Investigations of the catalytic mechanism of thioredoxin glutathione reductase from Schistosoma mansoni.
Identifieur interne : 000939 ( Main/Exploration ); précédent : 000938; suivant : 000940Investigations of the catalytic mechanism of thioredoxin glutathione reductase from Schistosoma mansoni.
Auteurs : Hsin-Hung Huang [États-Unis] ; Latasha Day ; Cynthia L. Cass ; David P. Ballou ; Charles H. Williams ; David L. WilliamsSource :
- Biochemistry [ 1520-4995 ] ; 2011.
Descripteurs français
- KwdFr :
- Animaux (MeSH), Biocatalyse (MeSH), Complexes multienzymatiques (composition chimique), Complexes multienzymatiques (génétique), Complexes multienzymatiques (métabolisme), Modèles moléculaires (MeSH), Mutagenèse dirigée (MeSH), NADH, NADPH oxidoreductases (composition chimique), NADH, NADPH oxidoreductases (génétique), NADH, NADPH oxidoreductases (métabolisme), Schistosoma mansoni (enzymologie), Structure tertiaire des protéines (MeSH), Sélénocystéine (MeSH).
- MESH :
- composition chimique : Complexes multienzymatiques, NADH, NADPH oxidoreductases.
- enzymologie : Schistosoma mansoni.
- génétique : Complexes multienzymatiques, NADH, NADPH oxidoreductases.
- métabolisme : Complexes multienzymatiques, NADH, NADPH oxidoreductases.
- Animaux, Biocatalyse, Modèles moléculaires, Mutagenèse dirigée, Structure tertiaire des protéines, Sélénocystéine.
English descriptors
- KwdEn :
- Animals (MeSH), Biocatalysis (MeSH), Models, Molecular (MeSH), Multienzyme Complexes (chemistry), Multienzyme Complexes (genetics), Multienzyme Complexes (metabolism), Mutagenesis, Site-Directed (MeSH), NADH, NADPH Oxidoreductases (chemistry), NADH, NADPH Oxidoreductases (genetics), NADH, NADPH Oxidoreductases (metabolism), Protein Structure, Tertiary (MeSH), Schistosoma mansoni (enzymology), Selenocysteine (MeSH).
- MESH :
- chemical , chemistry : Multienzyme Complexes, NADH, NADPH Oxidoreductases.
- chemical , genetics : Multienzyme Complexes, NADH, NADPH Oxidoreductases.
- chemical , metabolism : Multienzyme Complexes, NADH, NADPH Oxidoreductases.
- enzymology : Schistosoma mansoni.
- Animals, Biocatalysis, Models, Molecular, Mutagenesis, Site-Directed, Protein Structure, Tertiary, Selenocysteine.
Abstract
Thioredoxin glutathione reductase from Schistosoma mansoni (SmTGR) catalyzes the reduction of both thioredoxin and glutathione disulfides (GSSG), thus playing a crucial role in maintaining redox homeostasis in the parasite. In line with this role, previous studies have demonstrated that SmTGR is a promising drug target for schistosomiasis. To aid in the development of efficacious drugs that target SmTGR, it is essential to understand the catalytic mechanism of SmTGR. SmTGR is a dimeric flavoprotein in the glutathione reductase family and has a head-to-tail arrangement of its monomers; each subunit has the components of both a thioredoxin reductase (TrxR) domain and a glutaredoxin (Grx) domain. However, the active site of the TrxR domain is composed of residues from both subunits: FAD and a redox-active Cys-154/Cys-159 pair from one subunit and a redox-active Cys-596'/Sec-597' pair from the other; the active site of the Grx domain contains a redox-active Cys-28/Cys-31 pair. Via its Cys-28/Cys-31 dithiol and/or its Cys-596'/Sec-597' thiol-selenolate, SmTGR can catalyze the reduction of a variety of substrates by NADPH. It is presumed that SmTGR catalyzes deglutathionylation reactions via the Cys-28/Cys-31 dithiol. Our anaerobic titration data suggest that reducing equivalents from NADPH can indeed reach the Cys-28/Cys-31 disulfide in the Grx domain to facilitate reductions effected by this cysteine pair. To clarify the specific chemical roles of each redox-active residue with respect to its various reactivities, we generated variants of SmTGR. Cys-28 variants had no Grx deglutathionylation activity, whereas Cys-31 variants retained partial Grx deglutathionylation activity, indicating that the Cys-28 thiolate is the nucleophile initiating deglutathionylation. Lags in the steady-state kinetics, found when wild-type SmTGR was incubated at high concentrations of GSSG, were not present in Grx variants, indicating that this cysteine pair is in some way responsible for the lags. A Sec-597 variant was still able to reduce a variety of substrates, albeit slowly, showing that selenocysteine is important but is not the sole determinant for the broad substrate tolerance of the enzyme. Our data show that Cys-520 and Cys-574 are not likely to be involved in the catalytic mechanism.
