Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Brito, J.; Gutierres, A.; Denkmann, K.; Dahl, C.; Archer, M.
    Production, crystallization and preliminary crystallographic analysis of Allochromatium vinosum thiosulfate dehydrogenase TsdA, an unusual acidophilic c-type cytochrome (2014), Acta Crystallogr. Sect. F, 70, 1424-1427 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.8.2.2 gene tsdA, recombinant expression of Strep-tagged enzyme in Escherichia coli strain BL21(DE3) Allochromatium vinosum

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.8.2.2 purified recombinant enzyme, sitting drop vapour diffusion method, mixing of 0.003 ml of 8 mg/ml protein in 20 mM Bis-Tris-HCl, pH 6.5, with 0.0015 ml of reservoir solution containing 23.5% w/v PEG 3350, 0.2 M (NH4)2SO4, 0.1 M Bis-Tris, pH 6.28, and 0.1 M NaI, and equilibration against 0.120 ml of reservoir solution, 20°C, method optimization, X-ray diffraction structure determination and analysis at 1.98 A resolution. The protein crystallized in space group C2 with one molecule in the asymmetric unit. Initial crystallization trials renders multiple, urchin-like crystals with no diffraction ability. Using iodide as an additive significantly improves the X-ray diffraction quality of the crystals Allochromatium vinosum

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.8.2.2 periplasm
-
 Allochromatium vinosum
-
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.8.2.2 2 thiosulfate + 2 ferricytochrome c Allochromatium vinosum in Allochromatium vinosum, enzyme TsdA operates in the direction of tetrathionate formation tetrathionate + 2 ferrocytochrome c
-
 ?
1.8.2.2 2 thiosulfate + 2 ferricytochrome c Allochromatium vinosum ATCC 17899 in Allochromatium vinosum, enzyme TsdA operates in the direction of tetrathionate formation tetrathionate + 2 ferrocytochrome c
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.8.2.2 Allochromatium vinosum D3RVD4
-
-
1.8.2.2 Allochromatium vinosum ATCC 17899 D3RVD4
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.8.2.2 recombinant Strep-tagged enzyme from Escherichia coli strain BL21(DE3) by affinity chromatography and gel filtration Allochromatium vinosum

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.8.2.2 2 thiosulfate + 2 ferricytochrome c in Allochromatium vinosum, enzyme TsdA operates in the direction of tetrathionate formation Allochromatium vinosum tetrathionate + 2 ferrocytochrome c
-
 ?
1.8.2.2 2 thiosulfate + 2 ferricytochrome c in Allochromatium vinosum, enzyme TsdA operates in the direction of tetrathionate formation Allochromatium vinosum ATCC 17899 tetrathionate + 2 ferrocytochrome c
-
 ?

Subunits

EC Number Subunits Comment Organism
1.8.2.2 monomer 1 * 27200, SDS-PAGE Allochromatium vinosum

Synonyms

EC Number Synonyms Comment Organism
1.8.2.2 tetrathionate synthase UniProt Allochromatium vinosum
1.8.2.2 TsdA
-
 Allochromatium vinosum

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.8.2.2 4
-
-
 Allochromatium vinosum

Cofactor

EC Number Cofactor Comment Organism Structure
1.8.2.2 cytochrome c
-
 Allochromatium vinosum

General Information

EC Number General Information Comment Organism
1.8.2.2 additional information thiosulfate dehydrogenase is a periplasmic, monomeric 27.2 kDa diheme c-type cytochrome with an activity optimum at pH 4.0 Allochromatium vinosum
1.8.2.2 physiological function the enzyme catalyzes the oxidative condensation of two thiosulfate anions, a reaction that is widespread among prokaryotes Allochromatium vinosum