Plant members of the α1→3/4‐fucosyltransferase gene family encode an α1→4‐fucosyltransferase, potentially involved in Lewisa biosynthesis, and two core α1→3‐fucosyltransferases1

FEBS Letters

van Die, Irma¹  Schiphorst, Wietske E.C.M.¹  Bakker, Hans²  Jordi, Wilco²  de Vries, Theodora⁴  Lommen, Arjen³  Bosch, Dirk²  Schijlen, Elio² 

[1] Department of Molecular Cell Biology, Glycoimmunology Group, VU University Medical Center, Van der Boechorststraat 7, 1081 BT Amsterdam, The Netherlands;Plant Research International, Wageningen University and Research Centre, P.O. Box 16, 6700 AA Wageningen, The Netherlands;State Institute for Quality Control of Agricultural Products (RIKILT), Wageningen University and Research Centre, P.O. Box 230, 6700 AE Wageningen, The Netherlands;Department of Chemistry and Biochemistry, San Francisco State University, San Francisco, CA 94132, USA

关键词: Fucose;    Fucosyltransferase;    Glycosyltransferase;    Lewisa;    GlcNAc;    N-acetylglucosamine;    Fuc;    fucose;    FucT(-C3);    (core α1→3-)fucosyltransferase;    EST;    expressed sequence tag;    LNT;    lacto-N-tetraose;    LNFP II;    lacto-N-fucopentaose II;   

DOI  :  10.1016/S0014-5793(01)02999-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Three putative α1→3/4-fucosyltransferase (α1→3/4-FucT) genes have been detected in the Arabidopsis thaliana genome. The products of two of these genes have been identified in vivo as core α1→3-FucTs involved in N-glycosylation. An orthologue of the third gene was isolated from a Beta vulgaris cDNA library. The encoded enzyme efficiently fucosylates Galβ1→3GlcNAcβ1→3Galβ1→4Glc. Analysis of the product by 400 MHz ¹H-nuclear magnetic resonance spectroscopy showed that the product is α1→4-fucosylated at the N-acetylglucosamine residue. In vitro, the recombinant B. vulgaris α1→4-FucT acts efficiently only on neutral type 1 chain-based glycan structures. In plants the enzyme is expected to be involved in Lewis^a formation on N-linked glycans.

【 授权许可】

Unknown