| http://purl.uniprot.org/citations/22985967 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/22985967 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/22985967 | http://www.w3.org/2000/01/rdf-schema#comment | "2-Cys peroxiredoxin (Prx) enzymes are ubiquitously distributed peroxidases that make use of a peroxidatic cysteine (Cys(P)) to decompose hydroperoxides. A disulfide bond is generated as a consequence of the partial unfolding of the α-helix that contains Cys(P). Therefore, during its catalytic cycle, 2-Cys Prx alternates between two states, locally unfolded and fully folded. Tsa1 (thiol-specific antioxidant protein 1 from yeast) is by far the most abundant Cys-based peroxidase in Saccharomyces cerevisiae. In this work, we present the crystallographic structure at 2.8Å resolution of Tsa1(C47S) in the decameric form [(α(2))(5)] with a DTT molecule bound to the active site, representing one of the few available reports of a 2-Cys Prx (AhpC-Prx1 subfamily) (AhpC, alkyl hydroperoxide reductase subunit C) structure that incorporates a ligand. The analysis of the Tsa1(C47S) structure indicated that Glu50 and Arg146 participate in the stabilization of the Cys(P) α-helix. As a consequence, we raised the hypothesis that Glu50 and Arg146 might be relevant to the Cys(P) reactivity. Therefore, Tsa1(E50A) and Tsa1(R146Q) mutants were generated and were still able to decompose hydrogen peroxide, presenting a second-order rate constant in the range of 10(6)M(-1)s(-1). Remarkably, although Tsa1(E50A) and Tsa1(R146Q) were efficiently reduced by the low-molecular-weight reductant DTT, these mutants displayed only marginal thioredoxin (Trx)-dependent peroxidase activity, indicating that Glu50 and Arg146 are important for the Tsa1-Trx interaction. These results may impact the comprehension of downstream events of signaling pathways that are triggered by the oxidation of critical Cys residues, such as Trx."xsd:string |
| http://purl.uniprot.org/citations/22985967 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.jmb.2012.09.008"xsd:string |
| http://purl.uniprot.org/citations/22985967 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.jmb.2012.09.008"xsd:string |
| http://purl.uniprot.org/citations/22985967 | http://purl.uniprot.org/core/author | "Netto L.E."xsd:string |
| http://purl.uniprot.org/citations/22985967 | http://purl.uniprot.org/core/author | "Netto L.E."xsd:string |
| http://purl.uniprot.org/citations/22985967 | http://purl.uniprot.org/core/author | "de Oliveira M.A."xsd:string |
| http://purl.uniprot.org/citations/22985967 | http://purl.uniprot.org/core/author | "de Oliveira M.A."xsd:string |
| http://purl.uniprot.org/citations/22985967 | http://purl.uniprot.org/core/author | "Horta B.B."xsd:string |
| http://purl.uniprot.org/citations/22985967 | http://purl.uniprot.org/core/author | "Horta B.B."xsd:string |
| http://purl.uniprot.org/citations/22985967 | http://purl.uniprot.org/core/author | "Tairum C.A. Jr."xsd:string |
| http://purl.uniprot.org/citations/22985967 | http://purl.uniprot.org/core/author | "Tairum C.A. Jr."xsd:string |
| http://purl.uniprot.org/citations/22985967 | http://purl.uniprot.org/core/author | "Zara F.J."xsd:string |
| http://purl.uniprot.org/citations/22985967 | http://purl.uniprot.org/core/author | "Zara F.J."xsd:string |
| http://purl.uniprot.org/citations/22985967 | http://purl.uniprot.org/core/date | "2012"xsd:gYear |
| http://purl.uniprot.org/citations/22985967 | http://purl.uniprot.org/core/date | "2012"xsd:gYear |
| http://purl.uniprot.org/citations/22985967 | http://purl.uniprot.org/core/name | "J. Mol. Biol."xsd:string |
| http://purl.uniprot.org/citations/22985967 | http://purl.uniprot.org/core/name | "J. Mol. Biol."xsd:string |
| http://purl.uniprot.org/citations/22985967 | http://purl.uniprot.org/core/pages | "28-41"xsd:string |
| http://purl.uniprot.org/citations/22985967 | http://purl.uniprot.org/core/pages | "28-41"xsd:string |
| http://purl.uniprot.org/citations/22985967 | http://purl.uniprot.org/core/title | "Disulfide biochemistry in 2-cys peroxiredoxin: requirement of Glu50 and Arg146 for the reduction of yeast Tsa1 by thioredoxin."xsd:string |
| http://purl.uniprot.org/citations/22985967 | http://purl.uniprot.org/core/title | "Disulfide biochemistry in 2-cys peroxiredoxin: requirement of Glu50 and Arg146 for the reduction of yeast Tsa1 by thioredoxin."xsd:string |
| http://purl.uniprot.org/citations/22985967 | http://purl.uniprot.org/core/volume | "424"xsd:string |
| http://purl.uniprot.org/citations/22985967 | http://purl.uniprot.org/core/volume | "424"xsd:string |