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Showing 1 to 8 of 8 for “"rhodanese"”.
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Charakterisierung der Funktion der Rhodanese YnjE für die Molybdänkofaktor Biosynthese in Escherichia coli
… E. colis hin, welche in Verbindung mit einem rhodaneseähnlichen Protein den Schwefel in Form eines Persulfids übertragen. Ähnliche Mechanismen wurden bereits in der humanen Moco-Biosynthese und der Thiaminbiosynthese identifiziert. In dieser Arbeit wurde das E. coli Protein YnjE näher …
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A study of chemolithoautotrophic bacterial rhodanese, and its potential contribution to cyanide wastage during cyanidation of biooxidized concentrates
… reactive sulfur species and cyanide. The enzyme rhodanese (thiosulfate: cyanide sulfurtransferase EC 2.8.1.1) is also able to catalyze the formation of thiocyanate using thiosulfate and cyanide as substrates. Therefore, the most relevant members of the microbial consortium responsible for …
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Characterization of two novel proteins containing the rhodanese homology domain: YgaP and YbbB of Escherichia coli
Rhodanese homology domains are ubiquitous structural modules found in eubacteria, eukaryotes and archaea. The rhodanese homology domain may comprise the entire structure of a protein. Alternatively it is found as tandemly repeated modules in which the C-terminal domain displays the properly …
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Genetic and biochemical characterization of YrkF, a novel two-domain sulfurtransferase in Bacillus subtilis
… compounds and for normal cellular functions. The rhodanese homology domain is a ubiquitous structural module containing a characteristic active site cysteine residue. Some proteins containing a rhodanese domain display thiosulfate:cyanide sulfurtransferase activity in vitro. However, the …
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Characterization of PspE, a Secreted Sulfurtransferase of Escherichia coli
… nine proteins of Escherichia coli that contain a rhodanese homology domain. PspE is synthesized as a precursor with a 19-amino acid signal sequence and secreted to the periplasm. Mature PspE is the smallest rhodanese of E. coli (85 amino acids) and catalyzes the transfer of sulfur from thiosulfate …
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Biochemical and genetic characterization of mercaptopyruvate sulfurtransferase and paralogous putative sulfurtransferases of Escherichia coli
… including mercaptopyruvate sulfurtransferase and rhodanese, are widely distributed in living organisms. Mercaptopyruvate sulfurtransferase and rhodanese catalyze the transfer of sulfur from mercaptopyruvate and thiosulfate, respectively, to sulfur acceptors such as thiols or cyanide. There is …
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Characterization of AgaR and YihW, Members of the DeoR Family of Transcriptional Regulators, and GlpE, a Rhodanese Belonging to the GlpR Regulon, Also a Member of the DeoR Family
… GlpE was identified as a single-domain, 12-kDa rhodanese (thiosulfate:cyanide sulfurtransferase). The enzyme was purified to near homogeneity and characterized. As shown for other characterized rhodaneses, kinetic analysis revealed that catalysis occurs via an enzyme-sulfur intermediate …
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INVESTIGATION OF UNIQUE COENZYME A BIOSYNTHETIC AND REDOX FUNCTIONS IN Bacillus anthracis
… CoADR isoform, coenzyme A-disulfide reductase-rhodanese homology domain (CoADR-RHD), which does not catalyze the reduction of CoAD and is implicated in to function in sulfur metabolism. In order to test the physiological contributions of BACoADR and CoADR-RHD in thiol-disulfide redox …