Cloned (Comment) | Organism |
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GDP-D-mannose-4,6-dehydratase and GDP-4-keto-6-deoxymannose 3, 5-epimerase 4-reductase, the two crucial enzymes for the de novo GDP-L-fucose biosynthesis, are overexpressed in recombinant Escherichia coli by constructing inducible overexpression vectors. Optimum expression conditions in recombinant Escherichia coli BL21(DE3) are 25°C and 0.1 mM isopropyl-beta-D-thioglucopyranoside. Maximum GDP-L-fucose concentration of 38.9 mg/l is obtained in a glucose-limited fed-batch cultivation, and it is enhanced further by coexpression of NADPH-regenerating glucose-6-phosphate dehydrogenase encoded by the zwf gene to achieve 55.2 mg/l GDP-L-fucose under the same cultivation condition | Escherichia coli |
Organism | UniProt | Comment | Textmining |
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Escherichia coli | - |
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