GlutaredoxinV1, Main, Exploration, bibRecord, 001243

Protein disulphide oxidoreductases in bacteria.

Identifieur interne : 001243 ( Main/Exploration ); précédent : 001242; suivant : 001244

Protein disulphide oxidoreductases in bacteria.

Auteurs : H. Loferer [Suisse] ; H. Hennecke

Source :

Trends in biochemical sciences [ 0968-0004 ] ; 1994.

RBID : pubmed:8016867

Descripteurs français

KwdFr :
- Bactéries (enzymologie), Bactéries à Gram négatif (enzymologie), Cystéine (métabolisme), Disulfures (métabolisme), Glutarédoxines (MeSH), Isomerases (génétique), Isomerases (métabolisme), Oxidoreductases (génétique), Oxidoreductases (métabolisme), Protein Disulfide-Isomerases (MeSH), Protein-disulfide reductase (glutathione) (génétique), Protein-disulfide reductase (glutathione) (métabolisme), Protéines (MeSH), Thiorédoxines (métabolisme).
MESH :
- enzymologie : Bactéries, Bactéries à Gram négatif.
- génétique : Isomerases, Oxidoreductases, Protein-disulfide reductase (glutathione).
- métabolisme : Cystéine, Disulfures, Isomerases, Oxidoreductases, Protein-disulfide reductase (glutathione), Thiorédoxines.
- Glutarédoxines, Protein Disulfide-Isomerases, Protéines.

English descriptors

KwdEn :
- Bacteria (enzymology), Cysteine (metabolism), Disulfides (metabolism), Glutaredoxins (MeSH), Gram-Negative Bacteria (enzymology), Isomerases (genetics), Isomerases (metabolism), Oxidoreductases (genetics), Oxidoreductases (metabolism), Protein Disulfide Reductase (Glutathione) (genetics), Protein Disulfide Reductase (Glutathione) (metabolism), Protein Disulfide-Isomerases (MeSH), Proteins (MeSH), Thioredoxins (metabolism).
MESH :
- chemical , genetics : Isomerases, Oxidoreductases, Protein Disulfide Reductase (Glutathione).
- chemical , metabolism : Cysteine, Disulfides, Isomerases, Oxidoreductases, Protein Disulfide Reductase (Glutathione), Thioredoxins.
- enzymology : Bacteria, Gram-Negative Bacteria.
- chemical : Glutaredoxins, Protein Disulfide-Isomerases, Proteins.

Abstract

Thioredoxins and eukaryotic protein disulphide isomerases were, until recently, the only enzymes known to catalyse reversible oxidation and reduction of cysteine residues of a wide spectrum of protein substrates. Genetic and biochemical investigations on different bacterial systems have now led to the discovery of novel prokaryotic protein disulphide oxidoreductases that are located either in the periplasm or in the cytoplasmic membrane.

DOI: 10.1016/0968-0004(94)90279-8
PubMed: 8016867

Affiliations:

