GlutaredoxinV1, Main, Exploration, bibRecord, 000B94

Kinetic and mechanistic characterization and versatile catalytic properties of mammalian glutaredoxin 2: implications for intracellular roles.

Identifieur interne : 000B94 ( Main/Exploration ); précédent : 000B93; suivant : 000B95

Kinetic and mechanistic characterization and versatile catalytic properties of mammalian glutaredoxin 2: implications for intracellular roles.

Auteurs : Molly M. Gallogly [États-Unis] ; David W. Starke ; Amanda K. Leonberg ; Susan M English Ospina ; John J. Mieyal

Source :

Biochemistry [ 1520-4995 ] ; 2008.

RBID : pubmed:18816065

Descripteurs français

KwdFr :
- Animaux (MeSH), Bovins (MeSH), Cinétique (MeSH), Concentration en ions d'hydrogène (MeSH), Disulfure de glutathion (analogues et dérivés), Disulfure de glutathion (métabolisme), Glutarédoxines (métabolisme), Humains (MeSH), Modèles chimiques (MeSH), Protéines recombinantes (métabolisme), Souris (MeSH), Spectrophotométrie (MeSH), Spécificité du substrat (MeSH), Sérumalbumine bovine (métabolisme), Techniques in vitro (MeSH).
MESH :
- analogues et dérivés : Disulfure de glutathion.
- métabolisme : Disulfure de glutathion, Glutarédoxines, Protéines recombinantes, Sérumalbumine bovine.
- Animaux, Bovins, Cinétique, Concentration en ions d'hydrogène, Humains, Modèles chimiques, Souris, Spectrophotométrie, Spécificité du substrat, Techniques in vitro.

English descriptors

KwdEn :
- Animals (MeSH), Cattle (MeSH), Glutaredoxins (metabolism), Glutathione Disulfide (analogs & derivatives), Glutathione Disulfide (metabolism), Humans (MeSH), Hydrogen-Ion Concentration (MeSH), In Vitro Techniques (MeSH), Kinetics (MeSH), Mice (MeSH), Models, Chemical (MeSH), Recombinant Proteins (metabolism), Serum Albumin, Bovine (metabolism), Spectrophotometry (MeSH), Substrate Specificity (MeSH).
MESH :
- chemical , analogs & derivatives : Glutathione Disulfide.
- chemical , metabolism : Glutaredoxins, Glutathione Disulfide, Recombinant Proteins, Serum Albumin, Bovine.
- Animals, Cattle, Humans, Hydrogen-Ion Concentration, In Vitro Techniques, Kinetics, Mice, Models, Chemical, Spectrophotometry, Substrate Specificity.

Abstract

Glutaredoxin (Grx)-catalyzed deglutathionylation of protein-glutathione mixed disulfides (protein-SSG) serves important roles in redox homeostasis and signal transduction, regulating diverse physiological and pathophysiological events. Mammalian cells have two Grx isoforms: Grx1, localized to the cytosol and mitochondrial intermembrane space, and Grx2, localized primarily to the mitochondrial matrix [Pai, H. V., et al. (2007) Antioxid. Redox Signaling 9, 2027-2033]. The catalytic behavior of Grx1 has been characterized extensively, whereas Grx2 catalysis is less well understood. We observed that human Grx1 and Grx2 exhibit key catalytic similarities, including selectivity for protein-SSG substrates and a nucleophilic, double-displacement, monothiol mechanism exhibiting a strong commitment to catalysis. A key distinction between Grx1- and Grx2-mediated deglutathionylation is decreased catalytic efficiency ( k cat/ K M) of Grx2 for protein deglutathionylation (due primarily to a decreased k cat), reflecting a higher p K a of its catalytic cysteine, as well as a decreased enhancement of nucleophilicity of the second substrate, GSH. As documented previously for hGrx1 [Starke, D. W., et al. (2003) J. Biol. Chem. 278, 14607-14613], hGrx2 catalyzes glutathione-thiyl radical (GS (*)) scavenging, and it also mediates GS transfer (protein S-glutathionylation) reactions, where GS (*) serves as a superior glutathionyl donor substrate for formation of GAPDH-SSG, compared to GSNO and GSSG. In contrast to its lower k cat for deglutathionylation reactions, Grx2 promotes GS-transfer to the model protein substrate GAPDH at rates equivalent to those of Grx1. Estimation of Grx1 and Grx2 concentrations within mitochondria predicts comparable deglutathionylation activities within the mitochondrial subcompartments, suggesting localized regulatory functions for both isozymes.

