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

0428345 - MBÚ 2015 RIV US eng J - Journal Article
Slámová, Kristýna - Kulik, Natallia - Fiala, Martin - Krejzová, Jana - Ettrich, Rüdiger - Křen, Vladimír
Expression, characterization and homology modeling of a novel eukaryotic GH84 beta-N-acetylglucosaminidase from Penicillium chrysogenum.
Protein Expression and Purification. Roč. 95, MAR 2014 (2014), s. 204-210. ISSN 1046-5928. E-ISSN 1096-0279
R&D Projects: GA ČR(CZ) GAP207/11/0629; GA MŠMT(CZ) 7E11011
Institutional support: RVO:61388971 ; RVO:67179843
Keywords : beta-N-acetylglucosaminidase * Homology modeling * O-GlcNAcase
Subject RIV: EE - Microbiology, Virology
Impact factor: 1.695, year: 2014

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 were performed 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-acetylglucosaminidase
Permanent Link: http://hdl.handle.net/11104/0233700