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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

  • Czech description

Classification

  • Type

    J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

  • CEP classification

    CE - Biochemistry

  • OECD FORD branch

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

  • 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