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.
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.
Nishihara
S
S
Division of Cell Biology, Institute of Life Science, Soka University, Tokyo, Japan.
Iwasaki
H
H
Kaneko
M
M
Tawada
A
A
Ito
M
M
Narimatsu
H
H
D000117:Acetylglucosamine / Q000378:metabolism*; D000606:Amino Sugars / Q000302:isolation & purification / Q000378:metabolism*; D002240:Carbohydrate Sequence; D002851:Chromatography, High Pressure Liquid; D005647:Fucosyltransferases / Q000235:genetics / Q000378:metabolism*; D006031:Glycosylation; D006801:Humans; D016256:Lewis X Antigen / Q000096:biosynthesis; D008969:Molecular Sequence Data; D011134:Polysaccharides / Q000302:isolation & purification / Q000378:metabolism*; D011994:Recombinant Proteins / Q000378:metabolism*; D013379:Substrate Specificity
D000606:Amino Sugars; D016256:Lewis X Antigen; D011134:Polysaccharides; D011994:Recombinant Proteins; C066929:polylactosamine; D005647:Fucosyltransferases; C031692:galactoside 3-fucosyltransferase; D000117:Acetylglucosamine