http://www.cnr.it/ontology/cnr/individuo/prodotto/ID167402
Beta-N-Acetylhexosaminidases accept 4-deoxy-N-acetylhexosaminides as substrates (Articolo in rivista)
- Type
- Label
- Beta-N-Acetylhexosaminidases accept 4-deoxy-N-acetylhexosaminides as substrates (Articolo in rivista) (literal)
- Anno
- 2009-01-01T00:00:00+01:00 (literal)
- Alternative label
Slamova K. , Bojarova P., Gazak R., Tramice A., Kulik N., Mackova M., Kren V., (2009)
Beta-N-Acetylhexosaminidases accept 4-deoxy-N-acetylhexosaminides as substrates
in The FEBS journal (Print)
(literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
- Slamova K. , Bojarova P., Gazak R., Tramice A., Kulik N., Mackova M., Kren V., (literal)
- Pagina inizio
- Pagina fine
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
- 276, Issue Supplement s1 (literal)
- Rivista
- Note
- ISI Web of Science (WOS) (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
- K. Slamova1, P. Bojarova1, R. Gazak1, A. Tramice2, N. Kulik3,
M. Mackova4 and V. Kren1
1Laboratory of Biotransformation, Institute of Microbiology, Prague
4, CZECH REPUBLIC, 2Istituto di Chimica Biomolecolare
CNR, Istituto di Chimica Biomolecolare, Napoli, ITALY, 3Laboratory
of High Performance Computing, Institute of Systems Biology
and Ecology AV CR, Nove Hrady, CZECH REPUBLIC,
4Department of Biochemistry and Microbiology, Institute of
Chemical Technology, Prague 6, CZECH REPUBLIC (literal)
- Titolo
- Beta-N-Acetylhexosaminidases accept 4-deoxy-N-acetylhexosaminides as substrates (literal)
- Abstract
- b-N-Acetylhexosaminidases (EC 3.2.1.52, CAZy GH20) possess
so called wobbling specificity, which means that they cleave substrates
both in gluco- and galacto- configurations, with the activity
ratio depending on the enzyme source. Here we present a new
finding that fungal b-N-acetylhexosaminidases are also able to
hydrolyze and transfer 4-deoxy-N-acetylhexosaminides. This fact
clearly demonstrates that the 4-hydroxy moiety at the substrate
pyranose is not essential for the binding of the substrate to the
enzyme's active site, which was also confirmed by molecular
docking of the tested compounds into the model of the active site
of b-N-acetylhexosaminidase from Aspergillus oryzae. A set of
four 4-deoxy-N-acetylhexosaminides was prepared via chemical
synthesis and screened against a panel of b-N-acetylhexosaminidases
from various types of sources (fungal, human, animal, plant
and bacterial representatives) for hydrolysis. The results of this
screening as well as structures of 4-deoxy disaccharides prepared
by transglycosylation reaction using b-N-acetylhexosaminidase
fromTalaromyces flavus are reported. This structure-function relationship
study will be used in the design of new b-N-acetylhexosaminidase
inhibitors and for the synthesis of novel type of
glycomimetics. (literal)
- Prodotto di
- Autore CNR
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