Fucosyltransferase 9. GDP-Fucose Lactosamine α1,3-Fucosyltransferase. Lex Specific (FUT9)

Reference work entry


Mouse α1,3-fucosyltransferase-IX (Fuc-TIX, Fut9) has been cloned as the sixth member of the α1,3-fucosyltransferase family by an expression cloning method for a mouse brain cDNA library (Kudo et al. 1998). The nucleotide and amino acid sequences of human α1,3-fucosyltransferase-IX (FUT9) are highly conserved in comparison with those of mouse Fut9, indicating that α1,3-fucosyltransferase-IX had been under a strong selective pressure during its evolution (Kaneko et al. 1999). The other five α1,3FUTs (FUT3, 4, 5, 6, and 7) share a highly homologous sequence, whereas the FUT9 amino acid sequence shows the lowest homology with other α1,3FUTs. FUT9 exhibited very strong activity for the Lewis x (Lex: Galβ1-4(Fucα1-3)GlcNAc) and Lewis y (Ley: Fucα1-2Galβ1-4(Fucα1-3)GlcNAc) synthesis, but not for the synthesis of sialyl Lewis x epitope (sLex: Siaα2-3Galβ1-4(Fucα1-3)GlcNAc). Moreover, FUT9 has more efficient activity for synthesis of the Lex carbohydrate epitope than other α1,3FUTs (Nishihara et al. 1999).


Neurite Outgrowth Placental Malaria GlcNAc Residue Namalwa Cell Placental Malaria Infection 
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Copyright information

© Springer Japan 2014

Authors and Affiliations

  1. 1.University of TsukubaTsukubaJapan
  2. 2.Research Center for Medical GlycoscienceNational Institute of Advanced Industrial Science and Technology (AIST)TsukubaJapan

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