The methionine sulfoxide reductases: Catalysis and substrate specificities.
Identifieur interne : 003785 ( Main/Exploration ); précédent : 003784; suivant : 003786The methionine sulfoxide reductases: Catalysis and substrate specificities.
Auteurs : Sandrine Boschi-Muller [France] ; Adeline Gand ; Guy BranlantSource :
- Archives of biochemistry and biophysics [ 1096-0384 ] ; 2008.
Descripteurs français
- KwdFr :
- Animaux (MeSH), Bovins (MeSH), Catalyse (MeSH), Cinétique (MeSH), Cystéine (métabolisme), Escherichia coli (enzymologie), Methionine Sulfoxide Reductases (MeSH), Mycobacterium tuberculosis (enzymologie), Méthionine (analogues et dérivés), Méthionine (métabolisme), Neisseria (enzymologie), Oxidoreductases (composition chimique), Oxidoreductases (métabolisme), Populus (enzymologie), Spécificité du substrat (MeSH), Thiols (métabolisme).
- MESH :
- analogues et dérivés : Méthionine.
- composition chimique : Oxidoreductases.
- enzymologie : Escherichia coli, Mycobacterium tuberculosis, Neisseria, Populus.
- métabolisme : Cystéine, Méthionine, Oxidoreductases, Thiols.
- Animaux, Bovins, Catalyse, Cinétique, Methionine Sulfoxide Reductases, Spécificité du substrat.
English descriptors
- KwdEn :
- Animals (MeSH), Catalysis (MeSH), Cattle (MeSH), Cysteine (metabolism), Escherichia coli (enzymology), Kinetics (MeSH), Methionine (analogs & derivatives), Methionine (metabolism), Methionine Sulfoxide Reductases (MeSH), Mycobacterium tuberculosis (enzymology), Neisseria (enzymology), Oxidoreductases (chemistry), Oxidoreductases (metabolism), Populus (enzymology), Substrate Specificity (MeSH), Sulfhydryl Compounds (metabolism).
- MESH :
- chemical , analogs & derivatives : Methionine.
- chemical , chemistry : Oxidoreductases.
- chemical , metabolism : Cysteine, Methionine, Oxidoreductases, Sulfhydryl Compounds.
- enzymology : Escherichia coli, Mycobacterium tuberculosis, Neisseria, Populus.
- Animals, Catalysis, Cattle, Kinetics, Methionine Sulfoxide Reductases, Substrate Specificity.
Abstract
Oxidation of Met residues in proteins leads to the formation of methionine sulfoxides (MetSO). Methionine sulfoxide reductases (Msr) are ubiquitous enzymes, which catalyze the reduction of the sulfoxide function of the oxidized methionine residues. In vivo, the role of Msrs is described as essential in protecting cells against oxidative damages and to play a role in infection of cells by pathogenic bacteria. There exist two structurally-unrelated classes of Msrs, called MsrA and MsrB, with opposite stereoselectivity towards the S and R isomers of the sulfoxide function, respectively. Both Msrs present a similar three-step catalytic mechanism. The first step, called the reductase step, leads to the formation of a sulfenic acid on the catalytic Cys with the concomitant release of Met. In recent years, significant efforts have been made to characterize structural and molecular factors involved in the catalysis, in particular of the reductase step, and in structural specificities.
