Activation of 3-Mercaptopyruvate Sulfurtransferase by Glutaredoxin Reducing System.
Identifieur interne : 000093 ( Main/Exploration ); précédent : 000092; suivant : 000094Activation of 3-Mercaptopyruvate Sulfurtransferase by Glutaredoxin Reducing System.
Auteurs : Noriyuki Nagahara [Japon]Source :
- Biomolecules [ 2218-273X ] ; 2020.
Abstract
Glutaredoxin (EC 1.15-1.21) is known as an oxidoreductase that protects cysteine residues within proteins against oxidative stress. Glutaredoxin catalyzes an electron transfer reaction that donates an electron to substrate proteins in the reducing system composed of glutaredoxin, glutathione, glutathione reductase, and nicotinamide-adenine dinucleotide phosphate (reduced form). 3-mercaptopyruvate sulfurtransferase (EC 2.8.1.2) is a cysteine enzyme that catalyzes transsulfuration, and glutaredoxin activates 3-mercaptopyruvate sulfurtransferase in the reducing system. Interestingly, even when glutathione or glutathione reductase was absent, 3-mercaptopyruvate sulfurtransferase activity increased, probably because reduced glutaredoxin was partly present and able to activate 3-mercaptopyruvate sulfurtransferase until depletion. A study using mutant Escherichia coli glutaredoxin1 (Cys14 is the binding site of glutathione and was replaced with a Ser residue) confirmed these results. Some inconsistency was noted, and glutaredoxin with higher redox potential than either 3-mercaptopyruvate sulfurtransferase or glutathione reduced 3-mercaptopyruvate sulfurtransferase. However, electron-transfer enzymatically proceeded from glutaredoxin to 3-mercaptopyruvate sulfurtransferase.
DOI: 10.3390/biom10060826
PubMed: 32481517
PubMed Central: PMC7356906
Affiliations:
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<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Activation of 3-Mercaptopyruvate Sulfurtransferase by Glutaredoxin Reducing System.</title><author><name sortKey="Nagahara, Noriyuki" sort="Nagahara, Noriyuki" uniqKey="Nagahara N" first="Noriyuki" last="Nagahara">Noriyuki Nagahara</name><affiliation wicri:level="1"><nlm:affiliation>Isotope Research Laboratory, Nippon Medical School, 1-1-5 Sendagi Bunkyo-Ku, Tokyo 113-8602, Japan.</nlm:affiliation><country xml:lang="fr">Japon</country><wicri:regionArea>Isotope Research Laboratory, Nippon Medical School, 1-1-5 Sendagi Bunkyo-Ku, Tokyo 113-8602</wicri:regionArea><placeName><settlement type="city">Tokyo</settlement><region type="région">Région de Kantō</region></placeName></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2020">2020</date><idno type="RBID">pubmed:32481517</idno><idno type="pmid">32481517</idno><idno type="doi">10.3390/biom10060826</idno><idno type="pmc">PMC7356906</idno><idno type="wicri:Area/Main/Corpus">000052</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000052</idno><idno type="wicri:Area/Main/Curation">000052</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">000052</idno><idno type="wicri:Area/Main/Exploration">000052</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Activation of 3-Mercaptopyruvate Sulfurtransferase by Glutaredoxin Reducing System.</title><author><name sortKey="Nagahara, Noriyuki" sort="Nagahara, Noriyuki" uniqKey="Nagahara N" first="Noriyuki" last="Nagahara">Noriyuki Nagahara</name><affiliation wicri:level="1"><nlm:affiliation>Isotope Research Laboratory, Nippon Medical School, 1-1-5 Sendagi Bunkyo-Ku, Tokyo 113-8602, Japan.</nlm:affiliation><country xml:lang="fr">Japon</country><wicri:regionArea>Isotope Research Laboratory, Nippon Medical School, 1-1-5 Sendagi Bunkyo-Ku, Tokyo 113-8602</wicri:regionArea><placeName><settlement type="city">Tokyo</settlement><region type="région">Région de Kantō</region></placeName></affiliation></author></analytic><series><title level="j">Biomolecules</title><idno type="eISSN">2218-273X</idno><imprint><date when="2020" type="published">2020</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Glutaredoxin (EC 1.15-1.21) is known as an oxidoreductase that protects cysteine residues within proteins against oxidative stress. Glutaredoxin catalyzes an electron transfer reaction that donates an electron to substrate proteins in the reducing system composed of glutaredoxin, glutathione, glutathione reductase, and nicotinamide-adenine dinucleotide phosphate (reduced form). 