1.2.1.57: butanal dehydrogenase
This is an abbreviated version!
For detailed information about butanal dehydrogenase, go to the full flat file.
Word Map on EC 1.2.1.57
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1.2.1.57
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butanol
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acetobutylicum
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butyryl-coa
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butyrate
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acetyl-coa
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acetaldehyde
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crotonase
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coa-dependent
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a-transferase
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nad-dependent
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thiolase
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beijerinckii
- 1.2.1.57
- butanol
- acetobutylicum
- butyryl-coa
- butyrate
- acetyl-coa
- acetaldehyde
- crotonase
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coa-dependent
- a-transferase
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nad-dependent
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thiolase
- beijerinckii
Reaction
Synonyms
BCD, Bld, Bldh, Butyraldehyde dehydrogenase, butyryl CoA dehydrogenase, CoA-acylating aldehyde dehydrogenase, CoA-acylating butyraldehyde dehydrogenase, coenzyme A-acylating aldehyde dehydrogenase, PduP, Tthe_1660
ECTree
1.2.1.57 butanal dehydrogenaseAdvanced search results
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results (Engineering
Engineering on EC 1.2.1.57 - butanal dehydrogenase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
A176T
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random mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
A467S
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random mutagenesis, the mutant shows similar activity compared to the wild-type enzyme
K279R
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random mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
L273C
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site-directed mutagenesis, the mutant shows about 2fold increased activity compared to the wild-type enzyme
L273I
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random mutagenesis, the mutant shows about 3.5fold increased activity compared to the wild-type enzyme
L273M
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site-directed mutagenesis, the mutant shows about 2fold increased activity compared to the wild-type enzyme
L273S
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site-directed mutagenesis, the mutant shows slightly increased activity compared to the wild-type enzyme
L273T
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site-directed mutagenesis, the mutant shows about 4fold increased activity compared to the wild-type enzyme
L273V
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site-directed mutagenesis, the mutant shows slightly increased activity compared to the wild-type enzyme
M371R
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random mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
N409T
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random mutagenesis, the mutant shows similar activity compared to the wild-type enzyme
L273C
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site-directed mutagenesis, the mutant shows about 2fold increased activity compared to the wild-type enzyme
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L273I
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random mutagenesis, the mutant shows about 3.5fold increased activity compared to the wild-type enzyme
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L273M
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site-directed mutagenesis, the mutant shows about 2fold increased activity compared to the wild-type enzyme
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L273T
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site-directed mutagenesis, the mutant shows about 4fold increased activity compared to the wild-type enzyme
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additional information
additional information
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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
additional information
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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
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additional information
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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
additional information
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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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additional information
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recombinant expression of the enzyme from Clostridium acetobutylicum strain ATCC 824 in Thermoanaerobacterium saccharolyticum strain DSM 8691
additional information
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recombinant expression of the enzyme from Clostridium acetobutylicum strain ATCC 824 in Thermoanaerobacterium saccharolyticum strain DSM 8691
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