GlutaredoxinV1, Main, Exploration, bibRecord, 001094

Reactivity of glutaredoxins 1, 2 and 3 from Escherichia coli and protein disulfide isomerase towards glutathionyl-mixed disulfides in ribonuclease A.

Identifieur interne : 001094 ( Main/Exploration ); précédent : 001093; suivant : 001095

Reactivity of glutaredoxins 1, 2 and 3 from Escherichia coli and protein disulfide isomerase towards glutathionyl-mixed disulfides in ribonuclease A.

Auteurs : J. Lundström-Ljung [Suède] ; A. Vlamis-Gardikas ; F. Aslund ; A. Holmgren

Source :

FEBS letters [ 0014-5793 ] ; 1999.

RBID : pubmed:9989580

Descripteurs français

English descriptors

KwdEn :
- Bacterial Proteins (metabolism), Disulfides (metabolism), Escherichia coli (metabolism), Glutaredoxins (MeSH), Kinetics (MeSH), Oxidation-Reduction (MeSH), Oxidoreductases (MeSH), Protein Disulfide-Isomerases (metabolism), Protein Folding (MeSH), Proteins (metabolism), Ribonuclease, Pancreatic (metabolism).
MESH :
- chemical , metabolism : Bacterial Proteins, Disulfides, Protein Disulfide-Isomerases, Proteins, Ribonuclease, Pancreatic.
- metabolism : Escherichia coli.
- chemical : Glutaredoxins, Kinetics, Oxidation-Reduction, Oxidoreductases, Protein Folding.

Abstract

We have examined the activity of protein disulfide isomerase (PDI) and glutaredoxin (Grx) 1, 2 and 3 from Escherichia coli to catalyze the cleavage of glutathionylated ribonuclease A (RNase-SG) by 1 mM GSH to yield reduced RNase. Apparent Km values for RNase-SG were similar, 2-10 microM, for Grx 1, 3 and PDI but Grx I and Grx 3 showed 500-fold higher turnover numbers than PDI. The atypical Grx 2 also catalyzed deglutathionylation by GSH, but had higher Km and apparent turnover number values compared to the two classical Grx. Refolding of RNase in a glutathione redox buffer was catalyzed by PDI. However, it could be measured only after a characteristic lag phase that was shortened by all three E. coli Grxs in a concentration-dependent manner. A role of the glutaredoxin mechanism in the endoplasmic reticulum is suggested.

DOI: 10.1016/s0014-5793(98)01698-6
PubMed: 9989580

Affiliations:

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Le document en format XML

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<author><name sortKey="Vlamis Gardikas, A" sort="Vlamis Gardikas, A" uniqKey="Vlamis Gardikas A" first="A" last="Vlamis-Gardikas">A. Vlamis-Gardikas</name>
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<term>Disulfides (metabolism)</term>
<term>Escherichia coli (metabolism)</term>
<term>Glutaredoxins (MeSH)</term>
<term>Kinetics (MeSH)</term>
<term>Oxidation-Reduction (MeSH)</term>
<term>Oxidoreductases (MeSH)</term>
<term>Protein Disulfide-Isomerases (metabolism)</term>
<term>Protein Folding (MeSH)</term>
<term>Proteins (metabolism)</term>
<term>Ribonuclease, Pancreatic (metabolism)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Cinétique (MeSH)</term>
<term>Disulfures (métabolisme)</term>
<term>Escherichia coli (métabolisme)</term>
<term>Glutarédoxines (MeSH)</term>
<term>Oxidoreductases (MeSH)</term>
<term>Oxydoréduction (MeSH)</term>
<term>Pancreatic ribonuclease (métabolisme)</term>
<term>Pliage des protéines (MeSH)</term>
<term>Protein Disulfide-Isomerases (métabolisme)</term>
<term>Protéines (métabolisme)</term>
<term>Protéines bactériennes (métabolisme)</term>
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<term>Disulfides</term>
<term>Protein Disulfide-Isomerases</term>
<term>Proteins</term>
<term>Ribonuclease, Pancreatic</term>
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<keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Escherichia coli</term>
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<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Disulfures</term>
<term>Escherichia coli</term>
<term>Pancreatic ribonuclease</term>
<term>Protein Disulfide-Isomerases</term>
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<term>Oxidoreductases</term>
<term>Protein Folding</term>
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<front><div type="abstract" xml:lang="en">We have examined the activity of protein disulfide isomerase (PDI) and glutaredoxin (Grx) 1, 2 and 3 from Escherichia coli to catalyze the cleavage of glutathionylated ribonuclease A (RNase-SG) by 1 mM GSH to yield reduced RNase. Apparent Km values for RNase-SG were similar, 2-10 microM, for Grx 1, 3 and PDI but Grx I and Grx 3 showed 500-fold higher turnover numbers than PDI. The atypical Grx 2 also catalyzed deglutathionylation by GSH, but had higher Km and apparent turnover number values compared to the two classical Grx. Refolding of RNase in a glutathione redox buffer was catalyzed by PDI. However, it could be measured only after a characteristic lag phase that was shortened by all three E. coli Grxs in a concentration-dependent manner. A role of the glutaredoxin mechanism in the endoplasmic reticulum is suggested.</div>
</front>
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Serveur d'exploration sur la glutarédoxine

Reactivity of glutaredoxins 1, 2 and 3 from Escherichia coli and protein disulfide isomerase towards glutathionyl-mixed disulfides in ribonuclease A.

Reactivity of glutaredoxins 1, 2 and 3 from Escherichia coli and protein disulfide isomerase towards glutathionyl-mixed disulfides in ribonuclease A.

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