Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.1.6.1 (sulfatase)
 3,205 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

1. Dietary flavonoids including kaempferol, quercetin, genistein and daidzein were tested for their ability to alter the conjugation of oestradiol (E(2)) via rat liver sulfotransferases and glucuronosyltransferase. 2. All four flavonoids inhibited the sulfonation of E(2) via phenol sulfotransferase, SULT1A1 with IC(50)s ranging from 0.29 to 4.61 micro M. Sulfonation of dehydroisoandrosterone (DHEA) via hydroxysteroid sulfotransferase, SULT2A1, was inhibited by higher amounts of the flavonoids (IC(50)s ranging from 34 to 116 micro M). 3. All flavonoids inhibited the formation of E(2)-beta-glucuronides (at carbon atoms 3 and 17) with IC(50)s ranging from 43 to 260 micro M. Glucuronidation of 4-methylumbelliferone (4-MU) was inhibited by high amounts of the flavonoids (IC(50)s ranging from 860 to 1550 micro M). 4. Hydrolysis of sulfonated oestrogens via arylsulfatase-c (ARSC) or 4-methylumbelliferone beta-glucuronidate (MUG) were not inhibited by the flavonoids. 5. It is concluded that SULT1A1 but not SULT2A1 or glucuronosyltransferase is highly sensitive to inhibition by dietary flavonoids. The potency of the inhibition for SULT1A1 (quercetin > kaempferol > genistein > daidzein) suggests a dependency on the number and position of hydroxyl radicals in the flavonoid molecule.
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PMID:Inhibition of rat liver sulfotransferases SULT1A1 and SULT2A1 and glucuronosyltransferase by dietary flavonoids. 1474 43

A sensitive fluorometric assay was developed for alcohol sulfotransferase (AST). This was the first continuous fluorometric assay reported for AST. It used 3'-phosphoadenosine 5'-phosphosulfate regenerated from 3-phosphoadenosine 5'-phosphate by a recombinant phenol sulfotransferase (PST) using 4-methylumbelliferyl sulfate as the sulfuryl group donor. The recombinant PST did not use the alcohol substrate under the designed condition, and the sensitivity for AST activity was found to be comparable to that of radioactive assay as reported in the literature. The change of fluorescence intensity of 4-methylumbelliferone corresponded directly to the amount of active AST and was sensitive enough to measure nanogram or picomole amounts of the enzyme activity. This fluorometric assay was used to determine the activities of AST as purified form and in crude extracts of pig liver, rat liver, and Escherichia coli. Some properties of human dehydroepiandrosterone sulfotransferase were determined by this method and were found to be comparable to published data. Under similar assay conditions, the contaminated activities of arylsulfatase in crude extracts were also determined. This method not only is useful for the routine and detailed kinetic study of this important class of enzymes but also has the potential for the development of a high-throughput procedure using microplate reader.
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PMID:Fluorometric assay for alcohol sulfotransferase. 1576 10