Towards Keratan Sulfate - Chemoenzymatic Cascade Synthesis of Sulfated N-Acetyllactosamine (LacNAc) Glycan Oligomers
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388971%3A_____%2F16%3A00460034" target="_blank" >RIV/61388971:_____/16:00460034 - isvavai.cz</a>
Result on the web
<a href="http://dx.doi.org/10.1002/adsc.201500916" target="_blank" >http://dx.doi.org/10.1002/adsc.201500916</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1002/adsc.201500916" target="_blank" >10.1002/adsc.201500916</a>
Alternative languages
Result language
angličtina
Original language name
Towards Keratan Sulfate - Chemoenzymatic Cascade Synthesis of Sulfated N-Acetyllactosamine (LacNAc) Glycan Oligomers
Original language description
We report on a novel chemoenzymatic cascade for the synthesis of sulfated N-acetyllactosamine [(3Gal1,4GlcNAc1,)(n), LacNAc] oligomer structures. Starting from a linker modified GlcNAc substrate di- and trisaccharides were first synthesized by sequential use of human 4-galactosyltransferase-1 (4GalT-1) and 3-N-acetylglucosaminyltransferase from Helicobacter pylori (3GlcNAcT). Subsequent regioselective chemical sulfation rendered the C-6 mono-, di-, and tri-O-sulfated products in good yields. Further enzymatic elongation by 4GalT-1 and 3GlcNAcT in a sequential mode yielded 6-O-sulfated LacNAc oligomers up to hexasaccharide length with variable degrees of sulfation. These carbohydrate structures mimic the sulfation pattern found in keratan sulfate and are potential ligands for different classes of glycan binding proteins.
Czech name
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Czech description
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Classification
Type
J<sub>x</sub> - 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
2016
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Advanced Synthesis & Catalysis
ISSN
1615-4150
e-ISSN
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Volume of the periodical
358
Issue of the periodical within the volume
4
Country of publishing house
DE - GERMANY
Number of pages
13
Pages from-to
584-596
UT code for WoS article
000371665800013
EID of the result in the Scopus database
2-s2.0-84958753505