the oxygen sensitivity of CoA-acylating aldehyde dehydrogenase appears to be a key limiting factor for cyanobacteria to produce alcohols through the CoA-dependent route
the oxygen sensitivity of CoA-acylating aldehyde dehydrogenase appears to be a key limiting factor for cyanobacteria to produce alcohols through the CoA-dependent route
the oxygen sensitivity of CoA-acylating aldehyde dehydrogenase appears to be a key limiting factor for cyanobacteria to produce alcohols through the CoA-dependent route
the oxygen sensitivity of CoA-acylating aldehyde dehydrogenase appears to be a key limiting factor for cyanobacteria to produce alcohols through the CoA-dependent route
to fit enzyme Bld into the non-natural 1,4-butanediol pathway, it is engineered through random mutagenesis, library construction. Five Bld mutants are isolated using a colorimetric Schiff's reagent-based method. Subsequent site-directed mutagenesis of Bld generates the two best Bld mutants, L273I and L273T, which produce 1,4-butanediol titers fourfold greater than those of wild-type Bld. Butyraldehyde dehydrogenase (Bld) and butanol dehydrogenase (Bdh) of Clostridium saccharoperbutylacetonicum are selected as a substitute for the bifunctional AdhE2 in the reconstructed 1,4-butanediol biosynthesis pathway in Escherichia coli, coexpression of diverse involved genes in Escherichia coli
to fit enzyme Bld into the non-natural 1,4-butanediol pathway, it is engineered through random mutagenesis, library construction. Five Bld mutants are isolated using a colorimetric Schiff's reagent-based method. Subsequent site-directed mutagenesis of Bld generates the two best Bld mutants, L273I and L273T, which produce 1,4-butanediol titers fourfold greater than those of wild-type Bld. Butyraldehyde dehydrogenase (Bld) and butanol dehydrogenase (Bdh) of Clostridium saccharoperbutylacetonicum are selected as a substitute for the bifunctional AdhE2 in the reconstructed 1,4-butanediol biosynthesis pathway in Escherichia coli, coexpression of diverse involved genes in Escherichia coli
design of a coenzyme A (CoA) dependent n-butanol biosynthesis pathway tailored to the metabolic physiology of the cyanobacterium Synechococcus elongatus PCC 7942 by incorporating an ATP driving force and a kinetically irreversible trap. Oxygen-sensitive CoA-acylating butyraldehyde dehydrogenase (Bldh) is exchanged for the oxygen-tolerant PduP from Salmonella enterica. Replacing Bldh with PduP in the n-butanol synthesis pathway results in n-butanol production to a cumulative titer of 404 mg/l with peak productivity of 51 mg/l per day, exceeding the base strain by 20fold. Anaerobic growth rescue of Escherichia coli strain JCL166 by overexpression of the Clostridium butanol pathway with different aldehyde dehydrogenases PduP
design of a coenzyme A (CoA) dependent n-butanol biosynthesis pathway tailored to the metabolic physiology of the cyanobacterium Synechococcus elongatus PCC 7942 by incorporating an ATP driving force and a kinetically irreversible trap. Oxygen-sensitive CoA-acylating butyraldehyde dehydrogenase (Bldh) is exchanged for the oxygen-tolerant PduP from Salmonella enterica. Replacing Bldh with PduP in the n-butanol synthesis pathway results in n-butanol production to a cumulative titer of 404 mg/l with peak productivity of 51 mg/l per day, exceeding the base strain by 20fold. Anaerobic growth rescue of Escherichia coli strain JCL166 by overexpression of the Clostridium butanol pathway with different aldehyde dehydrogenases PduP
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene bcd, the genes (crt, bcd, etfB, etfA, hbd, and thl) responsible for butyryl-CoA formation occur as a multi-gene operon, plasmid construction map for expressing individual genes of the n-butanol pathway, plasmids pHBD,pCRT,pBCD-etfAB, and pADHE, overview
gene bld, butyraldehyde dehydrogenase gene of Clostridium saccharoperbutylacetonicum is coexpresses with diverse involved genes in Escherichia coli for the reconstruction of 1,4-butanediol biosynthesis pathway in Escherichia coli, recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
gene bldh, recombinant expression in Escherichia coli strain JCL166, strain JCL166 cannot grow anaerobically unless complemented by an exogenous fermentation pathway such as n-butanol biosynthesis
gene bldh, recombinant expression in Escherichia coli strain JCL166, strain JCL166 cannot grow anaerobically unless complemented by an exogenous fermentation pathway such as n-butanol biosynthesis. Recombinant coexpression of PduP with the enzymes of the n-butanol synthesis pathway in Synechococcus elongatus strain PCC 7942 results in autotrophic n-butanol production
gene pduP, recombinant expression in Escherichia coli strain JCL166, strain JCL166 cannot grow anaerobically unless complemented by an exogenous fermentation pathway such as n-butanol biosynthesis. Recombinant coexpression of PduP with the enzymes of the n-butanol synthesis pathway in Synechococcus elongatus strain PCC 7942 results in autotrophic n-butanol production. PduP from Lactobacillus brevis produces more n-butanol than ethanol