Statements in which the resource exists as a subject.
PredicateObject
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