Computational Modelling of Catalytic Properties and Modified Substrates of Fungal beta-N-Acetylhexosaminidases

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60076658%3A12640%2F11%3A43882314" target="_blank" >RIV/60076658:12640/11:43882314 - isvavai.cz</a>

Výsledek na webu

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DOI - Digital Object Identifier

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Jazyk výsledku

angličtina

Název v původním jazyce

Computational Modelling of Catalytic Properties and Modified Substrates of Fungal beta-N-Acetylhexosaminidases

Popis výsledku v původním jazyce

Besides their implication in human physiology and disease, beta-N-acetylhexosaminidases (EC 3.2.1.52, CAZy GH 20) have recently gained a lot of attention thanks to their great potential in the enzymatic synthesis of carbohydrates and glycomimetics. Extracellular beta-N-acetylhexosaminidases from filamentous fungi proved to be a powerful synthetic tool for the preparation of both natural and modified glycosides under mild conditions with good yields. A homology model of beta-N-acetylhexosaminidase from the filamentous fungus Aspergillus oryzae has recently been reported, and its quality was corroborated by vibrational spectroscopy and biochemical studies. Computational modelling and analysis helped to identify active site amino acids and other basic structural features of this enzyme important in the catalytic process; moreover, the surface interactions of the subunits of the glycosylated enzyme were identified. The model of beta-N-acetylhexosaminidase from Aspergillus oryzae prepared t

Název v anglickém jazyce

Computational Modelling of Catalytic Properties and Modified Substrates of Fungal beta-N-Acetylhexosaminidases

Popis výsledku anglicky

Besides their implication in human physiology and disease, beta-N-acetylhexosaminidases (EC 3.2.1.52, CAZy GH 20) have recently gained a lot of attention thanks to their great potential in the enzymatic synthesis of carbohydrates and glycomimetics. Extracellular beta-N-acetylhexosaminidases from filamentous fungi proved to be a powerful synthetic tool for the preparation of both natural and modified glycosides under mild conditions with good yields. A homology model of beta-N-acetylhexosaminidase from the filamentous fungus Aspergillus oryzae has recently been reported, and its quality was corroborated by vibrational spectroscopy and biochemical studies. Computational modelling and analysis helped to identify active site amino acids and other basic structural features of this enzyme important in the catalytic process; moreover, the surface interactions of the subunits of the glycosylated enzyme were identified. The model of beta-N-acetylhexosaminidase from Aspergillus oryzae prepared t

Druh

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

CEP obor

BO - Biofyzika

OECD FORD obor

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Projekt

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

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)<br>Z - Vyzkumny zamer (s odkazem do CEZ)<br>S - Specificky vyzkum na vysokych skolach

Rok uplatnění

2011

Kód důvěrnosti údajů

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

Název periodika

Mini-Reviews in Organic Chemistry

ISSN

1570-193X

e-ISSN

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Svazek periodika

8

Číslo periodika v rámci svazku

3

Stát vydavatele periodika

AE - Spojené arabské emiráty

Počet stran výsledku

11

Strana od-do

270-280

Kód UT WoS článku

000294408500008

EID výsledku v databázi Scopus

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