Počet záznamů: 1

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

  1. 1.
    0366613 - MBU-M 2012 RIV GB eng J - Článek v odborném periodiku
    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
    Grant CEP: GA MŠk(CZ) LC06010; GA MŠk 1M0505; GA ČR GA303/09/0477; GA ČR GP203/09/P024; GA ČR GD305/09/H008
    Výzkumný záměr: CEZ:AV0Z50200510; CEZ:AV0Z60870520
    Klíčová slova: deglycosylation * enzyme kinetics * hexosaminidase
    Kód oboru RIV: CE - Biochemie
    Impakt faktor: 3.790, rok: 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
    Trvalý link: http://hdl.handle.net/11104/0201536