Prokaryotic and Eukaryotic Aryl Sulfotransferases: Sulfation of Quercetin and Its Derivatives

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11310%2F15%3A10319402" target="_blank" >RIV/00216208:11310/15:10319402 - isvavai.cz</a>

Alternative codes found

RIV/61388971:_____/15:00448995 RIV/61389030:_____/15:00448995 RIV/61388963:_____/15:00448995

Result on the web

<a href="http://dx.doi.org/10.1002/cctc.201500298" target="_blank" >http://dx.doi.org/10.1002/cctc.201500298</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1002/cctc.201500298" target="_blank" >10.1002/cctc.201500298</a>

Result language

angličtina

Original language name

Prokaryotic and Eukaryotic Aryl Sulfotransferases: Sulfation of Quercetin and Its Derivatives

Original language description

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 ofthe 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.

Czech name

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Czech description

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Type

J_x - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

CEP classification

CE - Biochemistry

OECD FORD branch

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Project

Result was created during the realization of more than one project. More information in the Projects tab.

Continuities

S - Specificky vyzkum na vysokych skolach<br>I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Publication year

2015

Confidentiality

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Name of the periodical

ChemCatChem

ISSN

1867-3880

e-ISSN

—

Volume of the periodical

7

Issue of the periodical within the volume

19

Country of publishing house

DE - GERMANY

Number of pages

11

Pages from-to

3152-3162

UT code for WoS article

000362553100011

EID of the result in the Scopus database

2-s2.0-84943427153