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Information on EC 1.2.1.10 - acetaldehyde dehydrogenase (acetylating)
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EC Tree
1.2.1.10 acetaldehyde dehydrogenase (acetylating)IUBMB Comments
Also acts, more slowly, on glycolaldehyde, propanal and butanal. In several bacterial species this enzyme forms a bifunctional complex with EC 4.1.3.39, 4-hydroxy-2-oxovalerate aldolase. The enzymes from the bacteria Burkholderia xenovorans and Thermus thermophilus also perform the reaction of EC 1.2.1.87, propanal dehydrogenase (propanoylating). Involved in the meta-cleavage pathway for the degradation of phenols, methylphenols and catechols. NADP+ can replace NAD+ but the rate of reaction is much slower .
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Word Map
- 1.2.1.10
- synthesis
- propionaldehyde
-
nad-dependent
-
meta-cleavage
- biofuel production
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transthioesterification
- histolytica
- benzaldehyde
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pre-steady-state
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ammonia-lyase
- propionyl-coa
The enzyme appears in viruses and cellular organisms
Synonyms
dmpfg, coa-dependent aldehyde dehydrogenase, acetyl-coa reductase, tthb247, aldehyde dehydrogenase (acylating), coenzyme a linked aldehyde dehydrogenase, 4-hydroxy-2-ketovalerate aldolase/acylating acetaldehyde dehydrogenase, nonphosphorylating acylating aldehyde dehydrogenase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
4-hydroxy-2-ketovalerate aldolase/acylating acetaldehyde dehydrogenase
ACDH
acetaldehyde dehydrogenase
Acetaldehyde dehydrogenase [acetylating]
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acetaldehyde-alcohol dehydrogenase
acetyl-CoA reductase
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AdhE
aldehyde dehydrogenase (acylating)
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ALDH
CoA-dependent aldehyde dehydrogenase
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coenzyme A linked aldehyde dehydrogenase
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DmpF
DmpFG
NAD+/CoA-dependent aldehyde dehydrogenase
TTHB247
additional information
4-hydroxy-2-ketovalerate aldolase/acylating acetaldehyde dehydrogenase
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bifunctional enzyme
4-hydroxy-2-ketovalerate aldolase/acylating acetaldehyde dehydrogenase
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bifunctional enzyme
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ACDH
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acetaldehyde dehydrogenase
acetaldehyde dehydrogenase from Leuconostoc mesenteroides is a bifunctional enzyme possessing alcohol dehydrogenase und acetaldehyde dehydrogenase domains
acetaldehyde dehydrogenase
acetaldehyde dehydrogenase from Leuconostoc mesenteroides is a bifunctional enzyme possessing alcohol dehydrogenase und acetaldehyde dehydrogenase domains
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AdhE
bifunctional enzyme, containing both aldehyde dehydrogenase and alcohol dehydrogenase activities
AdhE
C7IV28
bifunctional enzyme, containing both aldehyde dehydrogenase and alcohol dehydrogenase activities
AdhE
C7IV28
bifunctional enzyme, containing both aldehyde dehydrogenase and alcohol dehydrogenase activities
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AdhE
bifunctional enzyme, catalyzes reactions of EC 1.1.1.1 and EC 1.2.1.10
AdhE
bifunctional enzyme, containing both aldehyde dehydrogenase and alcohol dehydrogenase activities
AdhE
bifunctional alcohol and aldehyde dehydrogenase gene
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
acetaldehyde + CoA + NAD+ = acetyl-CoA + NADH + H+
bi-uni-uni-uni-ping-pong mechanism
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acetaldehyde + CoA + NAD+ = acetyl-CoA + NADH + H+
bi-uni-uni-uni-ping-pong mechanism
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acetaldehyde + CoA + NAD+ = acetyl-CoA + NADH + H+
bi-uni-uni-uni-ping-pong mechanism
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acetaldehyde + CoA + NAD+ = acetyl-CoA + NADH + H+
part of a bifunctional enzyme complex that also displays 4-hydroxy-2-ketovalerate aldolase activity
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acetaldehyde + CoA + NAD+ = acetyl-CoA + NADH + H+
bi-uni-uni-uni-ping-pong mechanism
Escherichia coli B / ATCC 11303
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acetaldehyde + CoA + NAD+ = acetyl-CoA + NADH + H+
bi-uni-uni-uni-ping-pong mechanism
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acetaldehyde + CoA + NAD+ = acetyl-CoA + NADH + H+
part of a bifunctional enzyme complex that also displays 4-hydroxy-2-ketovalerate aldolase activity
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acetaldehyde + CoA + NAD+ = acetyl-CoA + NADH + H+
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
redox reaction
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reduction
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oxidation
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PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
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SYSTEMATIC NAME
IUBMB Comments
acetaldehyde:NAD+ oxidoreductase (CoA-acetylating)
Also acts, more slowly, on glycolaldehyde, propanal and butanal. In several bacterial species this enzyme forms a bifunctional complex with EC 4.1.3.39, 4-hydroxy-2-oxovalerate aldolase. The enzymes from the bacteria Burkholderia xenovorans and Thermus thermophilus also perform the reaction of EC 1.2.1.87, propanal dehydrogenase (propanoylating). Involved in the meta-cleavage pathway for the degradation of phenols, methylphenols and catechols. NADP+ can replace NAD+ but the rate of reaction is much slower [3].
