Targeted Fucosylation of Glycans with Engineered Bacterial Fucosyltransferase Variants

Abstract: 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 α1,3FucT 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 (FucTΔ52A128N/H129E/Y132I/S46F, FucTΔ52‐4M) and the truncated α3FucT from H. pylori NCTC11639 (FucTΔ66). N‐Acetyllactosamine type 1 and type 2 as well as N’,N’’‐diacetyllactosamine were investigated as substrates. Both FucT variants exhibit α1,3/4FucT 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 FucTΔ52‐4M. Our work paves the way for targeted fucosylation patterns that can be tested for lectin binding.

Object Details

• Location: Deutsche Nationalbibliothek Frankfurt am Main
• Extent: Online-Ressource
• Language: Englisch

References and Relationships

• Bibliographic citation: Targeted Fucosylation of Glycans with Engineered Bacterial Fucosyltransferase Variants ; day:15 ; month:02 ; year:2022 ; extent:1 ; ChemCatChem ; (15.02.2022) (gesamt 1)

Contributors, Places and Time

• Creator: Heine, Viktoria ; Pelantová, Helena ; Bojarová, Pavla ; Křen, Vladimír ; Elling, Lothar

Further information

• DOI: 10.1002/cctc.202200037
• URN: urn:nbn:de:101:1-2022021614113603600115
• Rights: Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
• Last update: 15.08.2025, 7:30 AM CEST