Expression, characterization and homology modeling of a novel eukaryotic GH84 beta-N-acetylglucosaminidase from Penicillium chrysogenum

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388971%3A_____%2F14%3A00428345" target="_blank" >RIV/61388971:_____/14:00428345 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/67179843:_____/14:00428345

Výsledek na webu

<a href="http://dx.doi.org/10.1016/j.pep.2014.01.002" target="_blank" >http://dx.doi.org/10.1016/j.pep.2014.01.002</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1016/j.pep.2014.01.002" target="_blank" >10.1016/j.pep.2014.01.002</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Expression, characterization and homology modeling of a novel eukaryotic GH84 beta-N-acetylglucosaminidase from Penicillium chrysogenum

Popis výsledku v původním jazyce

Beta-N-acetylglucosaminidases from the family 84 of glycoside hydrolases form a small group of glycosidases in eukaryotes responsible for the modification of nuclear and cytosolic proteins with O-GlcNAc, thus they are involved in a number of important cell processes. Here, the first fungal beta-N-acetylglucosaminidase from Penicillium chrysogenum was expressed in Pichia pastoris and secreted into the media, purified and characterized. Moreover, homology modeling and substrate and inhibitor docking wereperformed to obtain structural information on this new member of the GH84 family. Surprisingly, we found that this fungal beta-N-acetylglucosaminidase with its sequence and structure perfectly fitting to the GH84 family displays biochemical properties rather resembling the beta-N-acetylhexosaminidases from the family 20 of glycoside hydrolases. This work helped to increase the knowledge on the scarcely studied glycosidase family and revealed a new type of eukaryotic beta-N-acetylglucosam

Název v anglickém jazyce

Expression, characterization and homology modeling of a novel eukaryotic GH84 beta-N-acetylglucosaminidase from Penicillium chrysogenum

Popis výsledku anglicky

Beta-N-acetylglucosaminidases from the family 84 of glycoside hydrolases form a small group of glycosidases in eukaryotes responsible for the modification of nuclear and cytosolic proteins with O-GlcNAc, thus they are involved in a number of important cell processes. Here, the first fungal beta-N-acetylglucosaminidase from Penicillium chrysogenum was expressed in Pichia pastoris and secreted into the media, purified and characterized. Moreover, homology modeling and substrate and inhibitor docking wereperformed to obtain structural information on this new member of the GH84 family. Surprisingly, we found that this fungal beta-N-acetylglucosaminidase with its sequence and structure perfectly fitting to the GH84 family displays biochemical properties rather resembling the beta-N-acetylhexosaminidases from the family 20 of glycoside hydrolases. This work helped to increase the knowledge on the scarcely studied glycosidase family and revealed a new type of eukaryotic beta-N-acetylglucosam

Druh

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

CEP obor

EE - Mikrobiologie, virologie

OECD FORD obor

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Projekt

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

Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2014

Kód důvěrnosti údajů

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

Název periodika

Protein Expression and Purification

ISSN

1046-5928

e-ISSN

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Svazek periodika

95

Číslo periodika v rámci svazku

MAR 2014

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

7

Strana od-do

204-210

Kód UT WoS článku

000332192900029

EID výsledku v databázi Scopus

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