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Predicate | Object |
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rdf:type | |
lifeskim:mentions |
umls-concept:C0037791,
umls-concept:C0038164,
umls-concept:C0086418,
umls-concept:C0205147,
umls-concept:C0242767,
umls-concept:C0441655,
umls-concept:C0559956,
umls-concept:C0765250,
umls-concept:C1097129,
umls-concept:C1186763,
umls-concept:C1274040,
umls-concept:C1444754,
umls-concept:C1519623,
umls-concept:C2003941,
umls-concept:C2827421
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pubmed:issue |
15
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pubmed:dateCreated |
1995-5-19
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pubmed:abstractText |
The acceptor specificity of recombinant full-length, membrane-bound fucosyltransferases, expressed in COS-7 cells, and soluble, protein-A chimeric forms of alpha 1,3-fucosyltransferase (Fuc-T) III, Fuc-TIV, and Fuc-TV was analyzed toward a broad panel of oligosaccharide, glycolipid, and glycoprotein substrates. Our results on the full-length enzymes confirm and extend previous studies. However, chimeric Fuc-Ts showed increased activity toward glycoproteins, whereas chimeric Fuc-TIII and Fuc-TV had a decreased activity with glycosphingolipids, compared to the full-length enzymes. Unexpectedly, chimeric Fuc-TV exhibited a GDP-fucose hydrolyzing activity. In substrates with multiple acceptor sites, the preferred site of fucosylation was identified. Fuc-TIII and Fuc-TV catalyzed fucose transfer exclusively to OH-3 of glucose in lacto-N-neotetraose and lacto-N-tetraose, respectively, as was demonstrated by 1H NMR spectroscopy. Thin layer chromatography immunostaining revealed that FucT-IV preferred the distal GlcNAc residue in nLc6Cer, whereas Fuc-TV preferred the proximal Gl-cNAc residue. Incubation of Fuc-TIV or Fuc-TV with VI3NeuAcnLc6Cer resulted in products with the sialyl-LewisX epitope as well as the VIM-2 structure. To identify polar groups on acceptors that function in enzyme binding, deoxygenated substrate analogs were tested as acceptors. All three Fuc-Ts had an absolute requirement for a hydroxyl at C-6 of galactose in addition to the accepting hydroxyl at C-3 or C-4 of GlcNAc.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/3-galactosyl-N-acetylglucosaminide...,
http://linkedlifedata.com/resource/pubmed/chemical/Ethylmaleimide,
http://linkedlifedata.com/resource/pubmed/chemical/Fucosyltransferases,
http://linkedlifedata.com/resource/pubmed/chemical/Guanosine Diphosphate Fucose,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Staphylococcal Protein A
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
14
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pubmed:volume |
270
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
8712-22
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pubmed:dateRevised |
2008-8-15
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pubmed:meshHeading |
pubmed-meshheading:7721776-Animals,
pubmed-meshheading:7721776-Carbohydrate Sequence,
pubmed-meshheading:7721776-Cell Line,
pubmed-meshheading:7721776-Cell Membrane,
pubmed-meshheading:7721776-Ethylmaleimide,
pubmed-meshheading:7721776-Fucosyltransferases,
pubmed-meshheading:7721776-Guanosine Diphosphate Fucose,
pubmed-meshheading:7721776-Humans,
pubmed-meshheading:7721776-Hydrolysis,
pubmed-meshheading:7721776-Kinetics,
pubmed-meshheading:7721776-Magnetic Resonance Spectroscopy,
pubmed-meshheading:7721776-Molecular Sequence Data,
pubmed-meshheading:7721776-Recombinant Proteins,
pubmed-meshheading:7721776-Staphylococcal Protein A,
pubmed-meshheading:7721776-Substrate Specificity
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pubmed:year |
1995
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pubmed:articleTitle |
Acceptor specificity of different length constructs of human recombinant alpha 1,3/4-fucosyltransferases. Replacement of the stem region and the transmembrane domain of fucosyltransferase V by protein A results in an enzyme with GDP-fucose hydrolyzing activity.
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pubmed:affiliation |
Department of Chemistry and Biochemistry, San Francisco State University, California 94132, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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