Catalytic mechanism of thioltransferase.
Identifieur interne : 001307 ( Main/Exploration ); précédent : 001306; suivant : 001308Catalytic mechanism of thioltransferase.
Auteurs : Y F Yang [États-Unis] ; W W WellsSource :
- The Journal of biological chemistry [ 0021-9258 ] ; 1991.
Descripteurs français
- KwdFr :
- 2-Iodo-acétamide (pharmacologie), Animaux (MeSH), Autoradiographie (MeSH), Catalyse (MeSH), Focalisation isoélectrique (MeSH), Foie (enzymologie), Glutarédoxines (MeSH), Oxidoreductases (antagonistes et inhibiteurs), Oxidoreductases (métabolisme), Protein-disulfide reductase (glutathione) (MeSH), Suidae (MeSH), Électrophorèse sur gel de polyacrylamide (MeSH).
- MESH :
- antagonistes et inhibiteurs : Oxidoreductases.
- enzymologie : Foie.
- métabolisme : Oxidoreductases.
- pharmacologie : 2-Iodo-acétamide.
- Animaux, Autoradiographie, Catalyse, Focalisation isoélectrique, Glutarédoxines, Protein-disulfide reductase (glutathione), Suidae, Électrophorèse sur gel de polyacrylamide.
English descriptors
- KwdEn :
- Animals (MeSH), Autoradiography (MeSH), Catalysis (MeSH), Electrophoresis, Polyacrylamide Gel (MeSH), Glutaredoxins (MeSH), Iodoacetamide (pharmacology), Isoelectric Focusing (MeSH), Liver (enzymology), Oxidoreductases (antagonists & inhibitors), Oxidoreductases (metabolism), Protein Disulfide Reductase (Glutathione) (MeSH), Swine (MeSH).
- MESH :
- chemical , antagonists & inhibitors : Oxidoreductases.
- chemical , metabolism : Oxidoreductases.
- chemical , pharmacology : Iodoacetamide.
- chemical : Glutaredoxins, Protein Disulfide Reductase (Glutathione).
- enzymology : Liver.
- Animals, Autoradiography, Catalysis, Electrophoresis, Polyacrylamide Gel, Isoelectric Focusing, Swine.
Abstract
To evaluate potential catalytic mechanism for thioltransferase thiol-disulfide exchange reactions, seven pig liver mutants were constructed by site-directed mutagenesis. All the expressed enzymes, including wild-type and mutants with the exception of the inactive mutant, ETT-C22S, were variably inhibited by iodoacetamide, and similar results were obtained when these enzymes were preincubated with GSH. However, when preincubated with S-sulfocysteine or hydroxyethyl disulfide, the activity of the enzymes was totally or partially protected against inhibition by iodoacetamide, with the exception of the mutants, ETT-C25S and ETT-C25A. When simultaneously pretreated with GSH and S-sulfocysteine, all enzymes were highly protected. Isoelectric focusing analysis of the above preincubation mixtures showed that different enzyme-substrate intermediates occurred. Using radioactively labeled substrates, [U-14C]cystine and [glycine-2-3H] GSH, enzyme-substrate intermediates were detected. These data indicate that reduced thioltransferase reacts first with disulfide substrates, then with a thiol substrate, e.g. GSH. The formation of either enzyme-substrate mixed disulfide or protein intramolecular disulfide protected the enzyme from inactivation by iodoacetamide. Based on the experimental results, alternative methods of the catalytic mechanism for thioltransferases are proposed.
PubMed: 2061339
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Catalytic mechanism of thioltransferase.</title><author><name sortKey="Yang, Y F" sort="Yang, Y F" uniqKey="Yang Y" first="Y F" last="Yang">Y F Yang</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="Wells, W W" sort="Wells, W W" uniqKey="Wells W" first="W W" last="Wells">W W Wells</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="1991">1991</date><idno type="RBID">pubmed:2061339</idno><idno type="pmid">2061339</idno><idno type="wicri:Area/Main/Corpus">001299</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">001299</idno><idno type="wicri:Area/Main/Curation">001299</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">001299</idno><idno type="wicri:Area/Main/Exploration">001299</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Catalytic mechanism of thioltransferase.</title><author><name sortKey="Yang, Y F" sort="Yang, Y F" uniqKey="Yang Y" first="Y F" last="Yang">Y F Yang</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="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">The Journal of biological chemistry</title><idno type="ISSN">0021-9258</idno><imprint><date when="1991" type="published">1991</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals (MeSH)</term><term>Autoradiography (MeSH)</term><term>Catalysis (MeSH)</term><term>Electrophoresis, Polyacrylamide Gel (MeSH)</term><term>Glutaredoxins (MeSH)</term><term>Iodoacetamide (pharmacology)</term><term>Isoelectric Focusing (MeSH)</term><term>Liver (enzymology)</term><term>Oxidoreductases (antagonists & inhibitors)</term><term>Oxidoreductases (metabolism)</term><term>Protein Disulfide Reductase (Glutathione) (MeSH)</term><term>Swine (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>2-Iodo-acétamide (pharmacologie)</term><term>Animaux (MeSH)</term><term>Autoradiographie (MeSH)</term><term>Catalyse (MeSH)</term><term>Focalisation isoélectrique (MeSH)</term><term>Foie (enzymologie)</term><term>Glutarédoxines (MeSH)</term><term>Oxidoreductases (antagonistes et inhibiteurs)</term><term>Oxidoreductases (métabolisme)</term><term>Protein-disulfide reductase (glutathione) (MeSH)</term><term>Suidae (MeSH)</term><term>Électrophorèse sur gel de polyacrylamide (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="antagonists & inhibitors" xml:lang="en"><term>Oxidoreductases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Oxidoreductases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Iodoacetamide</term></keywords><keywords scheme="MESH" type="chemical" xml:lang="en"><term>Glutaredoxins</term><term>Protein Disulfide Reductase (Glutathione)</term></keywords><keywords scheme="MESH" qualifier="antagonistes et inhibiteurs" xml:lang="fr"><term>Oxidoreductases</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Foie</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Liver</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Oxidoreductases</term></keywords><keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>2-Iodo-acétamide</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Autoradiography</term><term>Catalysis</term><term>Electrophoresis, Polyacrylamide