rdf:type |
|
lifeskim:mentions |
|
pubmed:issue |
3
|
pubmed:dateCreated |
2001-11-6
|
pubmed:databankReference |
|
pubmed:abstractText |
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.
|
pubmed:language |
eng
|
pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
|
pubmed:status |
MEDLINE
|
pubmed:month |
Nov
|
pubmed:issn |
0014-5793
|
pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:day |
2
|
pubmed:volume |
507
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
307-12
|
pubmed:dateRevised |
2008-8-15
|
pubmed:meshHeading |
pubmed-meshheading:11696361-Acetylglucosamine,
pubmed-meshheading:11696361-Amino Acid Sequence,
pubmed-meshheading:11696361-Animals,
pubmed-meshheading:11696361-Arabidopsis,
pubmed-meshheading:11696361-Beta vulgaris,
pubmed-meshheading:11696361-CHO Cells,
pubmed-meshheading:11696361-Carbohydrate Sequence,
pubmed-meshheading:11696361-Cloning, Molecular,
pubmed-meshheading:11696361-Cricetinae,
pubmed-meshheading:11696361-Fucosyltransferases,
pubmed-meshheading:11696361-Magnetic Resonance Spectroscopy,
pubmed-meshheading:11696361-Molecular Sequence Data,
pubmed-meshheading:11696361-Multigene Family,
pubmed-meshheading:11696361-Plant Proteins,
pubmed-meshheading:11696361-Recombinant Proteins,
pubmed-meshheading:11696361-Sequence Homology, Amino Acid,
pubmed-meshheading:11696361-Substrate Specificity
|
pubmed:year |
2001
|
pubmed:articleTitle |
Plant members of the alpha1-->3/4-fucosyltransferase gene family encode an alpha1-->4-fucosyltransferase, potentially involved in Lewis(a) biosynthesis, and two core alpha1-->3-fucosyltransferases.
|
pubmed:affiliation |
Plant Research International, Wageningen University and Research Centre, The Netherlands. bakker.hans@mh-hannover.de
|
pubmed:publicationType |
Journal Article
|