Plant members of the α1→3/4-fucosyltransferase gene family encode an α1→4-fucosyltransferase, potentially involved in Lewisabiosynthesis, and two core α1→3-fucosyltransferases1
| ISSN: | 0014-5793 |
|---|---|
| Přístupová URL adresa: | https://explore.openaire.eu/search/publication?articleId=doi_________::6a48fe633a0c63472de600bf2d7464d8 https://doi.org/10.1016/s0014-5793(01)02999-4 |
| Rights: | CLOSED |
| Přírůstkové číslo: | edsair.doi...........6a48fe633a0c63472de600bf2d7464d8 |
| Autor: | Theodora de Vries, Elio Schijlen, Hans Bakker, Wietske E. C. M. Schiphorst, Arjen Lommen, Wilco Jordi, Irma van Die, Dirk Bosch |
| Rok vydání: | 2001 |
| Předmět: |
Glycan
Fucosyltransferase biology cDNA library Biophysics Cell Biology biology.organism_classification Biochemistry Molecular biology Fucose law.invention chemistry.chemical_compound chemistry Structural Biology law Genetics biology.protein Recombinant DNA Gene family Arabidopsis thaliana Molecular Biology Gene |
| Zdroj: | FEBS Letters. 507:307-312 |
| ISSN: | 0014-5793 |
| Popis: | Three putative alpha1-->3/4-fucosyltransferase (alpha1-->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 alpha1-->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 Galbeta1-->3GlcNAcbeta1-->3Galbeta1-->4Glc. Analysis of the product by 400 MHz (1)H-nuclear magnetic resonance spectroscopy showed that the product is alpha1-->4-fucosylated at the N-acetylglucosamine residue. In vitro, the recombinant B. vulgaris alpha1-->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. |
| Databáze: | OpenAIRE |
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