Literature summary for 1.8.2.2 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 .

Cloned(Commentary)

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

Crystallization (Commentary)

Crystallization (Comment)	Organism
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

Crystallization (Comment)

Organism

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

Localization	Comment	Organism	GeneOntology No.	Textmining
periplasm	-	Allochromatium vinosum	-	-

Natural Substrates/ Products (Substrates)

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

Organism	UniProt	Comment	Textmining
Allochromatium vinosum	D3RVD4	-	-
Allochromatium vinosum ATCC 17899	D3RVD4	-	-

Purification (Commentary)

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

Substrates and Products (Substrate)

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

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

Synonyms

Synonyms	Comment	Organism
tetrathionate synthase	UniProt	Allochromatium vinosum
TsdA	-	Allochromatium vinosum

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
4	-	-	Allochromatium vinosum

Cofactor

Cofactor	Comment	Organism	Structure
cytochrome c	-	Allochromatium vinosum

General Information

General Information	Comment	Organism
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
physiological function	the enzyme catalyzes the oxidative condensation of two thiosulfate anions, a reaction that is widespread among prokaryotes	Allochromatium vinosum