3-mercaptopyruvate sulfurtransferase (EC 2.8.1.2) is a cysteine enzyme that catalyzes transsulfuration, and glutaredoxin activates 3-mercaptopyruvate sulfurtransferase in the reducing system. Interestingly, even when glutathione or glutathione reductase was absent, 3-mercaptopyruvate sulfurtransferase activity increased, probably because reduced glutaredoxin was partly present and able to activate 3-mercaptopyruvate sulfurtransferase until depletion. A study using mutant <i>Escherichia coli</i> glutaredoxin1 (Cys<sup>14</sup> is the binding site of glutathione and was replaced with a Ser residue) confirmed these results. Some inconsistency was noted, and glutaredoxin with higher redox potential than either 3-mercaptopyruvate sulfurtransferase or glutathione reduced 3-mercaptopyruvate sulfurtransferase. However, electron-transfer enzymatically proceeded from glutaredoxin to 3-mercaptopyruvate sulfurtransferase.</div></front></TEI><pubmed><MedlineCitation Status="In-Data-Review" Owner="NLM"><PMID Version="1">32481517</PMID><DateRevised><Year>2020</Year><Month>07</Month><Day>23</Day></DateRevised><Article PubModel="Electronic"><Journal><ISSN IssnType="Electronic">2218-273X</ISSN><JournalIssue CitedMedium="Internet"><Volume>10</Volume><Issue>6</Issue><PubDate><Year>2020</Year><Month>May</Month><Day>28</Day></PubDate></JournalIssue><Title>Biomolecules</Title><ISOAbbreviation>Biomolecules</ISOAbbreviation></Journal><ArticleTitle>Activation of 3-Mercaptopyruvate Sulfurtransferase by Glutaredoxin Reducing System.</ArticleTitle><ELocationID EIdType="pii" ValidYN="Y">E826</ELocationID><ELocationID EIdType="doi" ValidYN="Y">10.3390/biom10060826</ELocationID><Abstract><AbstractText>Glutaredoxin (EC 1.15-1.21) is known as an oxidoreductase that protects cysteine residues within proteins against oxidative stress. Glutaredoxin catalyzes an electron transfer reaction that donates an electron to substrate proteins in the reducing system composed of glutaredoxin, glutathione, glutathione reductase, and nicotinamide-adenine dinucleotide phosphate (reduced form). 3-mercaptopyruvate sulfurtransferase (EC 2.8.1.2) is a cysteine enzyme that catalyzes transsulfuration, and glutaredoxin activates 3-mercaptopyruvate sulfurtransferase in the reducing system. Interestingly, even when glutathione or glutathione reductase was absent, 3-mercaptopyruvate sulfurtransferase activity increased, probably because reduced glutaredoxin was partly present and able to activate 3-mercaptopyruvate sulfurtransferase until depletion. A study using mutant <i>Escherichia coli</i> glutaredoxin1 (Cys<sup>14</sup> is the binding site of glutathione and was replaced with a Ser residue) confirmed these results. Some inconsistency was noted, and glutaredoxin with higher redox potential than either 3-mercaptopyruvate sulfurtransferase or glutathione reduced 3-mercaptopyruvate sulfurtransferase. However, electron-transfer enzymatically proceeded from glutaredoxin to 3-mercaptopyruvate sulfurtransferase.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Nagahara</LastName><ForeName>Noriyuki</ForeName><Initials>N</Initials><AffiliationInfo><Affiliation>Isotope Research Laboratory, Nippon Medical School, 1-1-5 Sendagi Bunkyo-Ku, Tokyo 113-8602, Japan.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2020</Year><Month>05</Month><Day>28</Day></ArticleDate></Article><MedlineJournalInfo><Country>Switzerland</Country><MedlineTA>Biomolecules</MedlineTA><NlmUniqueID>101596414</NlmUniqueID><ISSNLinking>2218-273X</ISSNLinking></MedlineJournalInfo><CitationSubset>IM</CitationSubset><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">3-mercaptopyruvate sulfurtransferase</Keyword><Keyword MajorTopicYN="N">glutaredoxin</Keyword><Keyword MajorTopicYN="N">glutathione</Keyword><Keyword MajorTopicYN="N">glutathione reductase</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2020</Year><Month>03</Month><Day>26</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2020</Year><Month>05</Month><Day>22</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2020</Year><Month>05</Month><Day>27</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2020</Year><Month>6</Month><Day>3</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2020</Year><Month>6</Month><Day>3</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2020</Year><Month>6</Month><Day>3</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>epublish</PublicationStatus><ArticleIdList><ArticleId 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