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http://purl.uniprot.org/citations/22032722http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/22032722http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/22032722http://www.w3.org/2000/01/rdf-schema#comment"Arsenate reductases (ArsCs) evolved independently as a defence mechanism against toxic arsenate. In the genome of Corynebacterium glutamicum, there are two arsenic resistance operons (ars1 and ars2) and four potential genes coding for arsenate reductases (Cg_ArsC1, Cg_ArsC2, Cg_ArsC1' and Cg_ArsC4). Using knockout mutants, in vitro reconstitution of redox pathways, arsenic measurements and enzyme kinetics, we show that a single organism has two different classes of arsenate reductases. Cg_ArsC1 and Cg_ArsC2 are single-cysteine monomeric enzymes coupled to the mycothiol/mycoredoxin redox pathway using a mycothiol transferase mechanism. In contrast, Cg_ArsC1' is a three-cysteine containing homodimer that uses a reduction mechanism linked to the thioredoxin pathway with a k(cat)/K(M) value which is 10(3) times higher than the one of Cg_ArsC1 or Cg_ArsC2. Cg_ArsC1' is constitutively expressed at low levels using its own promoter site. It reduces arsenate to arsenite that can then induce the expression of Cg_ArsC1 and Cg_ArsC2. We also solved the X-ray structures of Cg_ArsC1' and Cg_ArsC2. Both enzymes have a typical low-molecular-weight protein tyrosine phosphatases-I fold with a conserved oxyanion binding site. Moreover, Cg_ArsC1' is unique in bearing an N-terminal three-helical bundle that interacts with the active site of the other chain in the dimeric interface."xsd:string
http://purl.uniprot.org/citations/22032722http://purl.org/dc/terms/identifier"doi:10.1111/j.1365-2958.2011.07882.x"xsd:string
http://purl.uniprot.org/citations/22032722http://purl.org/dc/terms/identifier"doi:10.1111/j.1365-2958.2011.07882.x"xsd:string
http://purl.uniprot.org/citations/22032722http://purl.uniprot.org/core/author"Collet J.F."xsd:string
http://purl.uniprot.org/citations/22032722http://purl.uniprot.org/core/author"Collet J.F."xsd:string
http://purl.uniprot.org/citations/22032722http://purl.uniprot.org/core/author"Dufe V.T."xsd:string
http://purl.uniprot.org/citations/22032722http://purl.uniprot.org/core/author"Dufe V.T."xsd:string
http://purl.uniprot.org/citations/22032722http://purl.uniprot.org/core/author"Gil J.A."xsd:string
http://purl.uniprot.org/citations/22032722http://purl.uniprot.org/core/author"Gil J.A."xsd:string
http://purl.uniprot.org/citations/22032722http://purl.uniprot.org/core/author"Mateos L.M."xsd:string
http://purl.uniprot.org/citations/22032722http://purl.uniprot.org/core/author"Mateos L.M."xsd:string
http://purl.uniprot.org/citations/22032722http://purl.uniprot.org/core/author"Messens J."xsd:string
http://purl.uniprot.org/citations/22032722http://purl.uniprot.org/core/author"Messens J."xsd:string
http://purl.uniprot.org/citations/22032722http://purl.uniprot.org/core/author"Villadangos A.F."xsd:string
http://purl.uniprot.org/citations/22032722http://purl.uniprot.org/core/author"Villadangos A.F."xsd:string
http://purl.uniprot.org/citations/22032722http://purl.uniprot.org/core/author"Wahni K."xsd:string
http://purl.uniprot.org/citations/22032722http://purl.uniprot.org/core/author"Wahni K."xsd:string
http://purl.uniprot.org/citations/22032722http://purl.uniprot.org/core/author"De Galan S."xsd:string
http://purl.uniprot.org/citations/22032722http://purl.uniprot.org/core/author"De Galan S."xsd:string
http://purl.uniprot.org/citations/22032722http://purl.uniprot.org/core/author"Freitas S."xsd:string
http://purl.uniprot.org/citations/22032722http://purl.uniprot.org/core/author"Freitas S."xsd:string
http://purl.uniprot.org/citations/22032722http://purl.uniprot.org/core/author"Nur H."xsd:string
http://purl.uniprot.org/citations/22032722http://purl.uniprot.org/core/author"Nur H."xsd:string