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Literature summary 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

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.8.1.1 21600
-
-
Staphylococcus aureus

Natural Substrates/ Products (Substrates)

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

Organism

EC Number Organism UniProt Comment Textmining
2.8.1.1 Staphylococcus aureus
-
-
-

Substrates and Products (Substrate)

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

Subunits

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

Synonyms

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

General Information

EC Number General Information Comment Organism
2.8.1.1 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