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Prokaryotic and Eukaryotic Aryl Sulfotransferases: Sulfation of Quercetin and Its Derivatives
Author(s) -
Purchartová Kateřina,
Valentová Kateřina,
Pelantová Helena,
Marhol Petr,
Cvačka Josef,
Havlíček Libor,
Křenková Alena,
Vavříková Eva,
Biedermann David,
Chambers Christopher S.,
Křen Vladimír
Publication year - 2015
Publication title -
chemcatchem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.497
H-Index - 106
eISSN - 1867-3899
pISSN - 1867-3880
DOI - 10.1002/cctc.201500298
Subject(s) - sulfation , taxifolin , quercetin , chemistry , rutin , sulfotransferase , catechol , biochemistry , stereochemistry , enzyme , aryl , organic chemistry , antioxidant , alkyl
Two types of sulfotransferases, namely recombinant rat liver aryl sulfotransferase AstIV and bacterial aryl sulfotransferase from Desulfitobacterium hafniense , were used for the sulfation of quercetin, its glycosylated derivatives (isoquercitrin and rutin), and dihydroquercetin ((+)‐taxifolin). The rat liver enzyme was able to sulfate only quercetin and taxifolin, whereas the quercetin glycosides remained intact. The D. hafniense enzyme sulfated isoquercitrin and rutin selectively at the C‐4′ position of the catechol moiety with very good yields. Taxifolin was sulfated at the C‐4′ position and a minor amount of the C‐3′ isomer was formed. Sulfation of quercetin proceeded preferentially at the C‐3′ position, but a lower proportion of the C‐4′ isomer was formed as well. A detailed analysis of the kinetics of this reaction is provided and a full structural analysis of all products is presented.