DOI: 10.1021/bi800966v
PubMed: 18816065
PubMed Central: PMC3569056

Affiliations:

États-Unis

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Le document en format XML

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<term>Glutathione Disulfide (metabolism)</term>
<term>Humans (MeSH)</term>
<term>Hydrogen-Ion Concentration (MeSH)</term>
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<term>Kinetics (MeSH)</term>
<term>Mice (MeSH)</term>
<term>Models, Chemical (MeSH)</term>
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<term>Serum Albumin, Bovine (metabolism)</term>
<term>Spectrophotometry (MeSH)</term>
<term>Substrate Specificity (MeSH)</term>
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<term>Cinétique (MeSH)</term>
<term>Concentration en ions d'hydrogène (MeSH)</term>
<term>Disulfure de glutathion (analogues et dérivés)</term>
<term>Disulfure de glutathion (métabolisme)</term>
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<term>Souris (MeSH)</term>
<term>Spectrophotométrie (MeSH)</term>
<term>Spécificité du substrat (MeSH)</term>
<term>Sérumalbumine bovine (métabolisme)</term>
<term>Techniques in vitro (MeSH)</term>
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<front><div type="abstract" xml:lang="en">Glutaredoxin (Grx)-catalyzed deglutathionylation of protein-glutathione mixed disulfides (protein-SSG) serves important roles in redox homeostasis and signal transduction, regulating diverse physiological and pathophysiological events. Mammalian cells have two Grx isoforms: Grx1, localized to the cytosol and mitochondrial intermembrane space, and Grx2, localized primarily to the mitochondrial matrix [Pai, H. V., et al. (2007) Antioxid. Redox Signaling 9, 2027-2033]. The catalytic behavior of Grx1 has been characterized extensively, whereas Grx2 catalysis is less well understood. We observed that human Grx1 and Grx2 exhibit key catalytic similarities, including selectivity for protein-SSG substrates and a nucleophilic, double-displacement, monothiol mechanism exhibiting a strong commitment to catalysis. A key distinction between Grx1- and Grx2-mediated deglutathionylation is decreased catalytic efficiency ( k cat/ K M) of Grx2 for protein deglutathionylation (due primarily to a decreased k cat), reflecting a higher p K a of its catalytic cysteine, as well as a decreased enhancement of nucleophilicity of the second substrate, GSH. As documented previously for hGrx1 [Starke, D. W., et al. (2003) J. Biol. Chem. 278, 14607-14613], hGrx2 catalyzes glutathione-thiyl radical (GS (*)) scavenging, and it also mediates GS transfer (protein S-glutathionylation) reactions, where GS (*) serves as a superior glutathionyl donor substrate for formation of GAPDH-SSG, compared to GSNO and GSSG. In contrast to its lower k cat for deglutathionylation reactions, Grx2 promotes GS-transfer to the model protein substrate GAPDH at rates equivalent to those of Grx1. Estimation of Grx1 and Grx2 concentrations within mitochondria predicts comparable deglutathionylation activities within the mitochondrial subcompartments, suggesting localized regulatory functions for both isozymes.</div>
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<Abstract><AbstractText>Glutaredoxin (Grx)-catalyzed deglutathionylation of protein-glutathione mixed disulfides (protein-SSG) serves important roles in redox homeostasis and signal transduction, regulating diverse physiological and pathophysiological events. Mammalian cells have two Grx isoforms: Grx1, localized to the cytosol and mitochondrial intermembrane space, and Grx2, localized primarily to the mitochondrial matrix [Pai, H. V., et al. (2007) Antioxid. Redox Signaling 9, 2027-2033]. The catalytic behavior of Grx1 has been characterized extensively, whereas Grx2 catalysis is less well understood. We observed that human Grx1 and Grx2 exhibit key catalytic similarities, including selectivity for protein-SSG substrates and a nucleophilic, double-displacement, monothiol mechanism exhibiting a strong commitment to catalysis. A key distinction between Grx1- and Grx2-mediated deglutathionylation is decreased catalytic efficiency ( k cat/ K M) of Grx2 for protein deglutathionylation (due primarily to a decreased k cat), reflecting a higher p K a of its catalytic cysteine, as well as a decreased enhancement of nucleophilicity of the second substrate, GSH. As documented previously for hGrx1 [Starke, D. W., et al. (2003) J. Biol. Chem. 278, 14607-14613], hGrx2 catalyzes glutathione-thiyl radical (GS (*)) scavenging, and it also mediates GS transfer (protein S-glutathionylation) reactions, where GS (*) serves as a superior glutathionyl donor substrate for formation of GAPDH-SSG, compared to GSNO and GSSG. In contrast to its lower k cat for deglutathionylation reactions, Grx2 promotes GS-transfer to the model protein substrate GAPDH at rates equivalent to those of Grx1. Estimation of Grx1 and Grx2 concentrations within mitochondria predicts comparable deglutathionylation activities within the mitochondrial subcompartments, suggesting localized regulatory functions for both isozymes.</AbstractText>
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Kinetic and mechanistic characterization and versatile catalytic properties of mammalian glutaredoxin 2: implications for intracellular roles.

Kinetic and mechanistic characterization and versatile catalytic properties of mammalian glutaredoxin 2: implications for intracellular roles.

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