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A Redox-Controlled Substrate Engineering Strategy for Site-Specific Enzymatic Fucosylation.

Na Lu1, Yun Li2,3, Hui Xia1

  • 1National Glycoengineering Research Center, NMPA Key Laboratory for Quality Research and Evaluation of Carbohydrate-Based Medicine, and Shandong Key Laboratory of Carbohydrate Chemistry and Glycobiology, Shandong University, Qingdao, 266237, China.

Angewandte Chemie (International Ed. in English)
|October 17, 2022
PubMed
Summary
This summary is machine-generated.

Researchers developed a novel redox-controlled method for site-specific fucosylation of complex glycans. This strategy enables precise attachment of alpha1,3-linked fucose to oligo-N-acetyllactosamine (oligo-LacNAc) structures using engineered enzymes.

Keywords:
fucosylationgalactose oxidaseglycosideglycosylationoligo-LacNAc glycans

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Area of Science:

  • Biochemistry
  • Glycobiology
  • Enzymology

Background:

  • Fucosylation is a common glycan modification, crucial for biological processes.
  • Existing fucosyltransferases (FucTs) lack site-specificity for alpha1,3-fucosylation on oligo-N-acetyllactosamine (oligo-LacNAc) substrates.
  • Precise control over glycan structure is essential for understanding and manipulating biological functions.

Purpose of the Study:

  • To develop a general and facile strategy for site-specific alpha1,3-fucosylation of complex glycans.
  • To overcome the limitations of current fucosyltransferases in achieving regioselective fucosylation.
  • To enable the synthesis of well-defined fucosylated glycans for further research.

Main Methods:

  • Employed a redox-controlled substrate engineering approach.
  • Utilized galactose oxidase (GOase) to selectively oxidize oligo-LacNAc units to an aldehyde intermediate.
  • Leveraged the engineered substrate's altered reactivity with recombinant alpha1,3-FucT from Helicobacter pylori (Hpα1,3FucT) for site-specific fucosylation.

Main Results:

  • Demonstrated a robust method for site-specific alpha1,3-fucosylation of oligo-LacNAc.
  • Successfully synthesized various structurally defined fucosides of linear and branched O- and N-linked glycans.
  • The engineered oxidized LacNAc unit selectively directed fucosylation to intact LacNAc sites.

Conclusions:

  • The developed strategy provides a powerful tool for the site-specific synthesis of complex fucosylated glycans.
  • This approach offers broad applicability for engineering diverse glycan structures.
  • The method overcomes previous limitations in achieving regioselective alpha1,3-fucosylation, advancing glycan synthesis and research.