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dc.contributor.authorGarcera, Ana
dc.contributor.authorBarreto Parra, Lina Patricia
dc.contributor.authorPiedrafita Llorens, Lídia
dc.contributor.authorTamarit Sumalla, Jordi
dc.contributor.authorHerrero Perpiñán, Enrique
dc.date.accessioned2015-07-17T12:01:46Z
dc.date.issued2006
dc.identifier.issn0345-7532
dc.identifier.urihttp://hdl.handle.net/10459.1/48619
dc.description.abstractThe Saccharomyces cerevisiae genome encodes three proteins that Analysis of point mutants derived from wild-type Gto2 indicates display similarities with human GSTOs (Omega class glutathione that, among the three cysteine residues of the molecule, only the S-transferases) hGSTO1-1 and hGSTO2-2. The three yeast pro- residue at position 46 is required for the glutaredoxin activity. teins have been named Gto1, Gto2 and Gto3, and their purified This indicates that the thiol transferase acts through a mono- recombinant forms are active as thiol transferases (glutaredoxins) thiol mechanism. Replacing the active site of the yeast monothiol against HED (β-hydroxyethyl disulphide), as dehydroascorbate glutaredoxin Grx5 with the proposed Gto2 active site containing reductases and as dimethylarsinic acid reductases, while they are Cys46 allows Grx5 to retain some activity against HED. Therefore not active against the standard GST substrate CDNB (1-chloro- the residues adjacent to the respective active cysteine residues in 2,4-dinitrobenzene). Their glutaredoxin activity is also detectable Gto2 and Grx5 are important determinants for the thiol transferase in yeast cell extracts. The enzyme activity characteristics of the activity against small disulphide-containing molecules. Gto proteins contrast with those of another yeast GST, Gtt1. The latter is active against CDNB and also displays glutathione peroxidase activity against organic hydroperoxides such as cumene hydroperoxide, but is not active as a thiol transferase.ca_ES
dc.language.isoengca_ES
dc.publisherBiochemical Societyca_ES
dc.relation.isformatofReproducció del document publicat a https://doi.org/10.1042/BJ20060034ca_ES
dc.relation.ispartofBiochemical Journal, 2006, vol. 398, p. 187-196ca_ES
dc.rights(c) Biochemical Society, 2006ca_ES
dc.subjectDeglutathionylationca_ES
dc.subjectGlutaredoxin (Grx)ca_ES
dc.subjectGlutathione peroxidaseca_ES
dc.subjectGlutathione S-transferase (GST)ca_ES
dc.subjectRedox regulationca_ES
dc.subjectThiol oxidoreductaseca_ES
dc.titleSaccharomyces cerevisiae cells have three Omega class glutathione S-transferases acting as 1-Cys thiol transferasesca_ES
dc.typearticleca_ES
dc.identifier.idgrec010245
dc.type.versionpublishedVersionca_ES
dc.rights.accessRightsinfo:eu-repo/semantics/restrictedAccessca_ES
dc.identifier.doihttps://doi.org/10.1042/BJ20060034
dc.date.embargoEndDate2025-01-01


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