recombinant WsTsdA purified from Escherichia coli catalyzes both thiosulfate oxidation and tetrathionate reduction. Activity measurement by performing thiosulfate-dependent ferricyanide reduction
the enzyme TSdA is a periplasmic diheme cytochrome c with hemes. Two Cys-X-X-Cys-His heme c binding motifs are present in the sequence. The active site heme (heme 1) is characterized by an unusual His/Cys axial ligation in TsdA enzymes
a unique membrane-associated lipoprotein from Wolinella succinogenes, enhances tetrathionate reductase activity of enzyme TsdA. This effect is much stronger in the tetrathionate-reducing than in the thiosulfate-oxidizing direction. The TsdAC complex predominantly acts as a tetrathionate reductase in vivo
The Contribution of Eimeria Coinfection and Intestinal Inflammation to Cecal Colonization and Systemic Spread of Salmonella Typhimurium Deficient in Tetrathionate Reductase or Type III Secretion Systems Salmonella Pathogenicity Island 1 or 2.
[On the presence or absence of tetrathionate reductase in a collection of typhoid bacilli of various origins. Possible epidemiological importance of the study of this enzyme]
enzyme activity measured using ferricyanide as the electron acceptor is detected in cell extracts of Astrain ATCC 23270 grown on tetrathionate or sulfur, but no activity is detected in ferrous iron-grown cells
NaCl at an optimum concentration of 0.35 M stimulates the growth of strain SH on elemental sulfur, while LiCl and KCl cannot sustain the growth of strain SH
NaCl at an optimum concentration of 0.35 M stimulates the growth of strain SH on elemental sulfur, while LiCl and KCl cannot sustain the growth of strain SH
strain SH might have acquired a unique gene encoding the 44 kDa protein by horizontal transfer, as the protein with a high score and coverage is not found in other Acidithiobacillus thiooxidans genomes
the enzyme encoded by gene PSR1_00330 belongs to the tetrathionate reductase (TtrA) clade in the DMSO reductase family, phylogenetic analysis. Phylogenetic analysis of gene PSR1_00329 suggested that the encoded TtrB-related proteins does not form a single clade but consists of three distinct clades within the small electron transfer subunits of the DMSO reductase family. The putative psr1_00329-psr1_00330 operon lacked a gene encoding a membrane anchor subunit of tetrathionate reductase (TtrC), but a gene encoding a c-type cytochrome (cyt c) is adjacent to these two genes
strain SH might have acquired a unique gene encoding the 44 kDa protein by horizontal transfer, as the protein with a high score and coverage is not found in other Acidithiobacillus thiooxidans genomes
thiosulfate dehydrogenase plays a significant role in thiosulfate oxidation in the acidophilic, obligately chemolithoautotroph, Acidithiobacillus ferrooxidans
thiosulfate dehydrogenases (TsdAs) are bidirectional bacterial di-heme enzymes that catalyze the interconversion of tetrathionate and thiosulfate at measurable rates in both directions, cf. EC 1.8.2.2, thiosulfate dehydrogenase. The active site heme 1 in the enzyme has His/Cys ligation in the ferric and ferrous states. In Campylobacter jejuni, TsdA heme 2 has His/Met ligation. Enzyme CjTsdA allows use of tetrathionate as a terminal respiratory electron sink
TsdA is closely associated with the unprecedented lipoprotein TsdC encoded immediately downstream of tsdA in the same direction of transcription. TsdA from Wolinella succinogenes is a periplasmic diheme cytochrome c with hemes, lacking the 21-aa signal peptide. Two Cys-X-X-Cys-His heme c binding motifs are present in the sequence. The active site heme (heme 1) is characterized by an unusual His/Cys axial ligation in TsdA enzymes
the tsdA-like gene from Wolinella succinogenes encodes a periplasmic diheme cytochrome c with hemes, lacking the 21-aa signal peptide. Two Cys-X-X-Cys-His heme c binding motifs are present in the sequence. The active site heme (heme 1) is characterized by an unusual His/Cys axial ligation in TsdA enzymes
x * 37103, mature protein with two c-hemes, without the signal peptide, and with an N-terminal Strep II-tag preceded by three amino acids and followed by four amino acids, sequence calculation
native enzyme 71.4fold from the membrane fraction of strain SH by solubilization with n-dodecyl-beta-D-maltopyranoside, ultracentrifugation, anion exchange chromatography, dialysis, ultrafiltration, and gel filtration
recombinant Strep-tagged enzyme TsdA 41fold from Escherichia coli strains BL21(DE3) and C43(DE3) by membrane solubilization, affinity chromatography, desalting gel filtration, and ultrafiltration recombinant Strep-tagged TsdC by two steps of ultracentrifugation at 100000 x g, followed by affinity chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene tsdA, recombinant expression of Strep-tagged enzyme in Escherichia coli strains BL21(DE3) and C43(DE3), coexpression with Strep-tagged Wolinella succinogenes TsdC
genes PSR1_00330 /ttrA and PSR1_003329/ttrB, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis. The putative psr1_00329-psr1_00330 operon lacks a gene encoding a membrane anchor subunit of tetrathionate reductase (TtrC), but a gene encoding a c-type cytochrome (cyt c) is adjacent to these two genes. RT-PCR enzyme expression analysis
the Acidithiobacillus thiooxidans strain SH enzyme is isolated to develop a bioleaching process for NaCl-containing sulfide minerals. Thiosulfate-metabolizing activity is most important for bioleaching, as the sulfur moiety of sulfide minerals is thought to be metabolized via thiosulfate as an intermediate
the Acidithiobacillus thiooxidans strain SH enzyme is isolated to develop a bioleaching process for NaCl-containing sulfide minerals. Thiosulfate-metabolizing activity is most important for bioleaching, as the sulfur moiety of sulfide minerals is thought to be metabolized via thiosulfate as an intermediate
Liu, Y.; Denkmann, K.; Kosciow, K.; Dahl, C.; Kelly, D.
Tetrathionate stimulated growth of Campylobacter jejuni identifies a new type of bi-functional tetrathionate reductase (TsdA) that is widely distributed in bacteria