Amine N-sulfotransferase.
A highly purified amine N-sulfotransferase has been isolated from guinea pig liver that catalyzes sulfuryl group transfer from 3'-phosphoadenosine 5'-phosphosulfate to one of a large number of either primary or secondary amines forming the appropriate sulfamate and adenosine 3',5'-bisphosphate. Amines as different as aniline, 2-naphthylamine, octylamine, 1,2,3,4-tetrahydroisoquinoline and 1,2,3,4-tetrahydroisoquinoline, desmethylimipramine, and cyclohexylamine serve as acceptors; the product of the last of these substrates is the sugar-substitute cyclamate. Amine N-sulfotransferase activity is dependent on the presence of an unprotonated amino group. The purified enzyme preparation also has O-sulfotransferase activities, suggesting that transfer to oxygen could represent an intrinsic function of the N-sulfotransferase.
D000818:Animals; D002848:Chromatography, DEAE-Cellulose; D004591:Electrophoresis, Polyacrylamide Gel; D006168:Guinea Pigs; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008099:Liver / Q000201:enzymology*; D008274:Magnesium / Q000494:pharmacology; D008970:Molecular Weight; D010724:Phosphoadenosine Phosphosulfate / Q000378:metabolism; D013431:Sulfates / Q000378:metabolism; D015238:Sulfotransferases; D013466:Sulfurtransferases / Q000302:isolation & purification* / Q000378:metabolism
D013431:Sulfates; D010724:Phosphoadenosine Phosphosulfate; D013466:Sulfurtransferases; D015238:Sulfotransferases; C035817:amine sulfotransferase; D008274:Magnesium