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Acceptor Specificity of beta-N-Acetylhexosaminidase from Talaromyces flavus: A Rational Explanation

Identifikátory výsledku

  • Kód výsledku v IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F68407700%3A21460%2F19%3A00336103" target="_blank" >RIV/68407700:21460/19:00336103 - isvavai.cz</a>

  • Výsledek na webu

    <a href="https://doi.org/10.3390/ijms20246181" target="_blank" >https://doi.org/10.3390/ijms20246181</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.3390/ijms20246181" target="_blank" >10.3390/ijms20246181</a>

Alternativní jazyky

  • Jazyk výsledku

    angličtina

  • Název v původním jazyce

    Acceptor Specificity of beta-N-Acetylhexosaminidase from Talaromyces flavus: A Rational Explanation

  • Popis výsledku v původním jazyce

    Fungal beta-N-acetylhexosaminidases, though hydrolytic enzymes in vivo, are useful tools in the preparation of oligosaccharides of biological interest. The beta-N-acetylhexosaminidase from Talaromyces flavus is remarkable in terms of its synthetic potential, broad substrate specificity, and tolerance to substrate modifications. It can be heterologously produced in Pichia pastoris in a high yield. The mutation of the Tyr470 residue to histidine greatly enhances its transglycosylation capability. The aim of this work was to identify the structural requirements of this model beta-N-acetylhexosaminidase for its transglycosylation acceptors and formulate a structure-activity relationship study. Enzymatic reactions were performed using an activated glycosyl donor, 4-nitrophenyl N-acetyl-beta-d-glucosaminide or 4-nitrophenyl N-acetyl-beta-d-galactosaminide, and a panel of glycosyl acceptors of varying structural features (N-acetylglucosamine, glucose, N-acetylgalactosamine, galactose, N-acetylmuramic acid, and glucuronic acid). The transglycosylation products were isolated and structurally characterized. The C-2 N-acetamido group in the acceptor molecule was found to be essential for recognition by the enzyme. The presence of the C-2 hydroxyl moiety strongly hindered the normal course of transglycosylation, yielding unique non-reducing disaccharides in a low yield. Moreover, whereas the gluco-configuration at C-4 steered the glycosylation into the beta(1-4) position, the galacto-acceptor afforded a beta(1-6) glycosidic linkage. The Y470H mutant enzyme was tested with acceptors based on beta-glycosides of uronic acid and N-acetylmuramic acid. With the latter acceptor, we were able to isolate and characterize one glycosylation product in a low yield.

  • Název v anglickém jazyce

    Acceptor Specificity of beta-N-Acetylhexosaminidase from Talaromyces flavus: A Rational Explanation

  • Popis výsledku anglicky

    Fungal beta-N-acetylhexosaminidases, though hydrolytic enzymes in vivo, are useful tools in the preparation of oligosaccharides of biological interest. The beta-N-acetylhexosaminidase from Talaromyces flavus is remarkable in terms of its synthetic potential, broad substrate specificity, and tolerance to substrate modifications. It can be heterologously produced in Pichia pastoris in a high yield. The mutation of the Tyr470 residue to histidine greatly enhances its transglycosylation capability. The aim of this work was to identify the structural requirements of this model beta-N-acetylhexosaminidase for its transglycosylation acceptors and formulate a structure-activity relationship study. Enzymatic reactions were performed using an activated glycosyl donor, 4-nitrophenyl N-acetyl-beta-d-glucosaminide or 4-nitrophenyl N-acetyl-beta-d-galactosaminide, and a panel of glycosyl acceptors of varying structural features (N-acetylglucosamine, glucose, N-acetylgalactosamine, galactose, N-acetylmuramic acid, and glucuronic acid). The transglycosylation products were isolated and structurally characterized. The C-2 N-acetamido group in the acceptor molecule was found to be essential for recognition by the enzyme. The presence of the C-2 hydroxyl moiety strongly hindered the normal course of transglycosylation, yielding unique non-reducing disaccharides in a low yield. Moreover, whereas the gluco-configuration at C-4 steered the glycosylation into the beta(1-4) position, the galacto-acceptor afforded a beta(1-6) glycosidic linkage. The Y470H mutant enzyme was tested with acceptors based on beta-glycosides of uronic acid and N-acetylmuramic acid. With the latter acceptor, we were able to isolate and characterize one glycosylation product in a low yield.

Klasifikace

  • Druh

    J<sub>imp</sub> - Článek v periodiku v databázi Web of Science

  • CEP obor

  • OECD FORD obor

    10401 - Organic chemistry

Návaznosti výsledku

  • Projekt

  • Návaznosti

    V - Vyzkumna aktivita podporovana z jinych verejnych zdroju

Ostatní

  • Rok uplatnění

    2019

  • Kód důvěrnosti údajů

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

Údaje specifické pro druh výsledku

  • Název periodika

    International Journal of Molecular Sciences

  • ISSN

    1422-0067

  • e-ISSN

    1422-0067

  • Svazek periodika

    20

  • Číslo periodika v rámci svazku

    24

  • Stát vydavatele periodika

    CH - Švýcarská konfederace

  • Počet stran výsledku

    17

  • Strana od-do

  • Kód UT WoS článku

    000506840100075

  • EID výsledku v databázi Scopus

    2-s2.0-85076363105