Targeted Fucosylation of Glycans with Engineered Bacterial Fucosyltransferase Variants
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388971%3A_____%2F22%3A00560769" target="_blank" >RIV/61388971:_____/22:00560769 - isvavai.cz</a>
Result on the web
<a href="https://chemistry-europe.onlinelibrary.wiley.com/doi/10.1002/cctc.202200037" target="_blank" >https://chemistry-europe.onlinelibrary.wiley.com/doi/10.1002/cctc.202200037</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1002/cctc.202200037" target="_blank" >10.1002/cctc.202200037</a>
Alternative languages
Result language
angličtina
Original language name
Targeted Fucosylation of Glycans with Engineered Bacterial Fucosyltransferase Variants
Original language description
Fucosyltransferases (FucTs) are crucial for the synthesis of Lewis-type glycan epitopes. The synthetic capacity of efficient bacterial enzymes and their variants has not yet been fully exploited. In the present work, we investigated two previously described variants of a1,3FucT from Helicobacter pylori strains for their flexibility in substrate utilization and their applicability in the enzymatic synthesis of Lewis epitopes. We used the truncated enzyme variant of FutA from H. pylori 26695 (FucT Delta 52A128N/H129E/Y132I/S46F, FucT Delta 52-4M) and the trun-cated alpha 3FucT from H. pylori NCTC11639 (FucT.66). N-Acetyllactosamine type 1 and type 2 as well as N',N''-diacetyllactosamine were investigated as substrates. Both FucT variants exhibit alpha 1,3/4FucT activity. Novel glycan structures were obtained displaying Lewis blood group antigens in a site-specific sequence. Fucosylated N',N''-diacetyllactosamine was synthesized for the first time with FucT Delta 52-4M. Our work paves the way for targeted fucosylation patterns that can be tested for lectin binding.
Czech name
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Czech description
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Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
10608 - Biochemistry and molecular biology
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
2022
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
ChemCatChem
ISSN
1867-3880
e-ISSN
1867-3899
Volume of the periodical
14
Issue of the periodical within the volume
6
Country of publishing house
DE - GERMANY
Number of pages
9
Pages from-to
e202200037
UT code for WoS article
000755356100001
EID of the result in the Scopus database
2-s2.0-85124601570