Cloning, expression and characterization of Bombyx mori α1,6-fucosyltransferase.

Item request has been placed! ×
Item request cannot be made. ×
loading   Processing Request
Read More Add to Saved list
  • Author(s): Ihara H;Ihara H; Okada T; Okada T; Ikeda Y; Ikeda Y
  • Source:
    Biochemical and biophysical research communications [Biochem Biophys Res Commun] 2014 Jul 25; Vol. 450 (2), pp. 953-60. Date of Electronic Publication: 2014 Jun 25.
  • Publication Type:
    Journal Article; Research Support, Non-U.S. Gov't
  • Language:
    English
  • Additional Information
    • Source:
      Publisher: Elsevier Country of Publication: United States NLM ID: 0372516 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1090-2104 (Electronic) Linking ISSN: 0006291X NLM ISO Abbreviation: Biochem Biophys Res Commun Subsets: MEDLINE
    • Publication Information:
      Publication: <2002- >: San Diego, CA : Elsevier
      Original Publication: New York, Academic Press.
    • Subject Terms:
      Bombyx/*enzymology ; Fucosyltransferases/*chemistry; Amino Acid Sequence ; Animals ; Base Sequence ; Cell Line ; Cloning, Molecular ; Fucosyltransferases/genetics ; Fucosyltransferases/metabolism ; Glycosylation ; Humans ; Molecular Sequence Data ; Protein Multimerization ; Recombinant Proteins/chemistry ; Recombinant Proteins/genetics ; Sequence Alignment
    • Abstract:
      Although core α1,6-fucosylation is commonly observed in N-glycans of both vertebrates and invertebrates, the responsible enzyme, α1,6-fucosyltransferase, has been much less characterized in invertebrates compared to vertebrates. To investigate the functions of α1,6-fucosyltransferase in insects, we cloned the cDNA for the α1,6-fucosyltransferase from Bombyx mori (Bmα1,6FucT) and characterized the recombinant enzyme prepared using insect cell lines. The coding region of Bmα1,6FucT consists of 1737bp that code for 578 amino acids of the deduced amino acid sequence, showing significant similarity to other α1,6-fucosyltransferases. Enzyme activity assays demonstrated that Bmα1,6FucT is enzymatically active in spite of being less active compared to the human enzyme. The findings also indicate that Bmα1,6FucT, unlike human enzyme, is N-glycosylated and forms a disulfide-bonded homodimer. These findings contribute to a better understanding of roles of α1,6-fucosylation in invertebrates and also to the development of the more efficient engineering of N-glycosylation of recombinant glycoproteins in insect cells.
      (Copyright © 2014 Elsevier Inc. All rights reserved.)
    • Contributed Indexing:
      Keywords: Bombyx mori; Core α1,6-fucosylation; α1,6-Fucosyltransferase
    • Accession Number:
      0 (Recombinant Proteins)
      EC 2.4.1.- (Fucosyltransferases)
    • Publication Date:
      Date Created: 20140629 Date Completed: 20140924 Latest Revision: 20140725
    • Publication Date:
      20221213
    • Accession Number:
      10.1016/j.bbrc.2014.06.087
    • Accession Number:
      24973708