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Glycobiology, 2000, Vol. 10, No. 10 1041-1047
© 2000 Oxford University Press

Functional expression of Escherichia coli enzymes synthesizing GDP-L-fucose from inherent GDP-D-mannose in Saccharomyces cerevisiae

Pirkko Mattila1,2, Jarkko Räbinä2, Solveig Hortling2, Jari Helin3 and Risto Renkonen2,4

2Department of Bacteriology and Immunology, Haartman Institute, University of Helsinki, 3Institute of Biotechnology, University of Helsinki, and 4Helsinki University Central Hospital, Laboratory Diagnostics, Helsinki, Finland

Fucosylation of glycans on glycoproteins and -lipids requires the enzymatic activity of relevant fucosyltransferases and GDP-L-fucose as the donor. Due to the biological importance of fucosylated glycans, a readily accessible source of GDP-L-fucose would be required. Here we describe the construction of a stable recombinant S.cerevisiae strain expressing the E.coli genes gmd and wcaG encoding the two enzymes, GDP-mannose-4,6-dehydratase (GMD) and GDP-4-keto-6-deoxy-D-mannose-3,5-epimerase/4-reductase (GMER(FX)) respectively, needed to convert GDP-mannose to GDP-fucose via the de novo pathway. Taking advantage of the rich inherent cytosolic GDP-mannose pool in S.cerevisiae cells we could easily produce 0.2 mg/l of GDP-L-fucose with this recombinant yeast strain without addition of any external GDP-mannose. The GDP-L-fucose product could be used as the fucose donor for {alpha}1,3fucosyltransferase to synthesize sialyl Lewis x (sLex), a glycan crucial for the selectin-dependent leukocyte traffic.

1 To whom correspondence should be addressed at: Department of Bacteriology and Immunology, P.O. Box 21 (Haartmaninkatu 3), FIN-00014 University of Helsinki, Finland


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