Expression, characterization and homology modeling of a novel eukaryotic GH84 beta-N-acetylglucosaminidase from Penicillium chrysogenum
The result's identifiers
Result code in 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>
Alternative codes found
RIV/67179843:_____/14:00428345
Result on the web
<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>
Alternative languages
Result language
angličtina
Original language name
Expression, characterization and homology modeling of a novel eukaryotic GH84 beta-N-acetylglucosaminidase from Penicillium chrysogenum
Original language description
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
Czech name
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Czech description
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Classification
Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
EE - Microbiology, virology
OECD FORD branch
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Result continuities
Project
Result was created during the realization of more than one project. More information in the Projects tab.
Continuities
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Others
Publication year
2014
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Protein Expression and Purification
ISSN
1046-5928
e-ISSN
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Volume of the periodical
95
Issue of the periodical within the volume
MAR 2014
Country of publishing house
US - UNITED STATES
Number of pages
7
Pages from-to
204-210
UT code for WoS article
000332192900029
EID of the result in the Scopus database
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