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
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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
CC - Organic chemistry
OECD FORD branch
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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
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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
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