GlutaredoxinV1, Main, Exploration, bibRecord, 000B13

Inhibition of Schistosoma mansoni thioredoxin-glutathione reductase by auranofin: structural and kinetic aspects.

Identifieur interne : 000B13 ( Main/Exploration ); précédent : 000B12; suivant : 000B14

Inhibition of Schistosoma mansoni thioredoxin-glutathione reductase by auranofin: structural and kinetic aspects.

Auteurs : Francesco Angelucci [Italie] ; Ahmed A. Sayed ; David L. Williams ; Giovanna Boumis ; Maurizio Brunori ; Daniela Dimastrogiovanni ; Adriana E. Miele ; Frida Pauly ; Andrea Bellelli

Source :

The Journal of biological chemistry [ 1083-351X ] ; 2009.

RBID : pubmed:19710012

Descripteurs français

KwdFr :
- Animaux (MeSH), Antirhumatismaux (composition chimique), Antirhumatismaux (pharmacologie), Auranofine (composition chimique), Auranofine (pharmacologie), Catalyse (MeSH), Cinétique (MeSH), Complexes multienzymatiques (antagonistes et inhibiteurs), Complexes multienzymatiques (composition chimique), Cristallographie aux rayons X (méthodes), Cystéine (composition chimique), Modèles moléculaires (MeSH), NADH, NADPH oxidoreductases (antagonistes et inhibiteurs), NADH, NADPH oxidoreductases (composition chimique), Oxydoréduction (MeSH), Protéines d'helminthes (composition chimique), Relation dose-effet des médicaments (MeSH), Régulation de l'expression des gènes (MeSH), Schistosoma mansoni (métabolisme), Structure tertiaire des protéines (MeSH), Sélénium (composition chimique).
MESH :
- antagonistes et inhibiteurs : Complexes multienzymatiques, NADH, NADPH oxidoreductases.
- composition chimique : Antirhumatismaux, Auranofine, Complexes multienzymatiques, Cystéine, NADH, NADPH oxidoreductases, Protéines d'helminthes, Sélénium.
- métabolisme : Schistosoma mansoni.
- méthodes : Cristallographie aux rayons X.
- pharmacologie : Antirhumatismaux, Auranofine.
- Animaux, Catalyse, Cinétique, Modèles moléculaires, Oxydoréduction, Relation dose-effet des médicaments, Régulation de l'expression des gènes, Structure tertiaire des protéines.

English descriptors

KwdEn :
- Animals (MeSH), Antirheumatic Agents (chemistry), Antirheumatic Agents (pharmacology), Auranofin (chemistry), Auranofin (pharmacology), Catalysis (MeSH), Crystallography, X-Ray (methods), Cysteine (chemistry), Dose-Response Relationship, Drug (MeSH), Gene Expression Regulation (MeSH), Helminth Proteins (chemistry), Kinetics (MeSH), Models, Molecular (MeSH), Multienzyme Complexes (antagonists & inhibitors), Multienzyme Complexes (chemistry), NADH, NADPH Oxidoreductases (antagonists & inhibitors), NADH, NADPH Oxidoreductases (chemistry), Oxidation-Reduction (MeSH), Protein Structure, Tertiary (MeSH), Schistosoma mansoni (metabolism), Selenium (chemistry).
MESH :
- chemical , antagonists & inhibitors : Multienzyme Complexes, NADH, NADPH Oxidoreductases.
- chemical , chemistry : Antirheumatic Agents, Auranofin, Cysteine, Helminth Proteins, Multienzyme Complexes, NADH, NADPH Oxidoreductases, Selenium.
- chemical , pharmacology : Antirheumatic Agents, Auranofin.
- metabolism : Schistosoma mansoni.
- methods : Crystallography, X-Ray.
- Animals, Catalysis, Dose-Response Relationship, Drug, Gene Expression Regulation, Kinetics, Models, Molecular, Oxidation-Reduction, Protein Structure, Tertiary.

