constitutive levels of the enzyme are produced under all growth conditions. Growth on Lys leads to specific activity levels 2-3fold higher than growth on other amino acids
constitutive levels of the enzyme are produced under all growth conditions. Growth on Lys leads to specific activity levels 2-3fold higher than growth on other amino acids
glutarate semialdehyde dehydrogenase encoded by davD converts glutarate semialdehyde into glutaric acid. In the natural L-lysine catabolic pathway of Pseudomonas strains, glutaric acid is then further converted to acetyl-CoA, a main intermediate of Krebs cycle
glutarate semialdehyde dehydrogenase encoded by davD converts glutarate semialdehyde into glutaric acid. In the natural L-lysine catabolic pathway of Pseudomonas strains, glutaric acid is then further converted to acetyl-CoA, a main intermediate of Krebs cycle
glutarate semialdehyde dehydrogenase encoded by davD converts glutarate semialdehyde into glutaric acid. In the natural L-lysine catabolic pathway of Pseudomonas strains, glutaric acid is then further converted to acetyl-CoA, a main intermediate of Krebs cycle
glutarate semialdehyde dehydrogenase encoded by davD converts glutarate semialdehyde into glutaric acid. In the natural L-lysine catabolic pathway of Pseudomonas strains, glutaric acid is then further converted to acetyl-CoA, a main intermediate of Krebs cycle
metabolic engineering strategies for the production of 5-aminovalerate from L-lysine in vivo synthesized from glucose in Escherichia coli by amplifying metabolic fluxes and activities, e.g. enzyme glutarate semialdehyde dehydrogenase, and by removing repressions and feedback inhibitions involved in L-lysine metabolism, oevrview
metabolic engineering strategies for the production of 5-aminovalerate from L-lysine in vivo synthesized from glucose in Escherichia coli by amplifying metabolic fluxes and activities, e.g. enzyme glutarate semialdehyde dehydrogenase, and by removing repressions and feedback inhibitions involved in L-lysine metabolism, oevrview
metabolic engineering of Corynebacterium glutamicum for the production of glutaric acid, a C5 dicarboxylic acid platform chemical, by co-expression of Pseudomonas putida davT, davB, and davD genes encoding lysine 2-monooxygenase, delta-aminovaleramidase, and glutarate semialdehyde dehydrogenase, respectively, in Corynebacterium glutamicum. The glutaric acid biosynthesis pathway constructed in recombinant Corynebacterium glutamicum is engineered by examining strong synthetic promoters H30 and H36, Corynebacterium glutamicum codon-optimized davTDBA genes, and modification of davB gene with an N-terminal His6-tag to improve the production of glutaric acid. The use of N-terminal His6-tagged DavB is most suitable for the production of glutaric acid from glucose. Fed-batch fermentation on of the final engineered Corynebacterium glutamicum H30_GAHis strain, expressing davTDA genes along with davB fused with His6-tag at N-terminus can produce 24.5 g/l of glutaric acid with low accumulation of L-lysine (1.7 g/l), wherein 5-aminovaleric acid (5-AVA) ccumulation is not observed during fermentation. Metabolically engineered Corynebacterium glutamicum strain H30_GA-2 (engineered strain KCTC 1857) is able for catalysis of the biosynthesis of glutaric acid from glucose. Method optimization and evaluation, overview
metabolic engineering of Corynebacterium glutamicum for the production of glutaric acid, a C5 dicarboxylic acid platform chemical, by co-expression of Pseudomonas putida davT, davB, and davD genes encoding lysine 2-monooxygenase, delta-aminovaleramidase, and glutarate semialdehyde dehydrogenase, respectively, in Corynebacterium glutamicum. The glutaric acid biosynthesis pathway constructed in recombinant Corynebacterium glutamicum is engineered by examining strong synthetic promoters H30 and H36, Corynebacterium glutamicum codon-optimized davTDBA genes, and modification of davB gene with an N-terminal His6-tag to improve the production of glutaric acid. The use of N-terminal His6-tagged DavB is most suitable for the production of glutaric acid from glucose. Fed-batch fermentation on of the final engineered Corynebacterium glutamicum H30_GAHis strain, expressing davTDA genes along with davB fused with His6-tag at N-terminus can produce 24.5 g/l of glutaric acid with low accumulation of L-lysine (1.7 g/l), wherein 5-aminovaleric acid (5-AVA) ccumulation is not observed during fermentation. Metabolically engineered Corynebacterium glutamicum strain H30_GA-2 (engineered strain KCTC 1857) is able for catalysis of the biosynthesis of glutaric acid from glucose. Method optimization and evaluation, overview
