Production of GDP-L-fucose, L-fucose donor for fucosyloligosaccharide synthesis, in recombinant Escherichia coli. 2007

Seong-Goo Byun, and Myoung-Dong Kim, and Won-Heong Lee, and Kun-Jae Lee, and Nam Soo Han, and Jin-Ho Seo
Department of Agricultural Biotechnology and Center for Agricultural Biomaterials, Seoul National University, Seoul, South Korea.

A recombinant Escherichia coli strain was developed to produce guanosine 5'-diphosphate (GDP)-L-fucose, donor of L-fucose, which is an essential substrate for the synthesis of fucosyloligosaccharides. GDP-D: -mannose-4, 6-dehydratase (GMD) and GDP-4-keto-6-deoxymannose 3, 5-epimerase 4-reductase (WcaG), the two crucial enzymes for the de novo GDP-L-fucose biosynthesis, were overexpressed in recombinant E. coli by constructing inducible overexpression vectors. Optimum expression conditions for GMD and WcaG in recombinant E. coli BL21(DE3) were 25 degrees C and 0.1 mM isopropyl-beta-D-thioglucopyranoside. Maximum GDP-L-fucose concentration of 38.9 +/- 0.6 mg l(-1) was obtained in a glucose-limited fed-batch cultivation, and it was enhanced further by co-expression of NADPH-regenerating glucose-6-phosphate dehydrogenase encoded by the zwf gene to achieve 55.2 +/- 0.5 mg l(-1) GDP-L-fucose under the same cultivation condition.

UI MeSH Term Description Entries
D007218 Industrial Microbiology The study, utilization, and manipulation of those microorganisms capable of economically producing desirable substances or changes in substances, and the control of undesirable microorganisms. Microbiology, Industrial
D007658 Ketone Oxidoreductases Oxidoreductases that are specific for KETONES. Oxidoreductases, Ketone
D009097 Multienzyme Complexes Systems of enzymes which function sequentially by catalyzing consecutive reactions linked by common metabolic intermediates. They may involve simply a transfer of water molecules or hydrogen atoms and may be associated with large supramolecular structures such as MITOCHONDRIA or RIBOSOMES. Complexes, Multienzyme
D002238 Carbohydrate Epimerases Enzymes that catalyze the epimerization of chiral centers within carbohydrates or their derivatives. EC 5.1.3. Carbohydrate Isomerases,Epimerases, Carbohydrate,Isomerases, Carbohydrate
D004926 Escherichia coli A species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc. Alkalescens-Dispar Group,Bacillus coli,Bacterium coli,Bacterium coli commune,Diffusely Adherent Escherichia coli,E coli,EAggEC,Enteroaggregative Escherichia coli,Enterococcus coli,Diffusely Adherent E. coli,Enteroaggregative E. coli,Enteroinvasive E. coli,Enteroinvasive Escherichia coli
D005954 Glucosephosphate Dehydrogenase Glucose-6-Phosphate Dehydrogenase,Dehydrogenase, Glucose-6-Phosphate,Dehydrogenase, Glucosephosphate,Glucose 6 Phosphate Dehydrogenase
D006154 Guanosine Diphosphate Fucose A nucleoside diphosphate sugar formed from GDPmannose, which provides fucose for lipopolysaccharides of bacterial cell walls, and for blood group substances and other glycoproteins. GDP Fucose,Guanosine Diphosphofucose,Diphosphate Fucose, Guanosine,Diphosphofucose, Guanosine,Fucose, GDP,Fucose, Guanosine Diphosphate
D006836 Hydro-Lyases Enzymes that catalyze the breakage of a carbon-oxygen bond leading to unsaturated products via the removal of water. EC 4.2.1. Dehydratase,Dehydratases,Hydrase,Hydrases,Hydro Lyase,Hydro-Lyase,Hydro Lyases,Lyase, Hydro,Lyases, Hydro
D015870 Gene Expression The phenotypic manifestation of a gene or genes by the processes of GENETIC TRANSCRIPTION and GENETIC TRANSLATION. Expression, Gene,Expressions, Gene,Gene Expressions
D029968 Escherichia coli Proteins Proteins obtained from ESCHERICHIA COLI. E coli Proteins

Related Publications

Seong-Goo Byun, and Myoung-Dong Kim, and Won-Heong Lee, and Kun-Jae Lee, and Nam Soo Han, and Jin-Ho Seo
August 2011, Applied microbiology and biotechnology,
Seong-Goo Byun, and Myoung-Dong Kim, and Won-Heong Lee, and Kun-Jae Lee, and Nam Soo Han, and Jin-Ho Seo
March 2012, Applied microbiology and biotechnology,
Seong-Goo Byun, and Myoung-Dong Kim, and Won-Heong Lee, and Kun-Jae Lee, and Nam Soo Han, and Jin-Ho Seo
February 2015, Enzyme and microbial technology,
Seong-Goo Byun, and Myoung-Dong Kim, and Won-Heong Lee, and Kun-Jae Lee, and Nam Soo Han, and Jin-Ho Seo
February 2017, Biotechnology letters,
Seong-Goo Byun, and Myoung-Dong Kim, and Won-Heong Lee, and Kun-Jae Lee, and Nam Soo Han, and Jin-Ho Seo
April 2019, Biotechnology and bioengineering,
Seong-Goo Byun, and Myoung-Dong Kim, and Won-Heong Lee, and Kun-Jae Lee, and Nam Soo Han, and Jin-Ho Seo
May 2020, Journal of agricultural and food chemistry,
Seong-Goo Byun, and Myoung-Dong Kim, and Won-Heong Lee, and Kun-Jae Lee, and Nam Soo Han, and Jin-Ho Seo
September 2000, Glycobiology,
Seong-Goo Byun, and Myoung-Dong Kim, and Won-Heong Lee, and Kun-Jae Lee, and Nam Soo Han, and Jin-Ho Seo
October 2000, Glycobiology,
Seong-Goo Byun, and Myoung-Dong Kim, and Won-Heong Lee, and Kun-Jae Lee, and Nam Soo Han, and Jin-Ho Seo
January 2012, Enzyme and microbial technology,
Seong-Goo Byun, and Myoung-Dong Kim, and Won-Heong Lee, and Kun-Jae Lee, and Nam Soo Han, and Jin-Ho Seo
June 2011, Biotechnology letters,
Copied contents to your clipboard!