Galactosylation of glycoconjugates using Pacific oyster β-1,3-galactosyltransferases.

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  • Additional Information
    • Source:
      Publisher: Elsevier Country of Publication: Netherlands NLM ID: 0043535 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1873-426X (Electronic) Linking ISSN: 00086215 NLM ISO Abbreviation: Carbohydr Res Subsets: MEDLINE
    • Publication Information:
      Publication: Amsterdam : Elsevier
      Original Publication: Amsterdam.
    • Subject Terms:
      Galactosyltransferases*/metabolism ; Galactosyltransferases*/chemistry ; Galactosyltransferases*/genetics ; Glycoconjugates*/chemistry ; Glycoconjugates*/metabolism; Animals ; Glycosylation ; Ostreidae/enzymology ; Galactose/metabolism ; Galactose/chemistry ; Polysaccharides/metabolism ; Polysaccharides/chemistry
    • Abstract:
      The Pacific oyster (Magallana gigas) exhibits an extensive diversity of N- and O-linked glycoconjugates, offering significant potential for biotechnological applications. Through genomic data mining, we have identified and characterized a suite of β-1,3-galactosyltransferase enzymes, pivotal for the synthesis of glycan structures. Out of ten cloned gene candidates, six enzymes were successfully expressed recombinantly in Escherichia coli. Four of these enzymes exhibited measurable catalytic activity in the transfer of galactose to various acceptor substrates. Notably, MgB3GalT1 demonstrated the highest efficiency, achieving a 91.2 % conversion rate. This enzyme was proficient in glycosylating diverse glycan structures, including Core 2 O-glycans and several di-, tri-, and tetra-antennary complex N-glycan standards. Mass spectrometric analysis confirmed the successful modification of N-glycans. These findings open new approaches for utilizing oyster-derived enzymes in glycan-based therapeutics and molecular glycoengineering, highlighting their utility in synthetic applications and biotechnological advancements.
      Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.
      (Copyright © 2024 Elsevier Ltd. All rights reserved.)
    • Contributed Indexing:
      Keywords: Enzymatic activity; Galactosylation; Glycoengineering; Pacific oyster; Recombinant expression; β-1,3-Galactosyltransferases
    • Accession Number:
      EC 2.4.1.- (Galactosyltransferases)
      0 (Glycoconjugates)
      X2RN3Q8DNE (Galactose)
      0 (Polysaccharides)
    • Publication Date:
      Date Created: 20240831 Date Completed: 20240909 Latest Revision: 20240909
    • Publication Date:
      20240910
    • Accession Number:
      10.1016/j.carres.2024.109254
    • Accession Number:
      39216435