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Enzymatic Synthesis of New C-6-Acylated Derivatives of NAG-Thiazoline and Evaluation of their Inhibitor Activities Towards Fungal beta-N-Acetylhexosaminidase

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60461373%3A22330%2F13%3A43893970" target="_blank" >RIV/60461373:22330/13:43893970 - isvavai.cz</a>

  • Alternative codes found

    RIV/61388971:_____/13:00395403

  • Result on the web

    <a href="http://dx.doi.org/10.1016/j.molcatb.2012.10.016" target="_blank" >http://dx.doi.org/10.1016/j.molcatb.2012.10.016</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1016/j.molcatb.2012.10.016" target="_blank" >10.1016/j.molcatb.2012.10.016</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Enzymatic Synthesis of New C-6-Acylated Derivatives of NAG-Thiazoline and Evaluation of their Inhibitor Activities Towards Fungal beta-N-Acetylhexosaminidase

  • Original language description

    beta-N-Acetylhexosaminidases (EC 3.2.1.52) from the CAZy glycoside hydrolase families 20 and 84 are two distinct enzyme groups with similar reactivity and different physiological functions, thus selective inhibition of these enzymes is of crucial importance. Here, we report on the lipase-catalyzed synthesis of a set of novel monomeric and dimeric C-6-acylated derivatives of NAG-thiazoline, which is a typical competitive inhibitor of both these enzyme classes. The prepared compounds were tested as potential inhibitors of a fungal GH20 beta-N-acetylhexosaminidase from Talaromyces flavus, however, the results of the inhibition tests were quite ambiguous. The observed inhibition was generally weak with some features of competitive inhibition (increase of KM), but the overall pattern appeared indecisive.

  • 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

    Z - Vyzkumny zamer (s odkazem do CEZ)

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

  • ISSN

    1381-1177

  • e-ISSN

  • Volume of the periodical

    87

  • Issue of the periodical within the volume

    1

  • Country of publishing house

    NL - THE KINGDOM OF THE NETHERLANDS

  • Number of pages

    7

  • Pages from-to

    128-134

  • UT code for WoS article

    000314012900019

  • EID of the result in the Scopus database