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J. Biol. Chem., Vol. 262, Issue 21, 10039-10043, Jul, 1987

Amine N-sulfotransferase

SG Ramaswamy and WB Jakoby

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.
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