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Information on EC 1.2.1.10 - acetaldehyde dehydrogenase (acetylating)
for references in articles please use BRENDA:EC1.2.1.10
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EC Tree 1 Oxidoreductases
1.2 Acting on the aldehyde or oxo group of donors
1.2.1 With NAD+ or NADP+ as acceptor
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 .
The enzyme appears in viruses and cellular organisms
- 1.2.1.10
- synthesis
- propionaldehyde
-
nad-dependent
-
meta-cleavage
- biofuel production
-
transthioesterification
- histolytica
- benzaldehyde
-
pre-steady-state
-
ammonia-lyase
- propionyl-coa
showSynonyms
dmpfg, coa-dependent aldehyde dehydrogenase, acetyl-coa reductase, aldehyde dehydrogenase (acylating), tthb247, 4-hydroxy-2-ketovalerate aldolase/acylating acetaldehyde dehydrogenase, nonphosphorylating acylating aldehyde dehydrogenase, coenzyme a linked aldehyde dehydrogenase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
4-hydroxy-2-ketovalerate aldolase/acylating acetaldehyde dehydrogenase
ACDH
acetaldehyde dehydrogenase
Acetaldehyde dehydrogenase [acetylating]
-
-
-
-
acetaldehyde-alcohol dehydrogenase
acetyl-CoA reductase
-
-
-
-
AdhE
aldehyde dehydrogenase (acylating)
-
-
-
-
ALDH
CoA-dependent aldehyde dehydrogenase
-
-
-
-
coenzyme A linked aldehyde dehydrogenase
-
-
-
-
DmpF
DmpFG
NAD+/CoA-dependent aldehyde dehydrogenase
TTHB247
additional information
4-hydroxy-2-ketovalerate aldolase/acylating acetaldehyde dehydrogenase
-
bifunctional enzyme
4-hydroxy-2-ketovalerate aldolase/acylating acetaldehyde dehydrogenase
-
bifunctional enzyme
-
ACDH
-
-
-
-
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
-
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
-
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
-
acetaldehyde + CoA + NAD+ = acetyl-CoA + NADH + H+
bi-uni-uni-uni-ping-pong mechanism
-
acetaldehyde + CoA + NAD+ = acetyl-CoA + NADH + H+
bi-uni-uni-uni-ping-pong mechanism
-
acetaldehyde + CoA + NAD+ = acetyl-CoA + NADH + H+
part of a bifunctional enzyme complex that also displays 4-hydroxy-2-ketovalerate aldolase activity
-
acetaldehyde + CoA + NAD+ = acetyl-CoA + NADH + H+
bi-uni-uni-uni-ping-pong mechanism
Escherichia coli B / ATCC 11303
-
-
acetaldehyde + CoA + NAD+ = acetyl-CoA + NADH + H+
bi-uni-uni-uni-ping-pong mechanism
-
-
acetaldehyde + CoA + NAD+ = acetyl-CoA + NADH + H+
part of a bifunctional enzyme complex that also displays 4-hydroxy-2-ketovalerate aldolase activity
-
-
acetaldehyde + CoA + NAD+ = acetyl-CoA + NADH + H+
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
redox reaction
-
-
-
-
reduction
-
-
-
-
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+
-
14% activity compared to CoA
-
-
r
acetaldehyde + CoA + NADP+
acetyl-CoA + NADPH + H+
-
low activity with NADP+ compared to NAD+
-
-
r
acetaldehyde + pantetheine + NAD+
S-acetyl-pantetheine + NADH + H+
-
46% activity compared to CoA
-
-
r
butyraldehyde + CoA + NAD+
butanoyl-CoA + NADH
-
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
-
51.8% of the activity with acetaldehyde
-
-
?
valerylaldehyde + CoA + NAD+
valeryl-CoA + NADH + H+
-
5.6% activity compared to acetaldehyde
-
-
r
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH
-
-
-
r
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH
-
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
-
r
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH
-
during ethanol fermentation
-
?
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH
-
during ethanol fermentation
-
r
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH
-
during glucose fermentation
-
?
