Thioltransferases.
Identifieur interne : 001258 ( Main/Exploration ); précédent : 001257; suivant : 001259Thioltransferases.
Auteurs : W W Wells [États-Unis] ; Y. Yang ; T L Deits ; Z R GanSource :
- Advances in enzymology and related areas of molecular biology [ 0065-258X ] ; 1993.
Descripteurs français
- KwdFr :
- Cellules eucaryotes (enzymologie), Cellules procaryotes (enzymologie), Données de séquences moléculaires (MeSH), Glutarédoxines (MeSH), Oxidoreductases (génétique), Oxidoreductases (métabolisme), Protein-disulfide reductase (glutathione) (MeSH), Similitude de séquences d'acides aminés (MeSH), Séquence d'acides aminés (MeSH), Séquence nucléotidique (MeSH).
- MESH :
- enzymologie : Cellules eucaryotes, Cellules procaryotes.
- génétique : Oxidoreductases.
- métabolisme : Oxidoreductases.
- Données de séquences moléculaires, Glutarédoxines, Protein-disulfide reductase (glutathione), Similitude de séquences d'acides aminés, Séquence d'acides aminés, Séquence nucléotidique.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Base Sequence (MeSH), Eukaryotic Cells (enzymology), Glutaredoxins (MeSH), Molecular Sequence Data (MeSH), Oxidoreductases (genetics), Oxidoreductases (metabolism), Prokaryotic Cells (enzymology), Protein Disulfide Reductase (Glutathione) (MeSH), Sequence Homology, Amino Acid (MeSH).
- MESH :
- chemical , genetics : Oxidoreductases.
- chemical , metabolism : Oxidoreductases.
- chemical : Glutaredoxins, Protein Disulfide Reductase (Glutathione).
- enzymology : Eukaryotic Cells, Prokaryotic Cells.
- Amino Acid Sequence, Base Sequence, Molecular Sequence Data, Sequence Homology, Amino Acid.
Abstract
A family of small molecular weight proteins with thiol-disulfide exchange activity have been discovered, widely distributed from E. coli to mammalian systems, called thioltransferases or glutaredoxins. There are no substantiated reports of thioltransferases-glutaredoxins in plants; however, partially purified dehydroascorbate reductase from peas had thiol-disulfide exchange catalytic activity using glutathione as reductant and S-sulfocysteine as thiosulfate cosubstrate (unpublished data). Thus, this class of proteins is universally distributed. Based on mutagenesis studies, a sequence of Cys-Pro-Tyr(Phe)-Cys- followed by Arg-Lys- or Lys alone is critical for both the thiol-disulfide exchange reaction and the dehydroascorbate reductase activity. The dithiol-disulfide loop represented by this structure is unique since the cystine closer to the N-terminus has a highly acidic thiol pKa (3.8 as determined for the pig liver enzyme) that contributes to the protein's high S- nucleophilicity. Compared with the microbial enzyme, the mammalian thioltransferases (glutaredoxins) are extended at both N and C termini by 10-12 amino acid residues, including a second pair of cysteines toward the C-terminus with no known special function. Yeast thioltransferase is more like mammalian enzymes in length (106 amino acids) but more like E. coli glutaredoxin in being unblocked at the N-terminus and having only one set of cysteines; that is, at the active center. The three mammalian enzymes, for which sequences are available, are blocked at the N-terminus by an acetyl group linked to alanine with no known special function other than possibly to impart greater cellular turnover stability. A report of carbohydrate (8.6%) content in rat liver thioltransferase has not been verified by more sensitive methods of carbohydrate analysis, nor has carbohydrate been identified in samples of purified glutaredoxin from any source. Thiol transferase and glutaredoxin are two names for the same protein based on similarity of amino acid sequence, immunochemical cross-reactivity, and other enzyme properties. The inability of thioltransferase from some mammalian sources to act as an electron carrier in ribonucleotide reductase systems, whether homologous or heterologous in origin, remains to be explained in future studies.
