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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

  • Czech description

Classification

  • Type

    J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

  • CEP classification

    EE - Microbiology, virology

  • OECD FORD branch

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

  • 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