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH
-
during glucose fermentation
-
r
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH
Escherichia coli B / ATCC 11303
-
during glucose fermentation
-
r
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH
-
enzyme carries aldehyde and alcohol dehydrogenase activity
-
r
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH
Giardia intestinalis WB / CC 30957
-
enzyme carries aldehyde and alcohol dehydrogenase activity
-
r
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH
-
ethanol production in aerobic glucose dissimilation
-
r
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH
-
involved in degradation of toxic aromatic compounds via the intermediate catechol
-
-
r
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH
-
involved in degradation of toxic aromatic compounds via the intermediate catechol
-
-
r
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH + H+
-
best substrates
-
-
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
-
-
?
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
-
-
?
acetyl-CoA + NADH + H+
acetaldehyde + NAD+ + CoA
C7IV28
AdhE is a bifunctional enzyme, containing both aldehyde dehydrogenase and alcohol dehydrogenase activities
-
-
?
acetyl-CoA + NADH + H+
acetaldehyde + NAD+ + CoA
AdhE is a bifunctional enzyme, containing both aldehyde dehydrogenase and alcohol dehydrogenase activities
-
-
?
acetyl-CoA + NADPH + H+
acetaldehyde + CoA + NADP+
-
-
-
?
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+
-
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
-
-
-
-
?
n-butyraldehyde + CoA + NAD+
n-butyryl-CoA + NADH
-
-
-
-
r
n-butyraldehyde + CoA + NAD+
n-butyryl-CoA + NADH
-
-
-
r
propanal + CoA + NAD+
propionyl-CoA + NADH
-
is used 63% as efficiently as acetaldehyde
-
r
propanal + CoA + NAD+
propionyl-CoA + NADH
Giardia intestinalis WB / CC 30957
-
is used 63% as efficiently as acetaldehyde
-
r
propanal + CoA + NAD+
propionyl-CoA + NADH
-
fermentation of 1,2-propanediol
-
?, r
propanal + CoA + NAD+
propionyl-CoA + NADH
-
initial rate of reaction with propanal is 2.7fold slower than that with acetaldehyde
-
-
?
propanal + CoA + NAD+
propionyl-CoA + NADH
-
initial rate of reaction with propanal is 2.7fold slower than that with acetaldehyde
-
-
?
propionaldehyde + CoA + NAD+
propionyl-CoA + NADH + H+
-
-
-
?
propionaldehyde + CoA + NAD+
propionyl-CoA + NADH + H+
-
51.8% activity compared to acetaldehyde
-
-
r
propionaldehyde + CoA + NAD+
propionyl-CoA + NADH + H+
-
-
-
r
valeraldehyde + CoA + NAD+
valeryl-CoA + NADH
-
5.6% of the activity with acetaldehyde
-
-
?
additional information
?
-
-
substrate chain length specificity of the enzyme is C2-C4, overview
-
-
?
additional information
?
-
the bifunctional enzymes commonly produce ethanol from acetyl-CoA with acetaldehyde as intermediate
-
-
-
additional information
?
-
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
-
-
-
additional information
?
-
the bifunctional enzymes commonly produce ethanol from acetyl-CoA with acetaldehyde as intermediate
-
-
-
additional information
?
-
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
-
-
-
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
not: formaldehyde, chloral, benzaldehyde
-
-
?
additional information
?
-
-
not: chloral, formaldehyde, D,L-glyceraldehyde
-
-
?
additional information
?
-
the bifunctional enzymes commonly produce ethanol from acetyl-CoA with acetaldehyde as intermediate
-
-
-
additional information
?
-
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
-
-
?
additional information
?
-
-
not: formaldehyde, octylaldehyde, benzaldehyde, D,L-glyceraldehyde, glycolaldehyde
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
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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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+
-
-
-
?
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH
-
-
-
r
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH
-
during ethanol fermentation
-
?
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH
-
during ethanol fermentation
-
r
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH
-
during glucose fermentation
-
?
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH
-
during glucose fermentation
-
r
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH
Escherichia coli B / ATCC 11303
-
during glucose fermentation
-
r
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH
-
ethanol production in aerobic glucose dissimilation
-
r
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH
-
involved in degradation of toxic aromatic compounds via the intermediate catechol
-
-
r
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH
-
involved in degradation of toxic aromatic compounds via the intermediate catechol
-
-
r
propanal + CoA + NAD+
propionyl-CoA + NADH
-
is used 63% as efficiently as acetaldehyde
-
r
propanal + CoA + NAD+
propionyl-CoA + NADH
Giardia intestinalis WB / CC 30957
-
is used 63% as efficiently as acetaldehyde
-
r
propanal + CoA + NAD+
propionyl-CoA + NADH
-
fermentation of 1,2-propanediol
-
r
additional information
?
