Inhibition of microbial ?-N-acetylhexosaminidases by 4-deoxy- and galacto-analogues of NAG-thiazoline
Result description
NAG-thiazoline is a well-established competitive inhibitor of two physiologically relevant glycosidase families??-N-acetylhexosaminidases (GH20) and ?-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 ?-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.
Keywords
The result's identifiers
Result code in IS VaVaI
Result on the web
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DOI - Digital Object Identifier
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Alternative languages
Result language
angličtina
Original language name
Inhibition of microbial ?-N-acetylhexosaminidases by 4-deoxy- and galacto-analogues of NAG-thiazoline
Original language description
NAG-thiazoline is a well-established competitive inhibitor of two physiologically relevant glycosidase families??-N-acetylhexosaminidases (GH20) and ?-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 ?-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.
Czech name
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Czech description
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Classification
Type
Jx - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
CE - Biochemistry
OECD FORD branch
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Result continuities
Project
Result was created during the realization of more than one project. More information in the Projects tab.
Continuities
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Others
Publication year
2014
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Bioorganic and Medicinal Chemistry Letters
ISSN
0960-894X
e-ISSN
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Volume of the periodical
24
Issue of the periodical within the volume
22
Country of publishing house
GB - UNITED KINGDOM
Number of pages
3
Pages from-to
5321-5323
UT code for WoS article
000343901400039
EID of the result in the Scopus database
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Basic information
Result type
Jx - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP
CE - Biochemistry
Year of implementation
2014