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

被引：71

作者：

Nishihara, S

Iwasaki, H

Kaneko, M

Tawada, A

Ito, M

Narimatsu, H

机构：

[1] Soka Univ, Inst Life Sci, Div Cell Biol, Hachioji, Tokyo 1928577, Japan

[2] Seikagaku Corp, Tokyo Res Inst, Tokyo 2070021, Japan

[3] Soka Univ, Fac Engn, Dept Bioengn, Hachioji, Tokyo 1928577, Japan

来源：

FEBS LETTERS | 1999年 / 462卷 / 03期

关键词：

fucosyltransferase; 9; polylactosamine; Lewis x; stage-specific embryonal antigen-1; CD15;

D O I：

10.1016/S0014-5793(99)01549-5

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

We analyzed the substrate specificity of six human alpha 1,3-fucosyltransferases (alpha 1,3FUTs) for the 2-aminobenzamide (2AB)-labelled polylactosamine acceptor, Gal beta 1-4GlcNAc beta 1-3Gal beta 1-4GlcNAc beta 1-3Gal beta 1-4GlcNAc-2AB (3LN-2AB), FUT9 preferentially fucosylated the distal GlcNAc residue of the polylactosamine chain while the other four alpha 1,3FUT 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, (C) 1999 Federation of European Biochemical Societies.

引用

页码：289 / 294

页数：6

共 40 条

[1] BETA-GALACTOSIDASES FROM JACK BEAN MEAL AND ALMOND EMULSIN - APPLICATION FOR ENZYMATIC DISTINCTION OF GALBETA1-]4G1CNAC AND GALBETA1-]3G1CNAC LINKAGES [J].