Literature summary for 4.2.1.47 extracted from

Byun, S.G.; Kim, M.D.; Lee, W.H.; Lee, K.J.; Han, N.S.; Seo, J.H.
Production of GDP-L-fucose, L-fucose donor for fucosyloligosaccharide synthesis, in recombinant Escherichia coli (2007), Appl. Microbiol. Biotechnol., 74, 768-775.

Cloned(Commentary)

Cloned (Comment)	Organism
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

Cloned (Comment)

Organism

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

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-

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Release 2023.1 (January 2023)