title: Studies on the Arylsulphatase and phenol sulphotransferase activities of Aspergillus oryzae.
abstract: 1. Crude extracts of Aspergillus oryzae grown under conditions of sulphur limitation possess high arylsulphatase activity. 2. This activity can be greatly enhanced by the inclusion of tyramine or a number of other phenols in the assay medium. 3. The arylsulphatase activity of these extracts can be resolved into three distinct fractions by chromatography on DEAE-cellulose. 4. The effect of tyramine is restricted to one of these fractions only. 5. Evidence is presented which indicates that this effect is the consequence of a phenol sulphotransferase activity, which shows no requirement for 3'-phosphoadenosine 5'-phosphate as a cofactor, and which will not transfer sulphate from 3'-phosphoadenosine 5'-sulphatophosphate to potential phenolic acceptors. 6. The three enzymes differ also in their molecular weights and substrate specificities.
mesh_terms: D001192:Arylsulfatases / Q000378:metabolism*; D001230:Aspergillus / Q000201:enzymology*; D001236:Aspergillus oryzae / Q000201:enzymology*; D002848:Chromatography, DEAE-Cellulose; D002850:Chromatography, Gel; D002855:Chromatography, Thin Layer; D007700:Kinetics; D008970:Molecular Weight; D010636:Phenols / Q000494:pharmacology; D010724:Phosphoadenosine Phosphosulfate / Q000378:metabolism; D013429:Sulfatases / Q000378:metabolism*; D013466:Sulfurtransferases / Q000378:metabolism*; D014439:Tyramine / Q000494:pharmacology
chemical_list: D010636:Phenols; D010724:Phosphoadenosine Phosphosulfate; D013466:Sulfurtransferases; D013429:Sulfatases; D001192:Arylsulfatases; D014439:Tyramine