The Oxidized Protein Repair Enzymes Methionine Sulfoxide Reductases and Their Roles in Protecting against Oxidative Stress, in Ageing and in Regulating Protein Function.
Identifieur interne : 000206 ( Main/Exploration ); précédent : 000205; suivant : 000207The Oxidized Protein Repair Enzymes Methionine Sulfoxide Reductases and Their Roles in Protecting against Oxidative Stress, in Ageing and in Regulating Protein Function.
Auteurs : Sofia Lourenço Dos Santos [France] ; Isabelle Petropoulos [France] ; Bertrand Friguet [France]Source :
- Antioxidants (Basel, Switzerland) [ 2076-3921 ] ; 2018.
Abstract
Cysteine and methionine residues are the amino acids most sensitive to oxidation by reactive oxygen species. However, in contrast to other amino acids, certain cysteine and methionine oxidation products can be reduced within proteins by dedicated enzymatic repair systems. Oxidation of cysteine first results in either the formation of a disulfide bridge or a sulfenic acid. Sulfenic acid can be converted to disulfide or sulfenamide or further oxidized to sulfinic acid. Disulfide can be easily reversed by different enzymatic systems such as the thioredoxin/thioredoxin reductase and the glutaredoxin/glutathione/glutathione reductase systems. Methionine side chains can also be oxidized by reactive oxygen species. Methionine oxidation, by the addition of an extra oxygen atom, leads to the generation of methionine sulfoxide. Enzymatically catalyzed reduction of methionine sulfoxide is achieved by either methionine sulfoxide reductase A or methionine sulfoxide reductase B, also referred as to the methionine sulfoxide reductases system. This oxidized protein repair system is further described in this review article in terms of its discovery and biologically relevant characteristics, and its important physiological roles in protecting against oxidative stress, in ageing and in regulating protein function.
DOI: 10.3390/antiox7120191
PubMed: 30545068
PubMed Central: PMC6316033
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sort="Friguet, Bertrand" uniqKey="Friguet B" first="Bertrand" last="Friguet">Bertrand Friguet</name><affiliation wicri:level="3"><nlm:affiliation>Sorbonne Université, CNRS, INSERM, Institut de Biologie Paris-Seine, Biological Adaptation and Ageing, B2A-IBPS, F-75005 Paris, France. bertrand.friguet@sorbonne-universite.fr.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Sorbonne Université, CNRS, INSERM, Institut de Biologie Paris-Seine, Biological Adaptation and Ageing, B2A-IBPS, F-75005 Paris</wicri:regionArea><placeName><region type="region" nuts="2">Île-de-France</region><settlement type="city">Paris</settlement></placeName></affiliation></author></analytic><series><title level="j">Antioxidants (Basel, Switzerland)</title><idno type="ISSN">2076-3921</idno><imprint><date when="2018" type="published">2018</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Cysteine and methionine residues are the amino acids most sensitive to oxidation by reactive oxygen species. However, in contrast to other amino acids, certain cysteine and methionine oxidation products can be reduced within proteins by dedicated enzymatic repair systems. Oxidation of cysteine first results in either the formation of a disulfide bridge or a sulfenic acid. Sulfenic acid can be converted to disulfide or sulfenamide or further oxidized to sulfinic acid. Disulfide can be easily reversed by different enzymatic systems such as the thioredoxin/thioredoxin reductase and the glutaredoxin/glutathione/glutathione reductase systems. Methionine side chains can also be oxidized by reactive oxygen species. Methionine oxidation, by the addition of an extra oxygen atom, leads to the generation of methionine sulfoxide. Enzymatically catalyzed reduction of methionine sulfoxide is achieved by either methionine sulfoxide reductase A or methionine sulfoxide reductase B, also referred as to the methionine sulfoxide reductases system. This oxidized protein repair system is further described in this review article in terms of its discovery and biologically relevant characteristics, and its important physiological roles in protecting against oxidative stress, in ageing and in regulating protein function.