Počet záznamů: 1
Enzymatic characterization and molecular modeling of an evolutionarily interesting fungal β-N-acetylhexosaminidase
- 1.0366613 - MBÚ 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. E-ISSN 1742-4658
Grant CEP: GA MŠMT(CZ) LC06010; GA MŠMT 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
Počet záznamů: 1