Amine N-sulfotransferase.

S G Ramaswamy; W B Jakoby

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PubMed · 3475273

Amine N-sulfotransferase.

S G Ramaswamy·W B Jakoby

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Abstract

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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Animals Chromatography, DEAE-Cellulose Electrophoresis, Polyacrylamide Gel Guinea Pigs Hydrogen-Ion Concentration Kinetics Liver Magnesium Molecular Weight Phosphoadenosine Phosphosulfate Sulfates Sulfotransferases Sulfurtransferases Journal Article

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S G Ramaswamy, W B Jakoby. 1987-07-25. Amine N-sulfotransferase.. https://pubmed.ncbi.nlm.nih.gov/3475273/

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