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Literature summary for 2.8.1.1 extracted from

  • Higgins, K.A.; Peng, H.; Luebke, J.L.; Chang, F.M.; Giedroc, D.P.
    Conformational analysis and chemical reactivity of the multidomain sulfurtransferase, Staphylococcus aureus CstA (2015), Biochemistry, 54, 2385-2398.
    View publication on PubMed
Search for more literature for 2.8.1.1

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
21600
-
-
 Staphylococcus aureus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
thiosulfate + cyanide Staphylococcus aureus
-
 sulfite + thiocyanate
-
 ?

Organism

Organism UniProt Comment Textmining
Staphylococcus aureus
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the N-terminal domain of CstA exhibits thiosulfate sulfurtransferase activity Staphylococcus aureus ?
-
 ?
thiosulfate + cyanide
-
 Staphylococcus aureus sulfite + thiocyanate
-
 ?

Subunits

Subunits Comment Organism
monomer 1 * 21600, small-angle X-ray scattering and gel filtration Staphylococcus aureus

Synonyms

Synonyms Comment Organism
CsoR-like sulfurtransferase repressor
-
 Staphylococcus aureus
CST
-
 Staphylococcus aureus
rhodanese
-
 Staphylococcus aureus
TST
-
 Staphylococcus aureus

General Information

General Information Comment Organism
physiological function thiosulfate sulfurtransferases PspE and GlpE contribute to virulence of Salmonella typhimurium in the mouse model of systemic disease. GlpE but not PspE is important for resistance to H2O2. Both enzymes do not contribute to nitric oxid stress, to synthesis of essential sulfur containing amino acids, nor to detoxification of cyanide Staphylococcus aureus