DOI: 10.1002/9780470123126.ch4
PubMed: 8430514
Affiliations:
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<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Thioltransferases.</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.</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="Yang, Y" sort="Yang, Y" uniqKey="Yang Y" first="Y" last="Yang">Y. Yang</name></author><author><name sortKey="Deits, T L" sort="Deits, T L" uniqKey="Deits T" first="T L" last="Deits">T L Deits</name></author><author><name sortKey="Gan, Z R" sort="Gan, Z R" uniqKey="Gan Z" first="Z R" last="Gan">Z R Gan</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="1993">1993</date><idno type="RBID">pubmed:8430514</idno><idno type="pmid">8430514</idno><idno type="doi">10.1002/9780470123126.ch4</idno><idno type="wicri:Area/Main/Corpus">001272</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">001272</idno><idno type="wicri:Area/Main/Curation">001272</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">001272</idno><idno type="wicri:Area/Main/Exploration">001272</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Thioltransferases.</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.</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="Yang, Y" sort="Yang, Y" uniqKey="Yang Y" first="Y" last="Yang">Y. Yang</name></author><author><name sortKey="Deits, T L" sort="Deits, T L" uniqKey="Deits T" first="T L" last="Deits">T L Deits</name></author><author><name sortKey="Gan, Z R" sort="Gan, Z R" uniqKey="Gan Z" first="Z R" last="Gan">Z R Gan</name></author></analytic><series><title level="j">Advances in enzymology and related areas of molecular biology</title><idno type="ISSN">0065-258X</idno><imprint><date when="1993" type="published">1993</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence (MeSH)</term><term>Base Sequence (MeSH)</term><term>Eukaryotic Cells (enzymology)</term><term>Glutaredoxins (MeSH)</term><term>Molecular Sequence Data (MeSH)</term><term>Oxidoreductases (genetics)</term><term>Oxidoreductases (metabolism)</term><term>Prokaryotic Cells (enzymology)</term><term>Protein Disulfide Reductase (Glutathione) (MeSH)</term><term>Sequence Homology, Amino Acid (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Cellules eucaryotes (enzymologie)</term><term>Cellules procaryotes (enzymologie)</term><term>Données de séquences moléculaires (MeSH)</term><term>Glutarédoxines (MeSH)</term><term>Oxidoreductases (génétique)</term><term>Oxidoreductases (métabolisme)</term><term>Protein-disulfide reductase (glutathione) (MeSH)</term><term>Similitude de séquences d'acides aminés (MeSH)</term><term>Séquence d'acides aminés (MeSH)</term><term>Séquence nucléotidique (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" 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" xml:lang="en"><term>Glutaredoxins</term><term>Protein Disulfide Reductase (Glutathione)</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Cellules eucaryotes</term><term>Cellules procaryotes</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Eukaryotic Cells</term><term>Prokaryotic Cells</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Oxidoreductases</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Oxidoreductases</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Base Sequence</term><term>Molecular Sequence Data</term><term>Sequence Homology, Amino Acid</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Données de séquences moléculaires</term><term>Glutarédoxines</term><term>Protein-disulfide reductase (glutathione)</term><term>Similitude de séquences d'acides aminés</term><term>Séquence d'acides aminés</term><term>Séquence nucléotidique</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">A family of small molecular weight proteins with thiol-disulfide exchange activity have been discovered, widely distributed from E. coli to mammalian systems, called thioltransferases or glutaredoxins. There are no substantiated reports of thioltransferases-glutaredoxins in plants; however, partially purified dehydroascorbate reductase from peas had thiol-disulfide exchange catalytic activity using glutathione as reductant and S-sulfocysteine as thiosulfate cosubstrate (unpublished data). Thus, this class of proteins is universally distributed. Based on mutagenesis studies, a sequence of Cys-Pro-Tyr(Phe)-Cys- followed by Arg-Lys- or Lys alone is critical for both the thiol-disulfide exchange reaction and the dehydroascorbate reductase activity. The dithiol-disulfide loop represented by this structure is unique since the cystine closer to the N-terminus has a highly acidic thiol pKa (3.8 as determined for the pig liver enzyme) that contributes to the protein's high S- nucleophilicity. Compared with the microbial enzyme, the mammalian thioltransferases (glutaredoxins) are extended at both N and C termini by 10-12 amino acid residues, including a second pair of cysteines toward the C-terminus with no known special function. Yeast thioltransferase is more like mammalian enzymes in length (106 amino acids) but more like E. coli glutaredoxin in being unblocked at the N-terminus and having only one set of cysteines; that is, at the active center. The three mammalian enzymes, for which sequences are available, are blocked at the N-terminus by an acetyl group linked to alanine with no known special function other than possibly to impart greater cellular turnover stability. A report of carbohydrate (8.6%) content in rat liver thioltransferase has not been verified by more sensitive methods of carbohydrate analysis, nor has carbohydrate been identified in samples of purified glutaredoxin from any source. Thiol transferase and glutaredoxin are two names for the same protein based on similarity of amino acid sequence, immunochemical cross-reactivity, and other enzyme properties. The inability of thioltransferase from some mammalian sources to act as an electron carrier in ribonucleotide reductase systems, whether homologous or heterologous in origin, remains to be explained in future studies.