-
the bifunctional enzymes commonly produce ethanol from acetyl-CoA with acetaldehyde as intermediate
-
-
-
additional information
?
-
the bifunctional enzymes commonly produce ethanol from acetyl-CoA with acetaldehyde as intermediate
-
-
-
additional information
?
-
the bifunctional enzymes commonly produce ethanol from acetyl-CoA with acetaldehyde as intermediate
-
-
-
additional information
?
-
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
-
-
?
additional information
?
-
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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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
CoA
-
shares a binding site with NAD+. Rossmann fold can alternately bind CoA or NAD+ cofactors required for enzymatic catalysis
NAD+
-
shares a binding site with CoA. Rossmann fold can alternately bind CoA or NAD+ cofactors required for enzymatic catalysis
NADH
-
shows also activity with NADPH, NADH is more effective than NADPH
additional information
-
enzyme is able to acetylate other thiols than CoA, e.g. pantetheine, 2-mercaptoethanol, dithioerythritol, glutathione, cysteamine
-
additional information
-
the purified ADHES77 preferred to use NAD+ as an electron acceptor as compared to NADP+. In the specific activities of acetaldehyde dehydrogenase, the catalytic efficiencies for NAD+ i about 15.7 greater than for NADP+. Similarly, in the catalytic reductions of acetyl-CoA, the ADHES77 preferentially utilizes NADH as an electron donor, exhibiting approximately 5.6fold higher activity than for NADPH. The results suggest that the ADHES77 prefers to use NAD(H) as redox partners as compared to NADP(H)
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe2+
Fe2+
the residues potentially involved in iron coordination are Asp727, His731, His797, and His811. Two signatures for iron-binding are identified in the ADH domain: ADH_iron_1 (residues 706-734) and ADH_iron_2 (residues 794-814)
Fe2+
-
3fold activation with 0.00003 mM, 5fold activation with 0.03 mM, activation only of NADH oxidation, not NAD+ reduction
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
acetyl-CoA
-
competitive inhibitor with respect to NAD+; competitive to NAD+
additional information
-
low ionic strength buffers, 0.2 M boric acid/Na2CO3, 0.2 M glycine/NaOH, 0.2 M NH4Cl/NH4OH, pH 8.0, not inhibitory at 1 mM: K+, Na+, Li+, Mg2+, Mn2+, Zn2 +, Ca2+, Fe2+, Fe3+, EDTA, p-chloromercuribenzoate, iodoacetate, N3-, dipyridyl, lactic acid, acetic acid, ethanol, acetylphosphate, pyruvic acid, adenine, adenosine, guanine, guanosine, GMP, GDP, not inhibitory at 0.1 mM: NADP+, NADPH
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3-pyridinecarboxaldehyde adenine dinucleotide
-
NAD+ analogue, activates by binding strongly to activator site, binds weakly to catalytic site
NAD+
-
reduces lag phase before attainment of steady state rate in conjunction with 2-mercaptoethanol
2-mercaptoethanol
-
reduces lag phase before attainment of steady state rate in conjunction with NAD+
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
8.2
pentaldehyde
mutant enzyme I195A, at 25°C in 100 mM HEPES buffer (pH 8.0)
17
acetaldehyde
mutant enzyme I171A, at 25°C in 100 mM HEPES buffer (pH 8.0)
18.7
acetaldehyde
mutant enzyme D208A, at 25°C in 100 mM HEPES buffer (pH 8.0)
23.6
acetaldehyde
wild type enzyme, at 25°C in 100 mM HEPES buffer (pH 8.0)
34.9
acetaldehyde
