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Details on Person Two groups of sulfotransferease (SULT) enzymes catalyze the ...
| Class:Id | Summation:156585 |
|---|---|
| _displayName | Two groups of sulfotransferease (SULT) enzymes catalyze the ... |
| _timestamp | 2006-03-08 20:43:08 |
| created | [InstanceEdit:156583] Jassal, B, 2004-11-29 11:42:34 |
| literatureReference | [LiteratureReference:176546] A proposed nomenclature system for the cytosolic sulfotransferase (SULT) superfamily [LiteratureReference:176542] Human Sulfotransferases and Their Role in Chemical Metabolism [LiteratureReference:176637] Sulfotransferases in the bioactivation of xenobiotics |
| modified | [InstanceEdit:156610] Jassal, B, 2004-11-30 16:21:24 [InstanceEdit:156613] Jassal, B, 2004-12-01 15:37:38 [InstanceEdit:157995] Jassal, B, 2005-01-12 11:06:31 [InstanceEdit:159364] Jassal, B, 2005-03-03 15:42:04 [InstanceEdit:176534] D'Eustachio, P, 2006-03-08 20:43:01 |
| text | Two groups of sulfotransferease (SULT) enzymes catalyze the transfer of a sulfate group from 3-phosphoadenosine 5-phosphosulfate (PAPS) to a hydroxyl group on an acceptor molecule, yielding a sulfonated acceptor and 3-phosphoadenosine 5-phosphate (PAP). One is localized to the Golgi apparatus and mediates the sulfonation of proteoglycans. The second, annotated here, is cytosolic and mediates the sulfonation of a diverse array of small molecules, increasing their solubilities in water and modifying their physiological functions. There are probably thirteen or more human cytosolic SULT enzymes; eleven of these have been purified and characterized enzymatically, and are annotated here (Blanchard et al. 2004; Gamage et al. 2005). These enzymes appear to be active as dimers. Their substrate specificities are typically broad, and not related in an obvious way to their structures; indeed, apparently orthologous human and rodent SULT enzymes can have different substrate specificities (Glatt 2000), and none has been exhaustively characterized. The substrates listed in the table and annotated here are a sample of the known ones, chosen to indicate the range of activity of these enzymes and to capture some of their known physiologically important targets. Absence of a small molecule - enzyme pair from the table, however, may only mean that it has not yet been studied. |
| (summation) | [Pathway:156584] Cytosolic sulfonation of small molecules [Homo sapiens] |
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