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Le document en format XML

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<author><name sortKey="Loferer, H" sort="Loferer, H" uniqKey="Loferer H" first="H" last="Loferer">H. Loferer</name>
<affiliation wicri:level="3"><nlm:affiliation>Institute of Microbiology, Eidgenössische Technische Hochschule, ETH-Zentrum, Zürich, Switzerland.</nlm:affiliation>
<country xml:lang="fr">Suisse</country>
<wicri:regionArea>Institute of Microbiology, Eidgenössische Technische Hochschule, ETH-Zentrum, Zürich</wicri:regionArea>
<placeName><settlement type="city">Zurich</settlement>
<region nuts="3" type="region">Canton de Zurich</region>
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<author><name sortKey="Hennecke, H" sort="Hennecke, H" uniqKey="Hennecke H" first="H" last="Hennecke">H. Hennecke</name>
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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Bacteria (enzymology)</term>
<term>Cysteine (metabolism)</term>
<term>Disulfides (metabolism)</term>
<term>Glutaredoxins (MeSH)</term>
<term>Gram-Negative Bacteria (enzymology)</term>
<term>Isomerases (genetics)</term>
<term>Isomerases (metabolism)</term>
<term>Oxidoreductases (genetics)</term>
<term>Oxidoreductases (metabolism)</term>
<term>Protein Disulfide Reductase (Glutathione) (genetics)</term>
<term>Protein Disulfide Reductase (Glutathione) (metabolism)</term>
<term>Protein Disulfide-Isomerases (MeSH)</term>
<term>Proteins (MeSH)</term>
<term>Thioredoxins (metabolism)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Bactéries (enzymologie)</term>
<term>Bactéries à Gram négatif (enzymologie)</term>
<term>Cystéine (métabolisme)</term>
<term>Disulfures (métabolisme)</term>
<term>Glutarédoxines (MeSH)</term>
<term>Isomerases (génétique)</term>
<term>Isomerases (métabolisme)</term>
<term>Oxidoreductases (génétique)</term>
<term>Oxidoreductases (métabolisme)</term>
<term>Protein Disulfide-Isomerases (MeSH)</term>
<term>Protein-disulfide reductase (glutathione) (génétique)</term>
<term>Protein-disulfide reductase (glutathione) (métabolisme)</term>
<term>Protéines (MeSH)</term>
<term>Thiorédoxines (métabolisme)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Isomerases</term>
<term>Oxidoreductases</term>
<term>Protein Disulfide Reductase (Glutathione)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Cysteine</term>
<term>Disulfides</term>
<term>Isomerases</term>
<term>Oxidoreductases</term>
<term>Protein Disulfide Reductase (Glutathione)</term>
<term>Thioredoxins</term>
</keywords>
<keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Bactéries</term>
<term>Bactéries à Gram négatif</term>
</keywords>
<keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Bacteria</term>
<term>Gram-Negative Bacteria</term>
</keywords>
<keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Isomerases</term>
<term>Oxidoreductases</term>
<term>Protein-disulfide reductase (glutathione)</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Cystéine</term>
<term>Disulfures</term>
<term>Isomerases</term>
<term>Oxidoreductases</term>
<term>Protein-disulfide reductase (glutathione)</term>
<term>Thiorédoxines</term>
</keywords>
<keywords scheme="MESH" type="chemical" xml:lang="en"><term>Glutaredoxins</term>
<term>Protein Disulfide-Isomerases</term>
<term>Proteins</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Glutarédoxines</term>
<term>Protein Disulfide-Isomerases</term>
<term>Protéines</term>
</keywords>
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<front><div type="abstract" xml:lang="en">Thioredoxins and eukaryotic protein disulphide isomerases were, until recently, the only enzymes known to catalyse reversible oxidation and reduction of cysteine residues of a wide spectrum of protein substrates. Genetic and biochemical investigations on different bacterial systems have now led to the discovery of novel prokaryotic protein disulphide oxidoreductases that are located either in the periplasm or in the cytoplasmic membrane.</div>
</front>
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<PubDate><Year>1994</Year>
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<Title>Trends in biochemical sciences</Title>
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<ArticleTitle>Protein disulphide oxidoreductases in bacteria.</ArticleTitle>
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<Abstract><AbstractText>Thioredoxins and eukaryotic protein disulphide isomerases were, until recently, the only enzymes known to catalyse reversible oxidation and reduction of cysteine residues of a wide spectrum of protein substrates. Genetic and biochemical investigations on different bacterial systems have now led to the discovery of novel prokaryotic protein disulphide oxidoreductases that are located either in the periplasm or in the cytoplasmic membrane.</AbstractText>
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<ChemicalList><Chemical><RegistryNumber>0</RegistryNumber>
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<Chemical><RegistryNumber>EC 1.-</RegistryNumber>
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<GeneSymbol>tlpA</GeneSymbol>
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Protein disulphide oxidoreductases in bacteria.

Protein disulphide oxidoreductases in bacteria.

Source :

Descripteurs français

English descriptors

Abstract

Links toward previous steps (curation, corpus...)

Le document en format XML

Pour manipuler ce document sous Unix (Dilib)

Pour mettre un lien sur cette page dans le réseau Wicri

Pour générer des pages wiki