DOI: 10.1021/bi200107n
PubMed: 21630672
PubMed Central: PMC3658134
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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<term>Multienzyme Complexes (metabolism)</term>
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<term>Complexes multienzymatiques (métabolisme)</term>
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<front><div type="abstract" xml:lang="en">Thioredoxin glutathione reductase from Schistosoma mansoni (SmTGR) catalyzes the reduction of both thioredoxin and glutathione disulfides (GSSG), thus playing a crucial role in maintaining redox homeostasis in the parasite. In line with this role, previous studies have demonstrated that SmTGR is a promising drug target for schistosomiasis. To aid in the development of efficacious drugs that target SmTGR, it is essential to understand the catalytic mechanism of SmTGR. SmTGR is a dimeric flavoprotein in the glutathione reductase family and has a head-to-tail arrangement of its monomers; each subunit has the components of both a thioredoxin reductase (TrxR) domain and a glutaredoxin (Grx) domain. However, the active site of the TrxR domain is composed of residues from both subunits: FAD and a redox-active Cys-154/Cys-159 pair from one subunit and a redox-active Cys-596'/Sec-597' pair from the other; the active site of the Grx domain contains a redox-active Cys-28/Cys-31 pair. Via its Cys-28/Cys-31 dithiol and/or its Cys-596'/Sec-597' thiol-selenolate, SmTGR can catalyze the reduction of a variety of substrates by NADPH. It is presumed that SmTGR catalyzes deglutathionylation reactions via the Cys-28/Cys-31 dithiol. Our anaerobic titration data suggest that reducing equivalents from NADPH can indeed reach the Cys-28/Cys-31 disulfide in the Grx domain to facilitate reductions effected by this cysteine pair. To clarify the specific chemical roles of each redox-active residue with respect to its various reactivities, we generated variants of SmTGR. Cys-28 variants had no Grx deglutathionylation activity, whereas Cys-31 variants retained partial Grx deglutathionylation activity, indicating that the Cys-28 thiolate is the nucleophile initiating deglutathionylation. Lags in the steady-state kinetics, found when wild-type SmTGR was incubated at high concentrations of GSSG, were not present in Grx variants, indicating that this cysteine pair is in some way responsible for the lags. A Sec-597 variant was still able to reduce a variety of substrates, albeit slowly, showing that selenocysteine is important but is not the sole determinant for the broad substrate tolerance of the enzyme. Our data show that Cys-520 and Cys-574 are not likely to be involved in the catalytic mechanism.</div>
</front>
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<Abstract><AbstractText>Thioredoxin glutathione reductase from Schistosoma mansoni (SmTGR) catalyzes the reduction of both thioredoxin and glutathione disulfides (GSSG), thus playing a crucial role in maintaining redox homeostasis in the parasite. In line with this role, previous studies have demonstrated that SmTGR is a promising drug target for schistosomiasis. To aid in the development of efficacious drugs that target SmTGR, it is essential to understand the catalytic mechanism of SmTGR. SmTGR is a dimeric flavoprotein in the glutathione reductase family and has a head-to-tail arrangement of its monomers; each subunit has the components of both a thioredoxin reductase (TrxR) domain and a glutaredoxin (Grx) domain. However, the active site of the TrxR domain is composed of residues from both subunits: FAD and a redox-active Cys-154/Cys-159 pair from one subunit and a redox-active Cys-596'/Sec-597' pair from the other; the active site of the Grx domain contains a redox-active Cys-28/Cys-31 pair. Via its Cys-28/Cys-31 dithiol and/or its Cys-596'/Sec-597' thiol-selenolate, SmTGR can catalyze the reduction of a variety of substrates by NADPH. It is presumed that SmTGR catalyzes deglutathionylation reactions via the Cys-28/Cys-31 dithiol. Our anaerobic titration data suggest that reducing equivalents from NADPH can indeed reach the Cys-28/Cys-31 disulfide in the Grx domain to facilitate reductions effected by this cysteine pair. To clarify the specific chemical roles of each redox-active residue with respect to its various reactivities, we generated variants of SmTGR. Cys-28 variants had no Grx deglutathionylation activity, whereas Cys-31 variants retained partial Grx deglutathionylation activity, indicating that the Cys-28 thiolate is the nucleophile initiating deglutathionylation. Lags in the steady-state kinetics, found when wild-type SmTGR was incubated at high concentrations of GSSG, were not present in Grx variants, indicating that this cysteine pair is in some way responsible for the lags. A Sec-597 variant was still able to reduce a variety of substrates, albeit slowly, showing that selenocysteine is important but is not the sole determinant for the broad substrate tolerance of the enzyme. Our data show that Cys-520 and Cys-574 are not likely to be involved in the catalytic mechanism.</AbstractText>
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