Preparation of silybin and isosilybin sulfates by sulfotransferase from Desulfitobacterium hafniense
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11310%2F13%3A10192041" target="_blank" >RIV/00216208:11310/13:10192041 - isvavai.cz</a>
Alternative codes found
RIV/61388971:_____/13:00395307 RIV/61388963:_____/13:00395307
Result on the web
<a href="http://dx.doi.org/10.1016/j.molcatb.2012.12.005" target="_blank" >http://dx.doi.org/10.1016/j.molcatb.2012.12.005</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1016/j.molcatb.2012.12.005" target="_blank" >10.1016/j.molcatb.2012.12.005</a>
Alternative languages
Result language
angličtina
Original language name
Preparation of silybin and isosilybin sulfates by sulfotransferase from Desulfitobacterium hafniense
Original language description
Flavonolignans silybin and isosilybin are major components of silymarin complex isolated from seeds of the milk thistle (Silybum marianum) featuring strong antioxidant and hepatoprotective effects, and also anticancer, chemoprotective, dermatoprotectiveand hypocholesterolemic activities. Natural silybin and isosilybin are mixtures of diastereoisomers: silybin/isosilybin A (1a, 1b) and silybin/isosilybin B (2a, 2b). The metabolism of these compounds is supposed to be strongly linked to Phase II of biotransformation and the respective conjugates are rapidly excreted in bile and urine. The aim of this study was to obtain optically pure sulfated metabolites of both silybins and isosilybins. Aryl-sulfate sulfotransferase (EC 2.8.2.22) from Desulfitobacterium hafniense was found to be a highly effective tool for the regiospecific enzymatic synthesis of silybin A-20-O-sulfate, silybin B-20-O-sulfate, isosilybin A-20-O-sulfate and isosilybin B-20-O-sulfate providing nearly quantitative yields
Czech name
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Czech description
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Classification
Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
CE - Biochemistry
OECD FORD branch
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Result continuities
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
Others
Publication year
2013
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Journal of Molecular Catalysis - B Enzymatic
ISSN
1381-1177
e-ISSN
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Volume of the periodical
89
Issue of the periodical within the volume
May (2013)
Country of publishing house
NL - THE KINGDOM OF THE NETHERLANDS
Number of pages
4
Pages from-to
24-27
UT code for WoS article
000315552300004
EID of the result in the Scopus database
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