Abstract

Schistosomiasis is a parasitic disease affecting over 200 million people currently treated with one drug, praziquantel. A possible drug target is the seleno-protein thioredoxin-glutathione reductase (TGR), a key enzyme in the pathway of the parasite for detoxification of reactive oxygen species. The enzyme is a unique fusion of a glutaredoxin domain with a thioredoxin reductase domain, which contains a selenocysteine (Sec) as the penultimate amino acid. Auranofin (AF), a gold-containing compound already in clinical use as an anti-arthritic drug, has been shown to inhibit TGR and to substantially reduce worm burden in mice. Using x-ray crystallography we solved (at 2.5 A resolution) the structure of wild type TGR incubated with AF. The electron density maps show that the actual inhibitor is gold, released from AF. Gold is bound at three different sites not directly involving the C-terminal Sec residue; however, because the C terminus in the electron density maps is disordered, we cannot exclude the possibility that gold may also bind to Sec. To investigate the possible role of Sec in the inactivation kinetics, we tested the effect of AF on a model enzyme of the same superfamily, i.e. the naturally Sec-lacking glutathione reductase, and on truncated TGR. We demonstrate that the role of selenium in the onset of inhibition by AF is catalytic and can be mimicked by an external source of selenium (benzeneselenol). Therefore, we propose that Sec mediates the transfer of gold from its ligands in AF to the redox-active Cys couples of TGR.

DOI: 10.1074/jbc.M109.020701
PubMed: 19710012
PubMed Central: PMC2781444

Affiliations:

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

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to stream Main, to step Curation: 000A83

