Source:http://linkedlifedata.com/resource/pubmed/id/12056818
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
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pubmed:dateCreated |
2002-6-11
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pubmed:databankReference | |
pubmed:abstractText |
Fucose is a major component of complex carbohydrates. L-Fucose kinase (fucokinase) takes part in the salvage pathway for reutilization of fucose from the degradation of oligosaccharides. The amino acid sequence of human fucokinase was derived from a cDNA encoding a protein of hitherto unidentified function. Human fucokinase polypeptide chain consists of 990 amino acids with a predicted molecular mass of 107 kDa. The C-terminal part of its amino acid sequence showed sequence motifs typical for sugar kinases. Fucokinase full-length protein and a deletion mutant lacking the first 363 amino acids of the N-terminus were expressed in Escherichia coli BL21 cells. Both proteins displayed fucokinase activity. These results reveal that the discovered cDNA encodes the fucokinase protein and they confirm that a functional kinase domain is located in the C-terminal part of the enzyme.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0006-291X
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
14
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pubmed:volume |
294
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
650-4
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:12056818-Adenosine Triphosphate,
pubmed-meshheading:12056818-Amino Acid Sequence,
pubmed-meshheading:12056818-Base Sequence,
pubmed-meshheading:12056818-Binding Sites,
pubmed-meshheading:12056818-Cloning, Molecular,
pubmed-meshheading:12056818-Humans,
pubmed-meshheading:12056818-Molecular Sequence Data,
pubmed-meshheading:12056818-Peptide Mapping,
pubmed-meshheading:12056818-Phosphotransferases (Alcohol Group Acceptor),
pubmed-meshheading:12056818-Sequence Analysis, Protein
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pubmed:year |
2002
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pubmed:articleTitle |
Identification of human L-fucose kinase amino acid sequence.
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pubmed:affiliation |
Institut für Molekularbiologie und Biochemie, Freie Universität Berlin, Arnimallee 22, 14195 Berlin-Dahlem, Germany. hinderli@zedat.fu-berlin.de
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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