Enzymatic characterization and molecular modeling of an evolutionarily interesting fungal β-N-acetylhexosaminidase

0366613 - MBÚ 2012 RIV GB eng J - Journal Article
Ryšlavá, H. - Kalendová, A. - Doubnerová, V. - Skočdopol, P. - Kumar, V. - Kukačka, Z. - Pompach, Petr - Vaněk, Ondřej - Slámová, Kristýna - Bojarová, Pavla - Kulik, Natallia - Ettrich, Rüdiger - Křen, Vladimír - Bezouška, Karel
Enzymatic characterization and molecular modeling of an evolutionarily interesting fungal β-N-acetylhexosaminidase.
FEBS Journal. Roč. 278, č. 14 (2011), s. 2469-2484. ISSN 1742-464X. E-ISSN 1742-4658
R&D Projects: GA MŠMT(CZ) LC06010; GA MŠMT 1M0505; GA ČR GA303/09/0477; GA ČR GP203/09/P024; GA ČR GD305/09/H008
Institutional research plan: CEZ:AV0Z50200510; CEZ:AV0Z60870520
Keywords : deglycosylation * enzyme kinetics * hexosaminidase
Subject RIV: CE - Biochemistry
Impact factor: 3.790, year: 2011

Fungal b-N-acetylhexosaminidases are inducible extracellular enzymes with many biotechnological applications. The enzyme from Penicillium oxalicum has unique enzymatic properties despite its close evolutionary relationship with other fungal hexosaminidases. It has high GalNAcase activity, tolerates substrates with the modified N-acyl group better and has some other unusual catalytic properties. In order to understand these features, we performed isolation, biochemical and enzymological characterization, molecular cloning and molecular modelling. The native enzyme is composed of two catalytic units (65 kDa each) and two propeptides (15 kDa each), yielding a molecular weight of 160 kDa
Permanent Link: http://hdl.handle.net/11104/0201536