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
—