Identification of human L-fucose kinase amino acid sequence |
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Authors: | Hinderlich Stephan Berger Markus Blume Astrid Chen Hao Ghaderi Darius Bauer Christian |
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Affiliation: | Institut für Molekularbiologie und Biochemie, Freie Universit?t Berlin, Arnimallee 22, 14195 Berlin-Dahlem, Germany. hinderli@zedat.fu-berlin.de |
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Abstract: | 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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Keywords: | Fucose smallcaps" >l-Fucose kinase Amino acid sequence Sugar kinase |
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