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Enzymatic characterization and molecular modeling of an evolutionarily interesting fungal β-N-acetylhexosaminidase
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SYSNO ASEP 0366613 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Článek ve WOS Title Enzymatic characterization and molecular modeling of an evolutionarily interesting fungal β-N-acetylhexosaminidase Author(s) Ryšlavá, H. (CZ)
Kalendová, A. (CZ)
Doubnerová, V. (CZ)
Skočdopol, P. (CZ)
Kumar, V. (CZ)
Kukačka, Z. (CZ)
Pompach, Petr (MBU-M) RID, ORCID
Vaněk, Ondřej (MBU-M)
Slámová, Kristýna (MBU-M) RID, ORCID
Bojarová, Pavla (MBU-M) ORCID
Kulik, Natallia (UEK-B) RID
Ettrich, Rüdiger (UEK-B) RID, ORCID, SAI
Křen, Vladimír (MBU-M) RID, ORCID
Bezouška, Karel (MBU-M)Source Title FEBS Journal - ISSN 1742-464X
Roč. 278, č. 14 (2011), s. 2469-2484Number of pages 16 s. Language eng - English Country GB - United Kingdom Keywords deglycosylation ; enzyme kinetics ; hexosaminidase Subject RIV CE - Biochemistry R&D Projects LC06010 GA MŠMT - Ministry of Education, Youth and Sports (MEYS) 1M0505 GA MŠMT - Ministry of Education, Youth and Sports (MEYS) GA303/09/0477 GA ČR - Czech Science Foundation (CSF) GP203/09/P024 GA ČR - Czech Science Foundation (CSF) GD305/09/H008 GA ČR - Czech Science Foundation (CSF) CEZ AV0Z50200510 - MBU-M (2005-2011) AV0Z60870520 - UEK-B (2005-2011) UT WOS 000292932700007 DOI 10.1111/j.1742-4658.2011.08173.x Annotation 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 Workplace Institute of Microbiology Contact Eliška Spurná, eliska.spurna@biomed.cas.cz, Tel.: 241 062 231 Year of Publishing 2012
Number of the records: 1