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Inhibition of microbial β-N-acetylhexosaminidases by 4-deoxy- and galacto-analogues of NAG-thiazoline
J. Krejzová, L. Kalachova, P. Šimon, H. Pelantová, K. Slámová, V. Křen,
Bioorganic & medicinal chemistry letters.
2014 ;
24 (22) :
5321-3.
[pub] 20141002
Jazyk angličtina Země Anglie, Velká Británie
Typ dokumentu časopisecké články, práce podpořená grantem
Perzistentní odkaz
https://www.medvik.cz/link/bmc15031677
- MeSH
- acetylglukosamin analogy a deriváty chemická syntéza chemie metabolismus MeSH
- Bacteroides enzymologie MeSH
- bakteriální proteiny antagonisté a inhibitory metabolismus MeSH
- beta-N-acetylhexosaminidasy antagonisté a inhibitory metabolismus MeSH
- fungální proteiny antagonisté a inhibitory metabolismus MeSH
- houby enzymologie MeSH
- kinetika MeSH
- Streptomyces enzymologie MeSH
- substrátová specifita MeSH
- thiazoly chemická syntéza chemie metabolismus MeSH
- vazba proteinů MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
NAG-thiazoline is a well-established competitive inhibitor of two physiologically relevant glycosidase families-β-N-acetylhexosaminidases (GH20) and β-N-acetylglucosaminidases (GH84). Based on the different substrate flexibilities of these enzyme groups, we designed and synthesized the 4-deoxy derivative of NAG-thiazoline aiming at the selective inhibition of GH20 β-N-acetylhexosaminidases. One GH84 and two GH20 microbial glycosidases were employed as model enzymes for the inhibition assays. Surprisingly, the new compound 4-deoxy-thiazoline exhibited no activity inhibition with either of the enzyme families of interest. Unlike with the substrates, the 4-hydroxyl group of the inhibitor's sugar ring seems to be crucial for binding the inhibitor to the active sites of these enzymes.
Citace poskytuje Crossref.org
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