Gel</term><term>Isoelectric Focusing</term><term>Swine</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Autoradiographie</term><term>Catalyse</term><term>Focalisation isoélectrique</term><term>Glutarédoxines</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">To evaluate potential catalytic mechanism for thioltransferase thiol-disulfide exchange reactions, seven pig liver mutants were constructed by site-directed mutagenesis. All the expressed enzymes, including wild-type and mutants with the exception of the inactive mutant, ETT-C22S, were variably inhibited by iodoacetamide, and similar results were obtained when these enzymes were preincubated with GSH. However, when preincubated with S-sulfocysteine or hydroxyethyl disulfide, the activity of the enzymes was totally or partially protected against inhibition by iodoacetamide, with the exception of the mutants, ETT-C25S and ETT-C25A. When simultaneously pretreated with GSH and S-sulfocysteine, all enzymes were highly protected. Isoelectric focusing analysis of the above preincubation mixtures showed that different enzyme-substrate intermediates occurred. Using radioactively labeled substrates, [U-14C]cystine and [glycine-2-3H] GSH, enzyme-substrate intermediates were detected. These data indicate that reduced thioltransferase reacts first with disulfide substrates, then with a thiol substrate, e.g. GSH. The formation of either enzyme-substrate mixed disulfide or protein intramolecular disulfide protected the enzyme from inactivation by iodoacetamide. Based on the experimental results, alternative methods of the catalytic mechanism for thioltransferases are proposed.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">2061339</PMID><DateCompleted><Year>1991</Year><Month>08</Month><Day>07</Day></DateCompleted><DateRevised><Year>2013</Year><Month>11</Month><Day>21</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0021-9258</ISSN><JournalIssue CitedMedium="Print"><Volume>266</Volume><Issue>19</Issue><PubDate><Year>1991</Year><Month>Jul</Month><Day>05</Day></PubDate></JournalIssue><Title>The Journal of biological chemistry</Title><ISOAbbreviation>J Biol Chem</ISOAbbreviation></Journal><ArticleTitle>Catalytic mechanism of thioltransferase.</ArticleTitle><Pagination><MedlinePgn>12766-71</MedlinePgn></Pagination><Abstract><AbstractText>To evaluate potential catalytic mechanism for thioltransferase thiol-disulfide exchange reactions, seven pig liver mutants were constructed by site-directed mutagenesis. All the expressed enzymes, including wild-type and mutants with the exception of the inactive mutant, ETT-C22S, were variably inhibited by iodoacetamide, and similar results were obtained when these enzymes were preincubated with GSH. However, when preincubated with S-sulfocysteine or hydroxyethyl disulfide, the activity of the enzymes was totally or partially protected against inhibition by iodoacetamide, with the exception of the mutants, ETT-C25S and ETT-C25A. When simultaneously pretreated with GSH and S-sulfocysteine, all enzymes were highly protected. Isoelectric focusing analysis of the above preincubation mixtures showed that different enzyme-substrate intermediates occurred. Using radioactively labeled substrates, [U-14C]cystine and [glycine-2-3H] GSH, enzyme-substrate intermediates were detected. These data indicate that reduced thioltransferase reacts first with disulfide substrates, then with a thiol substrate, e.g. GSH. The formation of either enzyme-substrate mixed disulfide or protein intramolecular disulfide protected the enzyme from inactivation by iodoacetamide. Based on the experimental results, alternative methods of the catalytic mechanism for thioltransferases are proposed.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Yang</LastName><ForeName>Y F</ForeName><Initials>YF</Initials><AffiliationInfo><Affiliation>Department of Biochemistry, Michigan State University, East Lansing 48824.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Wells</LastName><ForeName>W W</ForeName><Initials>WW</Initials></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>CA-51937</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>EC 1.-</RegistryNumber><NameOfSubstance UI="D010088">Oxidoreductases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.8.4.2</RegistryNumber><NameOfSubstance UI="D011490">Protein Disulfide Reductase (Glutathione)</NameOfSubstance></Chemical><Chemical><RegistryNumber>ZRH8M27S79</RegistryNumber><NameOfSubstance UI="D007460">Iodoacetamide</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D001345" MajorTopicYN="N">Autoradiography</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002384" MajorTopicYN="N">Catalysis</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004591" MajorTopicYN="N">Electrophoresis, Polyacrylamide Gel</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D054477" MajorTopicYN="N">Glutaredoxins</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007460" MajorTopicYN="N">Iodoacetamide</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D007525" MajorTopicYN="N">Isoelectric Focusing</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008099" MajorTopicYN="N">Liver</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010088" MajorTopicYN="N">Oxidoreductases</DescriptorName><QualifierName UI="Q000037" MajorTopicYN="N">antagonists & inhibitors</QualifierName><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>1991</Year><Month>7</Month><Day>5</Day></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>1991</Year><Month>7</Month><Day>5</Day><Hour>0</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>1991</Year><Month>7</Month><Day>5</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">2061339</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="Yang, Y F" sort="Yang, Y F" uniqKey="Yang Y" first="Y F" last="Yang">Y F Yang</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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