Linked Life Data

14686921

Source:http://linkedlifedata.com/resource/pubmed/id/14686921

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2003-12-22
pubmed:databankReference
pubmed:abstractText
In the salvage pathway of GDP-L-fucose, free cytosolic fucose is phosphorylated by L-fucokinase to form L-fucose-L-phosphate, which is then further converted to GDP-L-fucose in the reaction catalyzed by GDP-L-fucose pyrophosphorylase. We report here the cloning and expression of murine L-fucokinase and GDP-L-fucose pyrophosphorylase. Murine L-fucokinase is expressed as two transcripts of 3057 and 3270 base pairs, encoding proteins of 1019 and 1090 amino acids with predicted molecular masses of 111 kDa and 120 kDa respectively. Only the longer splice variant of L-fucokinase was enzymatically active when expressed in COS-7 cells. Murine GDP-L-fucose pyrophosphorylase has an open reading frame of 1773 base pairs encoding a protein of 591 amino acids with a predicted molecular mass of 65.5 kDa. GDP-L-fucose, the reaction product of GDP-L-pyrophosphorylase, was identified by HPLC and MALDI-TOF MS analysis. The tissue distribution of murine L-fucokinase and GDP-L-fucose pyrophosphorylase was investigated by quantitative real time PCR, which revealed high expression of L-fucokinase and GDP-L-fucose pyrophosphorylase in various tissues. The wide expression of both enzymes can also be observed from the large amount of data collected from a number of expressed sequence tag libraries, which indicate that not only the de novo pathway alone, but also the salvage pathway, could have a significant role in the synthesis of GDP-L-fucose in the cytosol.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0014-2956
pubmed:author
pubmed:issnType
Print
pubmed:volume
271
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
78-86
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed-meshheading:14686921-Alternative Splicing, pubmed-meshheading:14686921-Amino Acid Sequence, pubmed-meshheading:14686921-Animals, pubmed-meshheading:14686921-Base Sequence, pubmed-meshheading:14686921-COS Cells, pubmed-meshheading:14686921-Cercopithecus aethiops, pubmed-meshheading:14686921-Cloning, Molecular, pubmed-meshheading:14686921-DNA, Complementary, pubmed-meshheading:14686921-DNA Primers, pubmed-meshheading:14686921-Expressed Sequence Tags, pubmed-meshheading:14686921-Genetic Variation, pubmed-meshheading:14686921-Mice, pubmed-meshheading:14686921-Molecular Sequence Data, pubmed-meshheading:14686921-Nucleotidyltransferases, pubmed-meshheading:14686921-Phosphotransferases (Alcohol Group Acceptor), pubmed-meshheading:14686921-Polymerase Chain Reaction, pubmed-meshheading:14686921-Recombinant Proteins, pubmed-meshheading:14686921-Transfection
pubmed:year
2004
pubmed:articleTitle
Cloning and expression of murine enzymes involved in the salvage pathway of GDP-L-fucose.
pubmed:affiliation
Department of Bacteriology and Immunology, Haartman Institute and Biomedicum, University of Helsinki, Finland.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't