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Acide déhydroascorbique</term><term>Cystéine</term><term>Glutathion</term><term>Glutathione peroxidase</term><term>Oxidoreductases</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Cattle</term><term>Electrophoresis, Polyacrylamide Gel</term><term>Glutaredoxins</term><term>Humans</term><term>Kinetics</term><term>Molecular Weight</term><term>Protein Disulfide Reductase (Glutathione)</term><term>Swine</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Bovins</term><term>Cinétique</term><term>Glutarédoxines</term><term>Humains</term><term>Masse moléculaire</term><term>Protein-disulfide reductase (glutathione)</term><term>Suidae</term><term>Électrophorèse sur gel de polyacrylamide</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Bovine erythrocyte glutathione (GSH) peroxidase (GPX, EC 1.11.1.9) was examined for GSH-dependent dehydroascorbate (DHA) reductase (EC 1.8.5.1) and thioltransferase (EC 1.8.4.1) activities. Using the direct assay method for GSH-dependent DHA reductase activity, GPX had a kcat (app) of 140 +/- 9 min-1 and specificity constants (kcat/Km(app)) of 5.74 +/- 0.78 x 10(2) M-1s-1 for DHA and 1.18 +/- 0.17 x 10(3) M-1s-1 for GSH based on the monomer Mr of 22,612. Using the coupled assay method for thioltransferase activity, GPX had a kcat (app) of 186 +/- 9 min-1 and specificity constants (app) of 1. 49 +/- 0.14 x 10(3) M-1s-1 for S-sulfocysteine and 1.51 +/- 0.18 x 10(3) M-1s-1 for GSH based on the GPX monomer molecular weight. GPX has a higher specificity constant for S-sulfocysteine than DHA, and both assay systems gave nearly identical specificity constants for GSH. The DHA reductase and thioltransferase activities of GPX adds to the repertoire of functions of this enzyme as an important protector against cellular oxidative stress.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">10198252</PMID><DateCompleted><Year>1999</Year><Month>05</Month><Day>24</Day></DateCompleted><DateRevised><Year>2017</Year><Month>11</Month><Day>16</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0006-291X</ISSN><JournalIssue CitedMedium="Print"><Volume>257</Volume><Issue>2</Issue><PubDate><Year>1999</Year><Month>Apr</Month><Day>13</Day></PubDate></JournalIssue><Title>Biochemical and biophysical research communications</Title><ISOAbbreviation>Biochem Biophys Res Commun</ISOAbbreviation></Journal><ArticleTitle>Identification of the dehydroascorbic acid reductase and thioltransferase (Glutaredoxin) activities of bovine erythrocyte glutathione peroxidase.</ArticleTitle><Pagination><MedlinePgn>567-71</MedlinePgn></Pagination><Abstract><AbstractText>Bovine erythrocyte glutathione (GSH) peroxidase (GPX, EC 1.11.1.9) was examined for GSH-dependent dehydroascorbate (DHA) reductase (EC 1.8.5.1) and thioltransferase (EC 1.8.4.1) activities. Using the direct assay method for GSH-dependent DHA reductase activity, GPX had a kcat (app) of 140 +/- 9 min-1 and specificity constants (kcat/Km(app)) of 5.74 +/- 0.78 x 10(2) M-1s-1 for DHA and 1.18 +/- 0.17 x 10(3) M-1s-1 for GSH based on the monomer Mr of 22,612. Using the coupled assay method for thioltransferase activity, GPX had a kcat (app) of 186 +/- 9 min-1 and specificity constants (app) of 1. 49 +/- 0.14 x 10(3) M-1s-1 for S-sulfocysteine and 1.51 +/- 0.18 x 10(3) M-1s-1 for GSH based on the GPX monomer molecular weight. GPX has a higher specificity constant for S-sulfocysteine than DHA, and both assay systems gave nearly identical specificity constants for GSH. The DHA reductase and thioltransferase activities of GPX adds to the repertoire of functions of this enzyme as an important protector against cellular oxidative stress.</AbstractText><CopyrightInformation>Copyright 1999 Academic Press.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Washburn</LastName><ForeName>M P</ForeName><Initials>MP</Initials><AffiliationInfo><Affiliation>Department of Biochemistry, Michigan State University, East Lansing, Michigan, 48824, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Wells</LastName><ForeName>W W</ForeName><Initials>WW</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D003160">Comparative Study</PublicationType><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="D054477">Glutaredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>885F2S42LL</RegistryNumber><NameOfSubstance UI="C011119">S-sulphocysteine</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.-</RegistryNumber><NameOfSubstance UI="D010088">Oxidoreductases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.11.1.9</RegistryNumber><NameOfSubstance UI="D005979">Glutathione Peroxidase</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.8.4.2</RegistryNumber><NameOfSubstance UI="D011490">Protein Disulfide Reductase (Glutathione)</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.8.5.1</RegistryNumber><NameOfSubstance UI="C020666">glutathione dehydrogenase (ascorbate)</NameOfSubstance></Chemical><Chemical><RegistryNumber>GAN16C9B8O</RegistryNumber><NameOfSubstance UI="D005978">Glutathione</NameOfSubstance></Chemical><Chemical><RegistryNumber>K848JZ4886</RegistryNumber><NameOfSubstance UI="D003545">Cysteine</NameOfSubstance></Chemical><Chemical><RegistryNumber>Y2Z3ZTP9UM</RegistryNumber><NameOfSubstance UI="D003683">Dehydroascorbic Acid</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="D003545" MajorTopicYN="N">Cysteine</DescriptorName><QualifierName UI="Q000031" MajorTopicYN="N">analogs & derivatives</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D003683" MajorTopicYN="N">Dehydroascorbic 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MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007700" MajorTopicYN="N">Kinetics</DescriptorName></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="D011490" MajorTopicYN="Y">Protein Disulfide Reductase (Glutathione)</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013552" MajorTopicYN="N">Swine</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>1999</Year><Month>4</Month><Day>13</Day></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>1999</Year><Month>4</Month><Day>13</Day><Hour>0</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>1999</Year><Month>4</Month><Day>13</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">10198252</ArticleId><ArticleId IdType="pii">S0006-291X(99)90508-9</ArticleId><ArticleId IdType="doi">10.1006/bbrc.1999.0508</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="Wells, W W" sort="Wells, W W" uniqKey="Wells W" first="W W" last="Wells">W W Wells</name></noCountry><country name="États-Unis"><region name="Michigan"><name sortKey="Washburn, M P" sort="Washburn, M P" uniqKey="Washburn M" first="M P" 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