Source:http://linkedlifedata.com/resource/pubmed/id/15499189
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
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pubmed:dateCreated |
2004-10-22
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pubmed:abstractText |
Regioselective sulfation of the phytoestrogens daidzein (DZ, 7,4'-dihydroxyisoflavone) and genistein (GS, 5,7,4'-trihydroxyisoflavone) was investigated using human liver cytosol and purified recombinant human sulfotransferase (SULT) isoforms, SULT1A1, SULT1A3, SULT2A1, and SULT1E1. 7-Position-preferential sulfation of DZ and GS was observed in human hepatic cytosols from 3 male and 3 female subjects. Average ratios for 7- to 4'-sulfate formation were 4.5:1 from DZ and 8.4:1 from GS in these human liver cytosols. Apparent K(m) values for the 7- and 4'-sulfation of DZ and GS by these cytosols were similar and in a range from 0.46 to 0.66 microM. All recombinant human SULTs had activity for 7- and 4'-sulfation of these phytoestrogens except for 7-sulfating activity of SULT1A3. SULT1A1 and SULT1E1 exhibited much higher catalytic efficiency, k(cat)/K(m), for 7- and 4'-sulfation of these substrates than did the other two, SULT1A3 and SULT2A1. SULT1A1 showed K(m) values of 0.47 and 0.52 microM for the mono-sulfation of DZ and GS, respectively, which were very similar to those of human cytosol. The observed k(cat)/K(m) indicated that SULT1A1 catalyzed 7-sulfation of DZ and GS at rates 4.4- and 8.8-fold higher, respectively, than such 4'-sulfation. However, with SULT1E1, catalytic efficiency was very similar for the sulfation of both positions. These data strongly suggest that SULT1A1 plays a major role in monosulfation of the phytoestrogens and determines the regioselectivity of sulfation in human hepatic cytosol. A kinetic study for 7,4'-disulfate formation of DZ and GS from their 7- and 4'-monosulfates indicated that SULT1E1 most efficiently catalyzed both reactions among human SULTs.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Arylsulfotransferase,
http://linkedlifedata.com/resource/pubmed/chemical/Genistein,
http://linkedlifedata.com/resource/pubmed/chemical/Isoflavones,
http://linkedlifedata.com/resource/pubmed/chemical/Phytoestrogens,
http://linkedlifedata.com/resource/pubmed/chemical/SULT1A1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Sulfates,
http://linkedlifedata.com/resource/pubmed/chemical/Sulfotransferases,
http://linkedlifedata.com/resource/pubmed/chemical/alcohol sulfotransferase,
http://linkedlifedata.com/resource/pubmed/chemical/daidzein,
http://linkedlifedata.com/resource/pubmed/chemical/estrone sulfotransferase,
http://linkedlifedata.com/resource/pubmed/chemical/monoamine-sulfating phenol...
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
1347-4367
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
19
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
216-26
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:15499189-Adult,
pubmed-meshheading:15499189-Aged,
pubmed-meshheading:15499189-Arylsulfotransferase,
pubmed-meshheading:15499189-Female,
pubmed-meshheading:15499189-Genistein,
pubmed-meshheading:15499189-Humans,
pubmed-meshheading:15499189-Isoflavones,
pubmed-meshheading:15499189-Liver,
pubmed-meshheading:15499189-Male,
pubmed-meshheading:15499189-Middle Aged,
pubmed-meshheading:15499189-Phytoestrogens,
pubmed-meshheading:15499189-Stereoisomerism,
pubmed-meshheading:15499189-Sulfates,
pubmed-meshheading:15499189-Sulfotransferases
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pubmed:year |
2004
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pubmed:articleTitle |
Regioselective monosulfation and disulfation of the phytoestrogens daidzein and genistein by human liver sulfotransferases.
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pubmed:affiliation |
Corporate, Scientific and Regulatory Affairs Division, Tobacco Headquarters, Japan Tobacco Inc., Tokyo.
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pubmed:publicationType |
Journal Article
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