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">8430514</PMID><DateCompleted><Year>1993</Year><Month>03</Month><Day>10</Day></DateCompleted><DateRevised><Year>2019</Year><Month>11</Month><Day>01</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0065-258X</ISSN><JournalIssue CitedMedium="Print"><Volume>66</Volume><PubDate><Year>1993</Year></PubDate></JournalIssue><Title>Advances in enzymology and related areas of molecular biology</Title><ISOAbbreviation>Adv Enzymol Relat Areas Mol Biol</ISOAbbreviation></Journal><ArticleTitle>Thioltransferases.</ArticleTitle><Pagination><MedlinePgn>149-201</MedlinePgn></Pagination><Abstract><AbstractText>A family of small molecular weight proteins with thiol-disulfide exchange activity have been discovered, widely distributed from E. coli to mammalian systems, called thioltransferases or glutaredoxins. There are no substantiated reports of thioltransferases-glutaredoxins in plants; however, partially purified dehydroascorbate reductase from peas had thiol-disulfide exchange catalytic activity using glutathione as reductant and S-sulfocysteine as thiosulfate cosubstrate (unpublished data). Thus, this class of proteins is universally distributed. Based on mutagenesis studies, a sequence of Cys-Pro-Tyr(Phe)-Cys- followed by Arg-Lys- or Lys alone is critical for both the thiol-disulfide exchange reaction and the dehydroascorbate reductase activity. The dithiol-disulfide loop represented by this structure is unique since the cystine closer to the N-terminus has a highly acidic thiol pKa (3.8 as determined for the pig liver enzyme) that contributes to the protein's high S- nucleophilicity. Compared with the microbial enzyme, the mammalian thioltransferases (glutaredoxins) are extended at both N and C termini by 10-12 amino acid residues, including a second pair of cysteines toward the C-terminus with no known special function. Yeast thioltransferase is more like mammalian enzymes in length (106 amino acids) but more like E. coli glutaredoxin in being unblocked at the N-terminus and having only one set of cysteines; that is, at the active center. The three mammalian enzymes, for which sequences are available, are blocked at the N-terminus by an acetyl group linked to alanine with no known special function other than possibly to impart greater cellular turnover stability. A report of carbohydrate (8.6%) content in rat liver thioltransferase has not been verified by more sensitive methods of carbohydrate analysis, nor has carbohydrate been identified in samples of purified glutaredoxin from any source. Thiol transferase and glutaredoxin are two names for the same protein based on similarity of amino acid sequence, immunochemical cross-reactivity, and other enzyme properties. The inability of thioltransferase from some mammalian sources to act as an electron carrier in ribonucleotide reductase systems, whether homologous or heterologous in origin, remains to be explained in future studies.</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.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Yang</LastName><ForeName>Y</ForeName><Initials>Y</Initials></Author><Author ValidYN="Y"><LastName>Deits</LastName><ForeName>T L</ForeName><Initials>TL</Initials></Author><Author ValidYN="Y"><LastName>Gan</LastName><ForeName>Z R</ForeName><Initials>ZR</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></GrantList><PublicationTypeList><PublicationType UI="D003160">Comparative Study</PublicationType><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013486">Research Support, U.S. Gov't, Non-P.H.S.</PublicationType><PublicationType UI="D013487">Research Support, U.S. Gov't, P.H.S.</PublicationType><PublicationType UI="D016454">Review</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Adv Enzymol Relat Areas Mol Biol</MedlineTA><NlmUniqueID>0337243</NlmUniqueID><ISSNLinking>0065-258X</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></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D001483" MajorTopicYN="N">Base Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005057" MajorTopicYN="N">Eukaryotic Cells</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D054477" MajorTopicYN="N">Glutaredoxins</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></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="D011387" MajorTopicYN="N">Prokaryotic Cells</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011490" MajorTopicYN="Y">Protein Disulfide Reductase (Glutathione)</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017386" MajorTopicYN="N">Sequence Homology, Amino Acid</DescriptorName></MeshHeading></MeshHeadingList><NumberOfReferences>197</NumberOfReferences></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>1993</Year><Month>1</Month><Day>1</Day></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>1993</Year><Month>1</Month><Day>1</Day><Hour>0</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>1993</Year><Month>1</Month><Day>1</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">8430514</ArticleId><ArticleId IdType="doi">10.1002/9780470123126.ch4</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="Deits, T L" sort="Deits, T L" uniqKey="Deits T" first="T L" last="Deits">T L Deits</name><name sortKey="Gan, Z R" sort="Gan, Z R" uniqKey="Gan Z" first="Z R" last="Gan">Z R Gan</name><name sortKey="Yang, Y" sort="Yang, Y" uniqKey="Yang Y" first="Y" last="Yang">Y. 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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