Source:http://linkedlifedata.com/resource/pubmed/id/15519322
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
16
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pubmed:dateCreated |
2004-11-2
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pubmed:abstractText |
New unnatural sugar nucleotides, UDP-Fuc and CDP-Fuc were synthesized from fucose-beta-1-phosphate and nucleotide monophosphates activated as morpholidates. Furthermore, a nucleotide analogue was prepared by phosphorylation of 1-(beta-D-ribofuranosyl)cyanuric acid, itself obtained as a protected derivative by condensation of the persilylated derivative of cyanuric acid with 1-O-acetyl-2,3,5-tri-O-benzoyl-beta-D-ribofuranose in 74% yield. This phosphate activated according to the same procedure was condensed with fucose-beta-1-phosphate, affording a new sugar nucleotide conjugate (NDP-Fuc) which was evaluated together with UDP-Fuc, CDP-Fuc and ADP-Fuc, as fucose donors in alpha-(1-->4/3)-fucosyltransferase (FucT-III) catalyzed reaction. Fucose transfer could be observed with each of the donors and kinetic parameters were determined using a fluorescent acceptor substrate. Efficiency of the four analogues towards FucT-III was in the following order: UDP-Fuc=ADP-Fuc>NDP-Fuc>CDP-Fuc. According to the same strategy ADP-GlcNAc was prepared from AMP-morpholidate and N-acetylglucosamine-alpha-1-phosphate; tested as a glucosaminyl donor towards Neisseria meningitidis N-acetylglucosaminyl transferase (LgtA), ADP-GlcNAc was recognized with 0.1% efficiency as compared with UDP-GlcNAc, the natural donor substrate.
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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/Adenosine Diphosphate Sugars,
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Fucosyltransferases,
http://linkedlifedata.com/resource/pubmed/chemical/Glycosyltransferases,
http://linkedlifedata.com/resource/pubmed/chemical/LgtA protein, bacteria,
http://linkedlifedata.com/resource/pubmed/chemical/N-Acetylglucosaminyltransferases,
http://linkedlifedata.com/resource/pubmed/chemical/Nucleoside Diphosphate Sugars,
http://linkedlifedata.com/resource/pubmed/chemical/Uridine Diphosphate Sugars
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0008-6215
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
339
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2641-9
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pubmed:dateRevised |
2008-8-15
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pubmed:meshHeading |
pubmed-meshheading:15519322-Adenosine Diphosphate Sugars,
pubmed-meshheading:15519322-Bacterial Proteins,
pubmed-meshheading:15519322-Catalysis,
pubmed-meshheading:15519322-Fucosyltransferases,
pubmed-meshheading:15519322-Glycosyltransferases,
pubmed-meshheading:15519322-Kinetics,
pubmed-meshheading:15519322-N-Acetylglucosaminyltransferases,
pubmed-meshheading:15519322-Nucleoside Diphosphate Sugars,
pubmed-meshheading:15519322-Structure-Activity Relationship,
pubmed-meshheading:15519322-Substrate Specificity,
pubmed-meshheading:15519322-Uridine Diphosphate Sugars
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pubmed:year |
2004
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pubmed:articleTitle |
Synthesis of unnatural sugar nucleotides and their evaluation as donor substrates in glycosyltransferase-catalyzed reactions.
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pubmed:affiliation |
Laboratoire de Chimie Organique Multifonctionnelle, UMR 8614, GDR 2590, Institut de Chimie Moléculaire et des Matériaux d'Orsay (ICMMO), Université Paris-Sud, Bât 420, F-91405 Orsay, France.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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