Alpha1,3-fucosyltransferase 9 (FUT9; Fuc-TIX) preferentially fucosylates the distal GlcNAc residue of polylactosamine chain while the other four alpha1,3FUT members preferentially fucosylate the inner GlcNAc residue

FEBS Lett. 1999 Dec 3;462(3):289-94. doi: 10.1016/s0014-5793(99)01549-5.

Abstract

We analyzed the substrate specificity of six human alpha1,3-fucosyltransferases (alpha1,3FUTs) for the 2-aminobenzamide (2AB)-labelled polylactosamine acceptor, Galbeta1-4GlcNAcbeta1-3Galbeta1-4GlcNAcbeta1- 3Galbeta1-4GlcNAc-2AB (3LN-2AB). FUT9 preferentially fucosylated the distal GlcNAc residue of the polylactosamine chain while the other four alpha1,3FUT 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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acetylglucosamine / metabolism*
  • Amino Sugars / isolation & purification
  • Amino Sugars / metabolism*
  • Carbohydrate Sequence
  • Chromatography, High Pressure Liquid
  • Fucosyltransferases / genetics
  • Fucosyltransferases / metabolism*
  • Glycosylation
  • Humans
  • Lewis X Antigen / biosynthesis
  • Molecular Sequence Data
  • Polysaccharides / isolation & purification
  • Polysaccharides / metabolism*
  • Recombinant Proteins / metabolism*
  • Substrate Specificity

Substances

  • Amino Sugars
  • Lewis X Antigen
  • Polysaccharides
  • Recombinant Proteins
  • polylactosamine
  • Fucosyltransferases
  • galactoside 3-fucosyltransferase
  • Acetylglucosamine