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CAS REGISTRY NUMBER
COMMENTARY
9028-91-5
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
acetaldehyde + 2-mercaptoethanol + NAD+
S-acetyl-2-mercaptoethanol + NADH + H+
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14% activity compared to CoA
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r
acetaldehyde + CoA + NADP+
acetyl-CoA + NADPH + H+
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low activity with NADP+ compared to NAD+
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r
acetaldehyde + pantetheine + NAD+
S-acetyl-pantetheine + NADH + H+
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46% activity compared to CoA
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r
butyraldehyde + CoA + NAD+
butanoyl-CoA + NADH
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21% of the activity with acetaldehyde
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-
?
butyryl-CoA + NADH + H+
butyraldehyde + CoA + NAD+
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-
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r
picolinaldehyde + CoA + NAD+
picolinyl-CoA + NADH + H+
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-
-
r
propionaldehyde + CoA + NAD+
propanoyl-CoA + NADH
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51.8% of the activity with acetaldehyde
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-
?
valerylaldehyde + CoA + NAD+
valeryl-CoA + NADH + H+
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5.6% activity compared to acetaldehyde
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r
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH
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r
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH
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0.1 mM CoA can be replaced by 25 mM pantetheine, 46% of CoA activity, 25 mM 2-mercaptoethanol, 14% of CoA activity, 25 mM dithioerythritol, 10% of CoA activity, 25 mM glutathione, 8.6% of CoA activity, 25 mM cysteamine, 4.6% of CoA activity
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r
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH
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during ethanol fermentation
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?
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH
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during ethanol fermentation
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r
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH
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during glucose fermentation
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?
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH
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during glucose fermentation
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r
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH
Escherichia coli B / ATCC 11303
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during glucose fermentation
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r
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH
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enzyme carries aldehyde and alcohol dehydrogenase activity
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r
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH
Giardia intestinalis WB / CC 30957
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enzyme carries aldehyde and alcohol dehydrogenase activity
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r
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH
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ethanol production in aerobic glucose dissimilation
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r
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH
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involved in degradation of toxic aromatic compounds via the intermediate catechol
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r
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH
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involved in degradation of toxic aromatic compounds via the intermediate catechol
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r
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH + H+
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best substrates
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r
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH + H+
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?, r
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH + H+
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r
acetyl-CoA + NADH + H+
acetaldehyde + CoA + NAD+
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?
acetyl-CoA + NADH + H+
acetaldehyde + CoA + NAD+
activity of the enzyme is confirmed by proteome analysis and enzyme assays with cell extract glycerol-grown cells
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?
acetyl-CoA + NADH + H+
acetaldehyde + CoA + NAD+
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r
acetyl-CoA + NADH + H+
acetaldehyde + CoA + NAD+
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?
acetyl-CoA + NADH + H+
acetaldehyde + CoA + NAD+
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?
acetyl-CoA + NADH + H+
acetaldehyde + NAD+ + CoA
C7IV28
AdhE is a bifunctional enzyme, containing both aldehyde dehydrogenase and alcohol dehydrogenase activities
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?
acetyl-CoA + NADH + H+
acetaldehyde + NAD+ + CoA
C7IV28
AdhE is a bifunctional enzyme, containing both aldehyde dehydrogenase and alcohol dehydrogenase activities
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?
acetyl-CoA + NADH + H+
acetaldehyde + NAD+ + CoA
AdhE is a bifunctional enzyme, containing both aldehyde dehydrogenase and alcohol dehydrogenase activities
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?
acetyl-CoA + NADPH + H+
acetaldehyde + CoA + NADP+
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?
acetyl-CoA + NADPH + H+
acetaldehyde + CoA + NADP+
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r
acetyl-CoA + NADPH + H+
acetaldehyde + CoA + NADP+
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?
acetyl-CoA + NADPH + H+
acetaldehyde + CoA + NADP+
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?