metabolic engineering strategies for the production of 5-aminovalerate from L-lysine in vivo synthesized from glucose in Escherichia coli by amplifying metabolic fluxes and activities, e.g. enzyme glutarate semialdehyde dehydrogenase, and by removing repressions and feedback inhibitions involved in L-lysine metabolism, oevrview
metabolic engineering of Corynebacterium glutamicum for the production of glutaric acid, a C5 dicarboxylic acid platform chemical, by co-expression of Pseudomonas putida davT, davB, and davD genes encoding lysine 2-monooxygenase, delta-aminovaleramidase, and glutarate semialdehyde dehydrogenase, respectively, in Corynebacterium glutamicum. The glutaric acid biosynthesis pathway constructed in recombinant Corynebacterium glutamicum is engineered by examining strong synthetic promoters H30 and H36, Corynebacterium glutamicum codon-optimized davTDBA genes, and modification of davB gene with an N-terminal His6-tag to improve the production of glutaric acid. The use of N-terminal His6-tagged DavB is most suitable for the production of glutaric acid from glucose. Fed-batch fermentation on of the final engineered Corynebacterium glutamicum H30_GAHis strain, expressing davTDA genes along with davB fused with His6-tag at N-terminus can produce 24.5 g/l of glutaric acid with low accumulation of L-lysine (1.7 g/l), wherein 5-aminovaleric acid (5-AVA) ccumulation is not observed during fermentation. Metabolically engineered Corynebacterium glutamicum strain H30_GA-2 (engineered strain KCTC 1857) is able for catalysis of the biosynthesis of glutaric acid from glucose. Method optimization and evaluation, overview
metabolic engineering of Corynebacterium glutamicum for the production of glutaric acid, a C5 dicarboxylic acid platform chemical, by co-expression of Pseudomonas putida davT, davB, and davD genes encoding lysine 2-monooxygenase, delta-aminovaleramidase, and glutarate semialdehyde dehydrogenase, respectively, in Corynebacterium glutamicum. The glutaric acid biosynthesis pathway constructed in recombinant Corynebacterium glutamicum is engineered by examining strong synthetic promoters H30 and H36, Corynebacterium glutamicum codon-optimized davTDBA genes, and modification of davB gene with an N-terminal His6-tag to improve the production of glutaric acid. The use of N-terminal His6-tagged DavB is most suitable for the production of glutaric acid from glucose. Fed-batch fermentation on of the final engineered Corynebacterium glutamicum H30_GAHis strain, expressing davTDA genes along with davB fused with His6-tag at N-terminus can produce 24.5 g/l of glutaric acid with low accumulation of L-lysine (1.7 g/l), wherein 5-aminovaleric acid (5-AVA) ccumulation is not observed during fermentation. Metabolically engineered Corynebacterium glutamicum strain H30_GA-2 (engineered strain KCTC 1857) is able for catalysis of the biosynthesis of glutaric acid from glucose. Method optimization and evaluation, overview
metabolic engineering of Corynebacterium glutamicum for the production of glutaric acid, a C5 dicarboxylic acid platform chemical, by co-expression of Pseudomonas putida davT, davB, and davD genes encoding lysine 2-monooxygenase, delta-aminovaleramidase, and glutarate semialdehyde dehydrogenase, respectively, in Corynebacterium glutamicum. The glutaric acid biosynthesis pathway constructed in recombinant Corynebacterium glutamicum is engineered by examining strong synthetic promoters H30 and H36, Corynebacterium glutamicum codon-optimized davTDBA genes, and modification of davB gene with an N-terminal His6-tag to improve the production of glutaric acid. The use of N-terminal His6-tagged DavB is most suitable for the production of glutaric acid from glucose. Fed-batch fermentation on of the final engineered Corynebacterium glutamicum H30_GAHis strain, expressing davTDA genes along with davB fused with His6-tag at N-terminus can produce 24.5 g/l of glutaric acid with low accumulation of L-lysine (1.7 g/l), wherein 5-aminovaleric acid (5-AVA) ccumulation is not observed during fermentation. Metabolically engineered Corynebacterium glutamicum strain H30_GA-2 (engineered strain KCTC 1857) is able for catalysis of the biosynthesis of glutaric acid from glucose. Method optimization and evaluation, overview
gene davD, recombinant expression in Escherichia coli strain W3110, coexpression with Pseudomonas putida gene gabT, encoding 5-aminovalerate aminotransferase, and davA and davB genes encoding delta-aminovaleramidase and lysine 2-monooxygenase, respectively. The recombinant Escherichia coli WL3110 strain expressingthe davAB and gabTD genes is cultured in a medium containing D-glucose, L-lysine, and 2-oxoglutarate, and produces glutarate
Factors influencing growth on L-lysine by Pseudomonas. Regulation of terminal enzymes in the delta-aminovalerate pathway and growth stimulation by alpha ketoglutarate