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
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nad-dependent
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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
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
results (
results (Substrates Products
Substrates Products on EC 1.2.1.10 - acetaldehyde dehydrogenase (acetylating)
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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+
-
-
r
acetaldehyde + pantetheine + NAD+
S-acetyl-pantetheine + NADH + H+
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46% activity compared to CoA
-
-
r
butyraldehyde + CoA + NAD+
butanoyl-CoA + NADH
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21% of the activity with acetaldehyde
-
-
?
butyryl-CoA + NADH + H+
butyraldehyde + CoA + NAD+
-
-
-
r
picolinaldehyde + CoA + NAD+
picolinyl-CoA + NADH + H+
-
-
-
r
propionaldehyde + CoA + NAD+
propanoyl-CoA + NADH
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51.8% of the activity with acetaldehyde
-
-
?
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
-
-
-
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+
-
-
-
?, r
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH + H+
-
-
-
r
acetyl-CoA + NADH + H+
acetaldehyde + CoA + NAD+
-
-
-
?
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+
-
-
-
r
acetyl-CoA + NADH + H+
acetaldehyde + CoA + NAD+
-
-
-
?
acetyl-CoA + NADH + H+
acetaldehyde + CoA + NAD+
-
-
-
?
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+
-
-
-
-
r
acetyl-CoA + NADPH + H+
acetaldehyde + CoA + NADP+
-
-
-
?
acetyl-CoA + NADPH + H+
acetaldehyde + CoA + NADP+
-
-
-
?
butyraldehyde + CoA + NAD+
butyryl-CoA + NADH + H+
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21.0% activity compared to acetaldehyde
-
-
r
butyraldehyde + CoA + NAD+
butyryl-CoA + NADH + H+
-
-
-
r
butyraldehyde + CoA + NAD+
butyryl-CoA + NADH + H+
-
-
-
r
butyryl-CoA + NADPH + H+
butyraldehyde + CoA + NADP+
-
-
-
-
r
isobutyraldehyde + CoA + NAD+
isobutyryl-CoA + NADH
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-
-
-
?
n-butyraldehyde + CoA + NAD+
n-butyryl-CoA + NADH
-
-
-
-
r
n-butyraldehyde + CoA + NAD+
n-butyryl-CoA + NADH
-
-
-
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+
-
-
-
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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-
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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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-
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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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-
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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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?
