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Literature summary extracted from

  • Yang, Y.S.; Marshall, A.D.; McPhie, P.; Guo, W.X.A.; Xie, X.; Chen, X.; Jakoby, W.B.
    Two phenol sulfotransferase species from one cDNA: nature of the differences (1996), Protein Expr. Purif., 8, 423-429.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
2.8.2.1 adenosine 3',5'-bisphosphate the beta-enzyme form shows a hyperbolic dependence on adenosine 3',5'-bisphosphate concentration, whereas the alpha-enzyme form is not stimulated Rattus norvegicus

Organism

EC Number Organism UniProt Comment Textmining
2.8.2.1 Rattus norvegicus
-
alpha- and beta-enzyme form
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.8.2.1 3'-phosphoadenylyl sulfate + a phenol
-
Rattus norvegicus adenosine 3',5'-bisphosphate + an aryl sulfate the alpha-enzyme form catalyzes only the reverse reaction r
2.8.2.1 3'-phosphoadenylylsulfate + 2-naphthol
-
Rattus norvegicus adenosine 3',5'-bisphosphate + 2-naphthyl sulfate
-
r
2.8.2.1 3'-phosphoadenylylsulfate + 4-nitrophenol
-
Rattus norvegicus adenosine 3',5'-bisphosphate + 4-nitrophenyl sulfate
-
r

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.8.2.1 7
-
assay at Rattus norvegicus

Cofactor

EC Number Cofactor Comment Organism Structure
2.8.2.1 adenosine 3',5'-bisphosphate 1 mol of, tightly bound to the alpha-enzyme form, but not to the beta-enzyme form Rattus norvegicus