1.2.1.10: acetaldehyde dehydrogenase (acetylating)
This is an abbreviated version!
For detailed information about acetaldehyde dehydrogenase (acetylating), go to the full flat file.
Word Map on EC 1.2.1.10
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1.2.1.10
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synthesis
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propionaldehyde
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nad-dependent
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meta-cleavage
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biofuel production
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transthioesterification
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histolytica
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benzaldehyde
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pre-steady-state
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ammonia-lyase
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propionyl-coa
- 1.2.1.10
- synthesis
- propionaldehyde
-
nad-dependent
-
meta-cleavage
- biofuel production
-
transthioesterification
- histolytica
- benzaldehyde
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pre-steady-state
-
ammonia-lyase
- propionyl-coa
Reaction
Synonyms
4-hydroxy-2-ketovalerate aldolase/acylating acetaldehyde dehydrogenase, ACDH, acetaldehyde dehydrogenase, Acetaldehyde dehydrogenase [acetylating], acetaldehyde-alcohol dehydrogenase, acetyl-CoA reductase, acylating acetaldehyde dehydrogenase, AdhE, ADHES77, aldehyde dehydrogenase, aldehyde dehydrogenase (acylating), aldehyde/alcohol dehydrogenase, ALDH, BAD, bi-functional alcohol/aldehyde dehydrogenase, bifunctional acetaldehyde-alcohol dehydrogenase, BphJ, CoA-acylating aldehyde dehydrogenase, CoA-dependent aldehyde dehydrogenase, coenzyme A linked aldehyde dehydrogenase, coenzyme A-acylating aldehyde dehydrogenase, DmpF, DmpFG, MhpF, More, NAD+/CoA-dependent aldehyde dehydrogenase, nonphosphorylating acylating aldehyde dehydrogenase, PduP, Teth514_0627, Teth514_1942, Tsac_0416, TTHB247
ECTree
1.2.1.10 acetaldehyde dehydrogenase (acetylating)Advanced search results
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Engineering on EC 1.2.1.10 - acetaldehyde dehydrogenase (acetylating)
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
D208A
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
I171A
level of activation of BphI by the mutant enzyme are reduced by more than 3fold in the presence of NADH and more than 4.5fold when the enzyme is undergoing turnover. The mutation results in a 35% reduction in acetaldehyde channeling efficiency
I171F
the mutant shows strongly reduced catalytic efficiency compared to the wild type enzyme
I195A
the variant has a 20fold higher catalytic efficiency for butyraldehyde and pentaldehyde compared to the catalytic efficiency of the wild type toward its natural substrate acetaldehyde. The mutation results in a 35% reduction in acetaldehyde channeling efficiency
I195F
the mutant shows severely reduced catalytic efficiency compared to the wild type enzyme
I195W
the mutant shows strongly reduced catalytic efficiency compared to the wild type enzyme
N170A
the mutation does not substantially alter aldehyde channeling efficiencies. The level of activation of BphI by the mutant enzyme are reduced by more than 3fold in the presence of NADH and more than 4.5fold when the enzyme is undergoing turnover
N170D
level of activation of BphI by the mutant enzyme are reduced by more than 3fold in the presence of NADH and more than 4.5fold when the enzyme is undergoing turnover
I159A
additional information
I159A
site-directed mutagenesis, the barrier into the dehydrogenase active site region has been virtually eliminated such that acetaldehyde is transported from one active site to the other in a downhill process
I159A
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site-directed mutagenesis, the barrier into the dehydrogenase active site region has been virtually eliminated such that acetaldehyde is transported from one active site to the other in a downhill process
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additional information
generation of enzyme overexpressing mutant strain 10-6C, which is a photosynthetic mutant impaired in CO2 assimilation because of a point mutation in the RBCL gene
additional information
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generation of enzyme overexpressing mutant strain 10-6C, which is a photosynthetic mutant impaired in CO2 assimilation because of a point mutation in the RBCL gene
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additional information
C7IV28
expression of a mutant enzyme (with a glycine to aspartic acid mutation in the NADH binding site of the ADH domain of AdhE) in Pyrococcus furiosus from which the native aldehyde oxidoreductase (AOR) gene is deleted results in a reduced ethanol production to the background level
additional information
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expression of a mutant enzyme (with a glycine to aspartic acid mutation in the NADH binding site of the ADH domain of AdhE) in Pyrococcus furiosus from which the native aldehyde oxidoreductase (AOR) gene is deleted results in a reduced ethanol production to the background level
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