α1,3-Fucosyltransferase 9 (FUT9; Fuc-TIX) preferentially fucosylates the distal GlcNAc residue of polylactosamine chain while the other four α1,3FUT members preferentially fucosylate the inner GlcNAc residue

Shoko Nishihara, Hiroko Iwasaki, Mika Kaneko, Akira Tawada, Masato Ito, Hisashi Narimatsu

Research output: Contribution to journalArticle

70 Citations (Scopus)

Abstract

We analyzed the substrate specificity of six human α1,3-fucosyltransferases (α1,3FUTs) for the 2-aminobenzamide (2AB)-labelled polylactosamine acceptor, Galβ1-4GlcNAcβ1-3Galβ1-4GlcNAcβ1-3Galβ1-4GlcNAc-2AB (3LN-2AB). FUT9 preferentially fucosylated the distal GlcNAc residue of the polylactosamine chain while the other four α1,3FUT members, FUT3, FUT4, FUT5 and FUT6, preferentially fucosylated the inner GlcNAc residue. This indicated that FUT9 exhibits more efficient activity for the synthesis of Lewis x carbohydrate epitope (Le(x); CD15; stage-specific embryonal antigen-1 (SSEA-1)). In contrast, the other four members synthesize more effectively the internal Le(x) epitope. FUT7 could not transfer a fucose to an acceptor which is non-sialylated. Copyright (C) 1999 Federation of European Biochemical Societies.

Original languageEnglish
Pages (from-to)289-294
Number of pages6
JournalFEBS Letters
Volume462
Issue number3
DOIs
Publication statusPublished - 1999 Dec 3

Keywords

  • CD15
  • Fucosyltransferase 9
  • Lewis x
  • Polylactosamine
  • Stage-specific embryonal antigen-1

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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