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An investigation of nitrile transforming enzymes in the chemo-enzymatic synthesis of the taxol sidechain

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388971%3A_____%2F15%3A00448779" target="_blank" >RIV/61388971:_____/15:00448779 - isvavai.cz</a>

  • Result on the web

    <a href="http://dx.doi.org/10.1039/c5ob01191d" target="_blank" >http://dx.doi.org/10.1039/c5ob01191d</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1039/c5ob01191d" target="_blank" >10.1039/c5ob01191d</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    An investigation of nitrile transforming enzymes in the chemo-enzymatic synthesis of the taxol sidechain

  • Original language description

    Paclitaxel (taxol) is an antimicrotubule agent widely used in the treatment of cancer. Taxol is prepared in a semisynthetic route by coupling the N-benzoyl-(2R, 3S)-3-phenylisoserine sidechain to the baccatin III core structure. Precursors of the taxol sidechain have previously been prepared in chemoenzymatic approaches using acylases, lipases, and reductases, mostly featuring the enantioselective, enzymatic step early in the reaction pathway. Here, nitrile hydrolysing enzymes, namely nitrile hydratasesand nitrilases, are investigated for the enzymatic hydrolysis of two different sidechain precursors. Both sidechain precursors, an openchain alpha-hydroxy-beta-amino nitrile and a cyanodihydrooxazole, are suitable for coupling to baccatin III directly after the enzymatic step. An extensive set of nitrilases and nitrile hydratases was screened towards their activity and selectivity in the hydrolysis of two taxol sidechain precursors and their epimers. A number of nitrilases and nitrile h

  • Czech name

  • Czech description

Classification

  • Type

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

  • CEP classification

    CC - Organic chemistry

  • OECD FORD branch

Result continuities

  • Project

    <a href="/en/project/GAP504%2F11%2F0394" target="_blank" >GAP504/11/0394: Interspecies comparison of nitrilases by using recombinant enzymes obtained by database-mining: their environmental impact and potential application</a><br>

  • Continuities

    I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Others

  • Publication year

    2015

  • Confidentiality

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

Data specific for result type

  • Name of the periodical

    Organic & Biomolecular Chemistry

  • ISSN

    1477-0520

  • e-ISSN

  • Volume of the periodical

    13

  • Issue of the periodical within the volume

    28

  • Country of publishing house

    GB - UNITED KINGDOM

  • Number of pages

    10

  • Pages from-to

    7803-7812

  • UT code for WoS article

    000358243200023

  • EID of the result in the Scopus database