mutant enzyme I171F, at 25°C in 100 mM HEPES buffer (pH 8.0)
45.6
acetaldehyde
mutant enzyme I195F, at 25°C in 100 mM HEPES buffer (pH 8.0)
133
acetaldehyde
mutant enzyme I195A, at 25°C in 100 mM HEPES buffer (pH 8.0)
0.0127
acetyl-CoA
pH 7.0, temperature not specified in the publication
3.7
Butyraldehyde
-
reverse reaction, with 0.32 mM NAD+ and 0.12 mM CoA
4.6
Butyraldehyde
mutant enzyme I195A, at 25°C in 100 mM HEPES buffer (pH 8.0)
12.6
Butyraldehyde
mutant enzyme I171A, at 25°C in 100 mM HEPES buffer (pH 8.0)
19.3
Butyraldehyde
mutant enzyme I171F, at 25°C in 100 mM HEPES buffer (pH 8.0)
31.7
Butyraldehyde
wild type enzyme, at 25°C in 100 mM HEPES buffer (pH 8.0)
0.064
CoA
-
reverse reaction, with 0.32 mM NAD+ and 11 mM butyraldehyde
0.25
NAD+
-
reverse reaction, with 0.12 mM CoA and 11 mM butyraldehyde
3.2
picolinaldehyde
mutant enzyme I171A, at 25°C in 100 mM HEPES buffer (pH 8.0)
6.9
picolinaldehyde
mutant enzyme I195A, at 25°C in 100 mM HEPES buffer (pH 8.0)
12
picolinaldehyde
mutant enzyme I171F, at 25°C in 100 mM HEPES buffer (pH 8.0)
18.2
picolinaldehyde
wild type enzyme, at 25°C in 100 mM HEPES buffer (pH 8.0)
20.4
propionaldehyde
mutant enzyme I171A, at 25°C in 100 mM HEPES buffer (pH 8.0)
23.1
propionaldehyde
wild type enzyme, at 25°C in 100 mM HEPES buffer (pH 8.0)
27.2
propionaldehyde
mutant enzyme I171F, at 25°C in 100 mM HEPES buffer (pH 8.0)
31.5
propionaldehyde
mutant enzyme I195A, at 25°C in 100 mM HEPES buffer (pH 8.0)
79.5
propionaldehyde
mutant enzyme I195F, at 25°C in 100 mM HEPES buffer (pH 8.0)
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
-
no Michaelis-Menten behaviour
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
13
pentaldehyde
mutant enzyme I195A, at 25°C in 100 mM HEPES buffer (pH 8.0)
6.9
acetaldehyde
mutant enzyme I195W, at 25°C in 100 mM HEPES buffer (pH 8.0)
7.6
acetaldehyde
mutant enzyme D208A, at 25°C in 100 mM HEPES buffer (pH 8.0)
7.8
acetaldehyde
mutant enzyme I171F, at 25°C in 100 mM HEPES buffer (pH 8.0)
15.4
acetaldehyde
mutant enzyme I195F, at 25°C in 100 mM HEPES buffer (pH 8.0)
17.2
acetaldehyde
wild type enzyme, at 25°C in 100 mM HEPES buffer (pH 8.0)
19.7
acetaldehyde
mutant enzyme I195A, at 25°C in 100 mM HEPES buffer (pH 8.0)
37.9
acetaldehyde
mutant enzyme I171A, at 25°C in 100 mM HEPES buffer (pH 8.0)
7.1
Butyraldehyde
mutant enzyme I171F, at 25°C in 100 mM HEPES buffer (pH 8.0)
9.5
Butyraldehyde
wild type enzyme, at 25°C in 100 mM HEPES buffer (pH 8.0)
12.6
Butyraldehyde
mutant enzyme I195A, at 25°C in 100 mM HEPES buffer (pH 8.0)
16.7
Butyraldehyde
mutant enzyme I171A, at 25°C in 100 mM HEPES buffer (pH 8.0)
1.9
picolinaldehyde
mutant enzyme I171A, at 25°C in 100 mM HEPES buffer (pH 8.0)
2.4
picolinaldehyde
mutant enzyme I171F, at 25°C in 100 mM HEPES buffer (pH 8.0)
2.8
picolinaldehyde
wild type enzyme, at 25°C in 100 mM HEPES buffer (pH 8.0)
3.2
picolinaldehyde
mutant enzyme I195A, at 25°C in 100 mM HEPES buffer (pH 8.0)
3.4
propionaldehyde
mutant enzyme I195W, at 25°C in 100 mM HEPES buffer (pH 8.0)
6
propionaldehyde
mutant enzyme I171F, at 25°C in 100 mM HEPES buffer (pH 8.0)
7.6
propionaldehyde
mutant enzyme I195F, at 25°C in 100 mM HEPES buffer (pH 8.0)
12.1
propionaldehyde
mutant enzyme I195A, at 25°C in 100 mM HEPES buffer (pH 8.0)
16.3
propionaldehyde
wild type enzyme, at 25°C in 100 mM HEPES buffer (pH 8.0)
24.9
propionaldehyde
mutant enzyme I171A, at 25°C in 100 mM HEPES buffer (pH 8.0)