</div></front></TEI><pubmed><MedlineCitation Status="PubMed-not-MEDLINE" Owner="NLM"><PMID Version="1">30545068</PMID><DateRevised><Year>2020</Year><Month>09</Month><Day>29</Day></DateRevised><Article PubModel="Electronic"><Journal><ISSN IssnType="Print">2076-3921</ISSN><JournalIssue CitedMedium="Print"><Volume>7</Volume><Issue>12</Issue><PubDate><Year>2018</Year><Month>Dec</Month><Day>12</Day></PubDate></JournalIssue><Title>Antioxidants (Basel, Switzerland)</Title><ISOAbbreviation>Antioxidants (Basel)</ISOAbbreviation></Journal><ArticleTitle>The Oxidized Protein Repair Enzymes Methionine Sulfoxide Reductases and Their Roles in Protecting against Oxidative Stress, in Ageing and in Regulating Protein Function.</ArticleTitle><ELocationID EIdType="pii" ValidYN="Y">E191</ELocationID><ELocationID EIdType="doi" ValidYN="Y">10.3390/antiox7120191</ELocationID><Abstract><AbstractText>Cysteine and methionine residues are the amino acids most sensitive to oxidation by reactive oxygen species. However, in contrast to other amino acids, certain cysteine and methionine oxidation products can be reduced within proteins by dedicated enzymatic repair systems. Oxidation of cysteine first results in either the formation of a disulfide bridge or a sulfenic acid. Sulfenic acid can be converted to disulfide or sulfenamide or further oxidized to sulfinic acid. Disulfide can be easily reversed by different enzymatic systems such as the thioredoxin/thioredoxin reductase and the glutaredoxin/glutathione/glutathione reductase systems. Methionine side chains can also be oxidized by reactive oxygen species. Methionine oxidation, by the addition of an extra oxygen atom, leads to the generation of methionine sulfoxide. Enzymatically catalyzed reduction of methionine sulfoxide is achieved by either methionine sulfoxide reductase A or methionine sulfoxide reductase B, also referred as to the methionine sulfoxide reductases system. This oxidized protein repair system is further described in this review article in terms of its discovery and biologically relevant characteristics, and its important physiological roles in protecting against oxidative stress, in ageing and in regulating protein function.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Lourenço Dos Santos</LastName><ForeName>Sofia</ForeName><Initials>S</Initials><AffiliationInfo><Affiliation>Sorbonne Université, CNRS, INSERM, Institut de Biologie Paris-Seine, Biological Adaptation and Ageing, B2A-IBPS, F-75005 Paris, France. sofia.lourenco.santos@gmail.com.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Petropoulos</LastName><ForeName>Isabelle</ForeName><Initials>I</Initials><AffiliationInfo><Affiliation>Sorbonne Université, CNRS, INSERM, Institut de Biologie Paris-Seine, Biological Adaptation and Ageing, B2A-IBPS, F-75005 Paris, France. isabelle.petropoulos@sorbonne-universite.fr.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Friguet</LastName><ForeName>Bertrand</ForeName><Initials>B</Initials><AffiliationInfo><Affiliation>Sorbonne Université, CNRS, INSERM, Institut de Biologie Paris-Seine, Biological Adaptation and Ageing, B2A-IBPS, F-75005 Paris, France. bertrand.friguet@sorbonne-universite.fr.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D016454">Review</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2018</Year><Month>12</Month><Day>12</Day></ArticleDate></Article><MedlineJournalInfo><Country>Switzerland</Country><MedlineTA>Antioxidants (Basel)</MedlineTA><NlmUniqueID>101668981</NlmUniqueID><ISSNLinking>2076-3921</ISSNLinking></MedlineJournalInfo><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">ageing</Keyword><Keyword MajorTopicYN="N">methionine oxidation</Keyword><Keyword MajorTopicYN="N">methionine sulfoxide reductases</Keyword><Keyword MajorTopicYN="N">oxidized protein repair</Keyword><Keyword MajorTopicYN="N">protein oxidation</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2018</Year><Month>11</Month><Day>15</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2018</Year><Month>11</Month><Day>30</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2018</Year><Month>12</Month><Day>01</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2018</Year><Month>12</Month><Day>15</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2018</Year><Month>12</Month><Day>14</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate 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