Le document en format XML

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<term>Antirheumatic Agents (chemistry)</term>
<term>Antirheumatic Agents (pharmacology)</term>
<term>Auranofin (chemistry)</term>
<term>Auranofin (pharmacology)</term>
<term>Catalysis (MeSH)</term>
<term>Crystallography, X-Ray (methods)</term>
<term>Cysteine (chemistry)</term>
<term>Dose-Response Relationship, Drug (MeSH)</term>
<term>Gene Expression Regulation (MeSH)</term>
<term>Helminth Proteins (chemistry)</term>
<term>Kinetics (MeSH)</term>
<term>Models, Molecular (MeSH)</term>
<term>Multienzyme Complexes (antagonists & inhibitors)</term>
<term>Multienzyme Complexes (chemistry)</term>
<term>NADH, NADPH Oxidoreductases (antagonists & inhibitors)</term>
<term>NADH, NADPH Oxidoreductases (chemistry)</term>
<term>Oxidation-Reduction (MeSH)</term>
<term>Protein Structure, Tertiary (MeSH)</term>
<term>Schistosoma mansoni (metabolism)</term>
<term>Selenium (chemistry)</term>
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<keywords scheme="KwdFr" xml:lang="fr"><term>Animaux (MeSH)</term>
<term>Antirhumatismaux (composition chimique)</term>
<term>Antirhumatismaux (pharmacologie)</term>
<term>Auranofine (composition chimique)</term>
<term>Auranofine (pharmacologie)</term>
<term>Catalyse (MeSH)</term>
<term>Cinétique (MeSH)</term>
<term>Complexes multienzymatiques (antagonistes et inhibiteurs)</term>
<term>Complexes multienzymatiques (composition chimique)</term>
<term>Cristallographie aux rayons X (méthodes)</term>
<term>Cystéine (composition chimique)</term>
<term>Modèles moléculaires (MeSH)</term>
<term>NADH, NADPH oxidoreductases (antagonistes et inhibiteurs)</term>
<term>NADH, NADPH oxidoreductases (composition chimique)</term>
<term>Oxydoréduction (MeSH)</term>
<term>Protéines d'helminthes (composition chimique)</term>
<term>Relation dose-effet des médicaments (MeSH)</term>
<term>Régulation de l'expression des gènes (MeSH)</term>
<term>Schistosoma mansoni (métabolisme)</term>
<term>Structure tertiaire des protéines (MeSH)</term>
<term>Sélénium (composition chimique)</term>
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<term>NADH, NADPH Oxidoreductases</term>
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<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Antirheumatic Agents</term>
<term>Auranofin</term>
<term>Cysteine</term>
<term>Helminth Proteins</term>
<term>Multienzyme Complexes</term>
<term>NADH, NADPH Oxidoreductases</term>
<term>Selenium</term>
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<keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Antirheumatic Agents</term>
<term>Auranofin</term>
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<keywords scheme="MESH" qualifier="antagonistes et inhibiteurs" xml:lang="fr"><term>Complexes multienzymatiques</term>
<term>NADH, NADPH oxidoreductases</term>
</keywords>
<keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Antirhumatismaux</term>
<term>Auranofine</term>
<term>Complexes multienzymatiques</term>
<term>Cystéine</term>
<term>NADH, NADPH oxidoreductases</term>
<term>Protéines d'helminthes</term>
<term>Sélénium</term>
</keywords>
<keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Schistosoma mansoni</term>
</keywords>
<keywords scheme="MESH" qualifier="methods" xml:lang="en"><term>Crystallography, X-Ray</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Schistosoma mansoni</term>
</keywords>
<keywords scheme="MESH" qualifier="méthodes" xml:lang="fr"><term>Cristallographie aux rayons X</term>
</keywords>
<keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Antirhumatismaux</term>
<term>Auranofine</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Animals</term>
<term>Catalysis</term>
<term>Dose-Response Relationship, Drug</term>
<term>Gene Expression Regulation</term>
<term>Kinetics</term>
<term>Models, Molecular</term>
<term>Oxidation-Reduction</term>
<term>Protein Structure, Tertiary</term>
</keywords>
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<term>Catalyse</term>
<term>Cinétique</term>
<term>Modèles moléculaires</term>
<term>Oxydoréduction</term>
<term>Relation dose-effet des médicaments</term>
<term>Régulation de l'expression des gènes</term>
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<front><div type="abstract" xml:lang="en">Schistosomiasis is a parasitic disease affecting over 200 million people currently treated with one drug, praziquantel. A possible drug target is the seleno-protein thioredoxin-glutathione reductase (TGR), a key enzyme in the pathway of the parasite for detoxification of reactive oxygen species. The enzyme is a unique fusion of a glutaredoxin domain with a thioredoxin reductase domain, which contains a selenocysteine (Sec) as the penultimate amino acid. Auranofin (AF), a gold-containing compound already in clinical use as an anti-arthritic drug, has been shown to inhibit TGR and to substantially reduce worm burden in mice. Using x-ray crystallography we solved (at 2.5 A resolution) the structure of wild type TGR incubated with AF. The electron density maps show that the actual inhibitor is gold, released from AF. Gold is bound at three different sites not directly involving the C-terminal Sec residue; however, because the C terminus in the electron density maps is disordered, we cannot exclude the possibility that gold may also bind to Sec. To investigate the possible role of Sec in the inactivation kinetics, we tested the effect of AF on a model enzyme of the same superfamily, i.e. the naturally Sec-lacking glutathione reductase, and on truncated TGR. We demonstrate that the role of selenium in the onset of inhibition by AF is catalytic and can be mimicked by an external source of selenium (benzeneselenol). Therefore, we propose that Sec mediates the transfer of gold from its ligands in AF to the redox-active Cys couples of TGR.</div>
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<Abstract><AbstractText>Schistosomiasis is a parasitic disease affecting over 200 million people currently treated with one drug, praziquantel. A possible drug target is the seleno-protein thioredoxin-glutathione reductase (TGR), a key enzyme in the pathway of the parasite for detoxification of reactive oxygen species. The enzyme is a unique fusion of a glutaredoxin domain with a thioredoxin reductase domain, which contains a selenocysteine (Sec) as the penultimate amino acid. Auranofin (AF), a gold-containing compound already in clinical use as an anti-arthritic drug, has been shown to inhibit TGR and to substantially reduce worm burden in mice. Using x-ray crystallography we solved (at 2.5 A resolution) the structure of wild type TGR incubated with AF. The electron density maps show that the actual inhibitor is gold, released from AF. Gold is bound at three different sites not directly involving the C-terminal Sec residue; however, because the C terminus in the electron density maps is disordered, we cannot exclude the possibility that gold may also bind to Sec. To investigate the possible role of Sec in the inactivation kinetics, we tested the effect of AF on a model enzyme of the same superfamily, i.e. the naturally Sec-lacking glutathione reductase, and on truncated TGR. We demonstrate that the role of selenium in the onset of inhibition by AF is catalytic and can be mimicked by an external source of selenium (benzeneselenol). Therefore, we propose that Sec mediates the transfer of gold from its ligands in AF to the redox-active Cys couples of TGR.</AbstractText>
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Inhibition of Schistosoma mansoni thioredoxin-glutathione reductase by auranofin: structural and kinetic aspects.

Inhibition of Schistosoma mansoni thioredoxin-glutathione reductase by auranofin: structural and kinetic aspects.

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