Protecting‐Group‐Controlled Enzymatic Glycosylation of Oligo‐<i>N</i>‐Acetyllactosamine Derivatives

Gagarinov, Ivan A.; Li, Tiehai; Wei, Na; Toraño, Javier Sastre; Vries, Robert P. de; Wolfert, Margreet A.; Boons, Geert‐Jan

doi:10.1002/ange.201903140

Cited by 6 publications

(2 citation statements)

References 30 publications

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“…So far, only two known approaches have recently been developed for the site‐specific enzymatic fucosylation of oligo‐LacNAc glycans. In 2019, Boons and co‐workers reported a protecting‐group controlled site‐specific enzymatic fucosylation strategy (Scheme 1a, i), [18] in which a chemically synthesized tri‐LacNAc hexasaccharide with orthogonal protected amine groups was used as the common substrate for site‐specific enzymatic fucosylation. The lacotosamine units containing either free amine or tert ‐butyloxycarbonyl (Boc) protecting group are not tolerated by both human and bacterial α1,3‐fucosyltransferases, thus the α1,3‐fucosylation could only take place at the intact LacNAc unit [18] .…”

Section: Introductionmentioning

confidence: 99%

“…In 2019, Boons and co‐workers reported a protecting‐group controlled site‐specific enzymatic fucosylation strategy (Scheme 1a, i), [18] in which a chemically synthesized tri‐LacNAc hexasaccharide with orthogonal protected amine groups was used as the common substrate for site‐specific enzymatic fucosylation. The lacotosamine units containing either free amine or tert ‐butyloxycarbonyl (Boc) protecting group are not tolerated by both human and bacterial α1,3‐fucosyltransferases, thus the α1,3‐fucosylation could only take place at the intact LacNAc unit [18] . This protecting group controlled site‐specific fucosylation strategy nicely combined the flexibility of chemical synthesis and efficiency of enzymatic glycosylation.…”

Section: Introductionmentioning

confidence: 99%

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A Redox‐Controlled Substrate Engineering Strategy for Site‐Specific Enzymatic Fucosylation

et al. 2022

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Fucosylation is one of the most common modifications of oligo-N-acetyllactosamine (oligo-Lac-NAc) glycans. However, none of known fucosyltransferases (FucTs) could install the α1,3-linked fucose to the oligo-LacNAc substrates in a site-specific manner. Here, we report a facile and general redox-controlled substrate engineering strategy for the site-specific α1,3-fucosylation of complex glycans containing multiple LacNAc units. This strategy takes advantage of an operationally simple oxidation enzyme module by using galactose oxidase (GOase) to convert the LacNAc unit into oxidized C6'-aldehyde LacNAc sequence, which is not a good substrate for recombinant α1,3-FucT from Helicobacter pylori strain 26695 (Hpα1,3FucT), enabling the site-specific α1,3-fucosylation at intact LacNAc sites. The general applicability and robustness of this strategy were demonstrated by the synthesis of a variety of structurally well-defined fucosides of linear and branched O-and N-linked glycans.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

A Redox‐Controlled Substrate Engineering Strategy for Site‐Specific Enzymatic Fucosylation

et al. 2022

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Ion‐Mobility Spectrometry Can Assign Exact Fucosyl Positions in Glycans and Prevent Misinterpretation of Mass‐Spectrometry Data After Gas‐Phase Rearrangement

et al. 2019

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The fucosylation of glycans leads to diverse structures and is associated with many biological and disease processes. The exact determination of fucoside positions by tandem mass spectrometry (MS/MS) is complicated because rearrangements in the gas phase lead to erroneous structural assignments. Here, we demonstrate that the combined use of ion‐mobility MS and well‐defined synthetic glycan standards can prevent misinterpretation of MS/MS spectra and incorrect structural assignments of fucosylated glycans. We show that fucosyl residues do not migrate to hydroxyl groups but to acetamido moieties of N‐acetylneuraminic acid as well as N‐acetylglucosamine residues and nucleophilic sites of an anomeric tag, yielding specific isomeric fragment ions. This mechanistic insight enables the characterization of unique IMS arrival‐time distributions of the isomers which can be used to accurately determine fucosyl positions in glycans.

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Systematic Enzymatic Synthesis of dTDP‐Activated Sugar Nucleotides

et al. 2023

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Deoxythymidine diphosphate (dTDP)‐activated sugar nucleotides are the most diverse sugar nucleotides in nature. They serve as the glycosylation donors of glycosyltransferases to produce various carbohydrate structures in living organisms. However, most of the dTDP‐sugars are difficult to obtain due to synthetic difficulties. The limited availability of dTDP‐sugars has hindered progress in investigating the biosynthesis of carbohydrates and exploring new glycosyltransferases in nature. In this study, based on the de novo and salvage biosynthetic pathways, a variety of dTDP‐activated sugar nucleotides were successfully prepared in high yields and on a large scale from readily available starting materials. The produced sugar nucleotides could provide effective tools for fundamental research in glycoscience.

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Protecting‐Group‐Controlled Enzymatic Glycosylation of Oligo‐N‐Acetyllactosamine Derivatives

Abstract: Supportinginformation and the ORCID identification number(s) for the author(s) of this article can be found under: https://doi.

Cited by 6 publications

References 30 publications

A Redox‐Controlled Substrate Engineering Strategy for Site‐Specific Enzymatic Fucosylation

A Redox‐Controlled Substrate Engineering Strategy for Site‐Specific Enzymatic Fucosylation

Ion‐Mobility Spectrometry Can Assign Exact Fucosyl Positions in Glycans and Prevent Misinterpretation of Mass‐Spectrometry Data After Gas‐Phase Rearrangement

Systematic Enzymatic Synthesis of dTDP‐Activated Sugar Nucleotides

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