butyraldehyde + CoA + NAD+
butyryl-CoA + NADH + H+
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21.0% activity compared to acetaldehyde
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r
butyraldehyde + CoA + NAD+
butyryl-CoA + NADH + H+
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r
butyraldehyde + CoA + NAD+
butyryl-CoA + NADH + H+
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r
butyryl-CoA + NADPH + H+
butyraldehyde + CoA + NADP+
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r
isobutyraldehyde + CoA + NAD+
isobutyryl-CoA + NADH
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?
n-butyraldehyde + CoA + NAD+
n-butyryl-CoA + NADH
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r
n-butyraldehyde + CoA + NAD+
n-butyryl-CoA + NADH
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r
propanal + CoA + NAD+
propionyl-CoA + NADH
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is used 63% as efficiently as acetaldehyde
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r
propanal + CoA + NAD+
propionyl-CoA + NADH
Giardia intestinalis WB / CC 30957
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is used 63% as efficiently as acetaldehyde
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r
propanal + CoA + NAD+
propionyl-CoA + NADH
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fermentation of 1,2-propanediol
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?, r
propanal + CoA + NAD+
propionyl-CoA + NADH
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initial rate of reaction with propanal is 2.7fold slower than that with acetaldehyde
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?
propanal + CoA + NAD+
propionyl-CoA + NADH
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initial rate of reaction with propanal is 2.7fold slower than that with acetaldehyde
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?
propionaldehyde + CoA + NAD+
propionyl-CoA + NADH + H+
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?
propionaldehyde + CoA + NAD+
propionyl-CoA + NADH + H+
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51.8% activity compared to acetaldehyde
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r
propionaldehyde + CoA + NAD+
propionyl-CoA + NADH + H+
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r
valeraldehyde + CoA + NAD+
valeryl-CoA + NADH
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5.6% of the activity with acetaldehyde
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?
additional information
?
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substrate chain length specificity of the enzyme is C2-C4, overview
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?
additional information
?
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the bifunctional enzymes commonly produce ethanol from acetyl-CoA with acetaldehyde as intermediate
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additional information
?
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ADHE catalyzes the reversible NADH-mediated interconversions of acetyl-CoA, acetaldehyde, and ethanol but seemed to be poised toward the production of ethanol from acetaldehyde
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additional information
?
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the bifunctional enzymes commonly produce ethanol from acetyl-CoA with acetaldehyde as intermediate
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additional information
?
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ADHE catalyzes the reversible NADH-mediated interconversions of acetyl-CoA, acetaldehyde, and ethanol but seemed to be poised toward the production of ethanol from acetaldehyde
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additional information
?
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bifunctional enzyme consisting of an N-terminal acetaldehyde dehydrogenase (ALDH) and a C-terminal alcohol dehydrogenase (ADH). The specificity constant (kcat/Km) is 47fold higher for acetaldehyde reductase than that for ethanol dehydrogenase
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?
additional information
?
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the enzyme has the ability to oxidize straight-chain aldehydes. The ADHES77 shows relatively high specific activity for acetaldehyde, as compared to activities for propionaldehyde, butyraldehyde, and valeraldehyde. The ADHES77 can use various types of aldehydes as substrates, in which the ADHES77 has a preference for C2 acetaldehyde when compared to C3-C5 aldehydes. No activity with formaldehyde and benzaldehyde as substrates
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?
additional information
?
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not: formaldehyde, chloral, benzaldehyde
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?
additional information
?
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not: chloral, formaldehyde, D,L-glyceraldehyde
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?
additional information
?
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the bifunctional enzymes commonly produce ethanol from acetyl-CoA with acetaldehyde as intermediate
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additional information
?
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BphJ forms a heterotetrameric complex with the class II aldolase BphI that channels aldehydes produced in the aldol cleavage reaction to the dehydrogenase via a molecular tunnel
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?
additional information
?
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not: formaldehyde, octylaldehyde, benzaldehyde, D,L-glyceraldehyde, glycolaldehyde
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?
additional information
?
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DmpFG is a bifunctional enzyme comprised of an aldolase subunit, DmpG, and a dehydrogenase subunit, DmpF. The aldehyde intermediate produced by the aldolase is channeled directly through a buried molecular channel in the protein structure from the aldolase to the dehydrogenase active site. Binding and channeling of alternative substrates in the enzyme DmpFG, molecular dynamics, overview
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?
additional information
?
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DmpFG is a bifunctional enzyme comprised of an aldolase subunit, DmpG, and a dehydrogenase subunit, DmpF. The aldehyde intermediate produced by the aldolase is channeled directly through a buried molecular channel in the protein structure from the aldolase to the dehydrogenase active site. Binding and channeling of alternative substrates in the enzyme DmpFG, molecular dynamics, overview
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?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
propionaldehyde + CoA + NAD+
propionyl-CoA + NADH + H+
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?
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH
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r
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH
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during ethanol fermentation
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?
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH
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during ethanol fermentation
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r