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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
Author(s) -
Nishihara Shoko,
Iwasaki Hiroko,
Kaneko Mika,
Tawada Akira,
Ito Masato,
Narimatsu Hisashi
Publication year - 1999
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(99)01549-5
Subject(s) - chemistry , residue (chemistry) , fucosyltransferase , epitope , fucose , stereochemistry , fucosylation , acceptor , glycolipid , biochemistry , antigen , enzyme , galactose , biology , immunology , physics , condensed matter physics
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.