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.147
acetaldehyde
mutant enzyme I195A, at 25°C in 100 mM HEPES buffer (pH 8.0)
0.152
acetaldehyde
mutant enzyme I195W, at 25°C in 100 mM HEPES buffer (pH 8.0)
0.223
acetaldehyde
mutant enzyme I171F, at 25°C in 100 mM HEPES buffer (pH 8.0)
0.457
acetaldehyde
mutant enzyme I195F, at 25°C in 100 mM HEPES buffer (pH 8.0)
0.46
acetaldehyde
mutant enzyme D208A, at 25°C in 100 mM HEPES buffer (pH 8.0)
0.73
acetaldehyde
wild type enzyme, at 25°C in 100 mM HEPES buffer (pH 8.0)
2.224
acetaldehyde
mutant enzyme I171A, at 25°C in 100 mM HEPES buffer (pH 8.0)
0.0433
Butyraldehyde
mutant enzyme I195F, at 25°C in 100 mM HEPES buffer (pH 8.0)
0.0458
Butyraldehyde
mutant enzyme I195W, at 25°C in 100 mM HEPES buffer (pH 8.0)
0.3
Butyraldehyde
wild type enzyme, at 25°C in 100 mM HEPES buffer (pH 8.0)
0.37
Butyraldehyde
mutant enzyme I171F, at 25°C in 100 mM HEPES buffer (pH 8.0)
1.323
Butyraldehyde
mutant enzyme I171A, at 25°C in 100 mM HEPES buffer (pH 8.0)
2.763
Butyraldehyde
mutant enzyme I195A, at 25°C in 100 mM HEPES buffer (pH 8.0)
0.0265
pentaldehyde
mutant enzyme I195W, at 25°C in 100 mM HEPES buffer (pH 8.0)
0.0346
pentaldehyde
mutant enzyme I195F, at 25°C in 100 mM HEPES buffer (pH 8.0)
0.0728
pentaldehyde
mutant enzyme I171A, at 25°C in 100 mM HEPES buffer (pH 8.0)
0.076
pentaldehyde
wild type enzyme, at 25°C in 100 mM HEPES buffer (pH 8.0)
1.584
pentaldehyde
mutant enzyme I195A, at 25°C in 100 mM HEPES buffer (pH 8.0)
0.00011
picolinaldehyde
mutant enzyme I195W, at 25°C in 100 mM HEPES buffer (pH 8.0)
0.00076
picolinaldehyde
mutant enzyme I195F, at 25°C in 100 mM HEPES buffer (pH 8.0)
0.0387
picolinaldehyde
mutant enzyme I171F, at 25°C in 100 mM HEPES buffer (pH 8.0)
0.154
picolinaldehyde
wild type enzyme, at 25°C in 100 mM HEPES buffer (pH 8.0)
0.468
picolinaldehyde
mutant enzyme I195A, at 25°C in 100 mM HEPES buffer (pH 8.0)
0.597
picolinaldehyde
mutant enzyme I171A, at 25°C in 100 mM HEPES buffer (pH 8.0)
0.0425
propionaldehyde
mutant enzyme I195W, at 25°C in 100 mM HEPES buffer (pH 8.0)
0.167
propionaldehyde
mutant enzyme I195F, at 25°C in 100 mM HEPES buffer (pH 8.0)
0.221
propionaldehyde
mutant enzyme I171F, at 25°C in 100 mM HEPES buffer (pH 8.0)
0.384
propionaldehyde
mutant enzyme I195A, at 25°C in 100 mM HEPES buffer (pH 8.0)
0.7
propionaldehyde
wild type enzyme, at 25°C in 100 mM HEPES buffer (pH 8.0)
1.219
propionaldehyde
mutant enzyme I171A, at 25°C in 100 mM HEPES buffer (pH 8.0)
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.04
gene AdhE deletion mutant, cosubstrate NADH, pH 7.0, 55°C
0.05
wild-type, cosubstrate NADPH, pH 7.0, 55°C
0.09
0.1
gene AdhE deletion mutant, cosubstrate NADPH, pH 7.0, 55°C
1.6
crude extracts from expression in Escherichia coli DH5alpha, one unit is defined as the amount of enzyme activity that catalysed the transformation of 1 micromol NADH per min
1.7
7.36
8.75
-
bifunctional fusion protein of aldehyde and alcohol dehydrogenase
0.09
gene AdhE deletion mutant, cosubstrate NADH, pH 7.0, 55°C
0.09
gene AdhE deletion mutant, cosubstrate NADPH, pH 7.0, 55°C
0.09
wild-type, cosubstrate NADH, pH 7.0, 55°C
1.7
crude extracts from expression in Escherichia coli BL21, one unit is defined as the amount of enzyme activity that catalysed the transformation of 1 micromol NADH per min
7.36
-
purified native enzyme, acetaldehyde oxidation with NAD+, pH 7.0, 30°C
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5