DOI: 10.1016/j.abb.2008.02.007
PubMed: 18302927
Affiliations:
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(enzymology)</term><term>Substrate Specificity (MeSH)</term><term>Sulfhydryl Compounds (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Animaux (MeSH)</term><term>Bovins (MeSH)</term><term>Catalyse (MeSH)</term><term>Cinétique (MeSH)</term><term>Cystéine (métabolisme)</term><term>Escherichia coli (enzymologie)</term><term>Methionine Sulfoxide Reductases (MeSH)</term><term>Mycobacterium tuberculosis (enzymologie)</term><term>Méthionine (analogues et dérivés)</term><term>Méthionine (métabolisme)</term><term>Neisseria (enzymologie)</term><term>Oxidoreductases (composition chimique)</term><term>Oxidoreductases (métabolisme)</term><term>Populus (enzymologie)</term><term>Spécificité du substrat (MeSH)</term><term>Thiols (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="analogs & derivatives" xml:lang="en"><term>Methionine</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Oxidoreductases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Cysteine</term><term>Methionine</term><term>Oxidoreductases</term><term>Sulfhydryl Compounds</term></keywords><keywords scheme="MESH" qualifier="analogues et dérivés" xml:lang="fr"><term>Méthionine</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Oxidoreductases</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Escherichia coli</term><term>Mycobacterium tuberculosis</term><term>Neisseria</term><term>Populus</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Escherichia coli</term><term>Mycobacterium tuberculosis</term><term>Neisseria</term><term>Populus</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Cystéine</term><term>Méthionine</term><term>Oxidoreductases</term><term>Thiols</term></keywords><keywords 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Methionine sulfoxide reductases (Msr) are ubiquitous enzymes, which catalyze the reduction of the sulfoxide function of the oxidized methionine residues. In vivo, the role of Msrs is described as essential in protecting cells against oxidative damages and to play a role in infection of cells by pathogenic bacteria. There exist two structurally-unrelated classes of Msrs, called MsrA and MsrB, with opposite stereoselectivity towards the S and R isomers of the sulfoxide function, respectively. Both Msrs present a similar three-step catalytic mechanism. The first step, called the reductase step, leads to the formation of a sulfenic acid on the catalytic Cys with the concomitant release of Met. In recent years, significant efforts have been made to characterize structural and molecular factors involved in the catalysis, in particular of the reductase step, and in structural specificities.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">18302927</PMID><DateCompleted><Year>2008</Year><Month>07</Month><Day>28</Day></DateCompleted><DateRevised><Year>2015</Year><Month>11</Month><Day>19</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1096-0384</ISSN><JournalIssue CitedMedium="Internet"><Volume>474</Volume><Issue>2</Issue><PubDate><Year>2008</Year><Month>Jun</Month><Day>15</Day></PubDate></JournalIssue><Title>Archives of biochemistry and biophysics</Title><ISOAbbreviation>Arch Biochem Biophys</ISOAbbreviation></Journal><ArticleTitle>The methionine sulfoxide reductases: Catalysis and substrate specificities.</ArticleTitle><Pagination><MedlinePgn>266-73</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.abb.2008.02.007</ELocationID><Abstract><AbstractText>Oxidation of Met residues in proteins leads to the formation of methionine sulfoxides (MetSO). Methionine sulfoxide reductases (Msr) are ubiquitous enzymes, which catalyze the reduction of the sulfoxide function of the oxidized methionine residues. In vivo, the role of Msrs is described as essential in protecting cells against oxidative damages and to play a role in infection of cells by pathogenic bacteria. There exist two structurally-unrelated classes of Msrs, called MsrA and MsrB, with opposite stereoselectivity towards the S and R isomers of the sulfoxide function, respectively. Both Msrs present a similar three-step catalytic mechanism. The first step, called the reductase step, leads to the formation of a sulfenic acid on the catalytic Cys with the concomitant release of Met. In recent years, significant efforts have been made to characterize structural and molecular factors involved in the catalysis, in particular of the reductase step, and in structural specificities.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Boschi-Muller</LastName><ForeName>Sandrine</ForeName><Initials>S</Initials><AffiliationInfo><Affiliation>UMR 7567 CNRS-UHP--Maturation des ARN et Enzymologie Moléculaire, Nancy Université, BP 239, 54506 Vandoeuvre-lès-Nancy, France. sandrine.boschi@maem.uhp-nancy.fr</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Gand</LastName><ForeName>Adeline</ForeName><Initials>A</Initials></Author><Author ValidYN="Y"><LastName>Branlant</LastName><ForeName>Guy</ForeName><Initials>G</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType><PublicationType UI="D016454">Review</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2008</Year><Month>02</Month><Day>13</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Arch Biochem Biophys</MedlineTA><NlmUniqueID>0372430</NlmUniqueID><ISSNLinking>0003-9861</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D013438">Sulfhydryl Compounds</NameOfSubstance></Chemical><Chemical><RegistryNumber>AE28F7PNPL</RegistryNumber><NameOfSubstance UI="D008715">Methionine</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.-</RegistryNumber><NameOfSubstance UI="D010088">Oxidoreductases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.8.4.-</RegistryNumber><NameOfSubstance UI="D051150">Methionine Sulfoxide Reductases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.8.4.11</RegistryNumber><NameOfSubstance 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sortKey="Branlant, Guy" sort="Branlant, Guy" uniqKey="Branlant G" first="Guy" last="Branlant">Guy Branlant</name><name sortKey="Gand, Adeline" sort="Gand, Adeline" uniqKey="Gand A" first="Adeline" last="Gand">Adeline Gand</name></noCountry><country name="France"><region name="Grand Est"><name sortKey="Boschi Muller, Sandrine" sort="Boschi Muller, Sandrine" uniqKey="Boschi Muller S" first="Sandrine" last="Boschi-Muller">Sandrine Boschi-Muller</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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