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

Kód výsledku v 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>

Nalezeny alternativní kódy

RIV/61388971:_____/13:00395403

Výsledek na webu

<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>

Jazyk výsledku

angličtina

Název v původním jazyce

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

Popis výsledku v původním jazyce

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.

Název v anglickém jazyce

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

Popis výsledku anglicky

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.

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

CE - Biochemie

OECD FORD obor

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Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

Z - Vyzkumny zamer (s odkazem do CEZ)

Rok uplatnění

2013

Kód důvěrnosti údajů

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

Název periodika

Journal of Molecular Catalysis B

ISSN

1381-1177

e-ISSN

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Svazek periodika

87

Číslo periodika v rámci svazku

1

Stát vydavatele periodika

NL - Nizozemsko

Počet stran výsledku

7

Strana od-do

128-134

Kód UT WoS článku

000314012900019

EID výsledku v databázi Scopus

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