6.8
8.5
8.8
-
in cyclohexylaminoethanesulfonic acid or Tris-(hydroxymethyl)-methyl-amino-propanesulfonic acid buffer
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5 - 8
-
narrow activity range, inactivation at pH 5.5, profile overview
6.2 - 7.4
-
67% of maximal activity at pH 6.2, 79% of maximal activity at pH 7.4
8.5 - 10
-
70% of maximal activity at pH 8.5, 80% of maximal activity at pH 10
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
40
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20 - 60
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
bifunctional aldehyde-alcohol dehydrogenase
UniProt
brenda
bifunctional aldehyde-alcohol dehydrogenase
UniProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
at pH 6.0 and pH 3.7
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
higher enzyme level in mitochondria from cells grown at pH 6.0 than in mitochondria from cells grown at pH 3.7
brenda
additional information
additional information
the enzyme protein exhibits an extended N-terminus (about 60 residues), which serves as an intracellular targeting signal
-
brenda
additional information
-
the enzyme protein exhibits an extended N-terminus (about 60 residues), which serves as an intracellular targeting signal
-
-
brenda
additional information
the enzyme occurs in an oligomeric form called spirosomes
-
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
cells with increased ADHE abundance exhibit better survival under dark anoxia
metabolism
physiological function
additional information
evolution
distribution of ADHE among the five eukaryotic supergroups, overview
evolution
the bifunctional AdhE enzyme is conserved in all bacterial kingdoms but also in more phylogenetically distant microorganisms such as green microalgae
metabolism
DmpFG catalyzes the final two steps of the meta-cleavage pathway of catechol and its methylated substituents. This pathway breaks down toxic waste products such as naphthalenes, salicylates, and benzoates to harmless metabolites
metabolism
ADHE can be involved either in ethanol production or assimilation, or both, depending upon environmental conditions. Presence of ADHE in an oxygen-respiring algal mitochondrion and co-expression at ambient oxygen levels with respiratory chain components is unexpected with respect to the view that eukaryotes acquire ADHE genes specifically as an adaptation to an anaerobic lifestyle
metabolism
-
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
metabolism
anaerobic fermentative metabolism of glycerol. Proteome analysis as well as enzyme assays performed in cell-free extracts demonstrate that glycerol is degraded via glyceraldehyde-3-phosphate, which is further metabolized through the lower part of glycolysis leading to formation of mainly ethanol and hydrogen
metabolism
analysis of the anerobic metabolic routes involving the enzyme in Chlamydomonas reinhardtii, overview
metabolism
-
DmpFG catalyzes the final two steps of the meta-cleavage pathway of catechol and its methylated substituents. This pathway breaks down toxic waste products such as naphthalenes, salicylates, and benzoates to harmless metabolites
-
physiological function
deletion of the bifunctional alcohol and aldehyde dehydrogenase gene adhE reduces ethanol production by more than 95%. In the deletion strain, fermentation products shift from ethanol to lactate production and result in lower cell density and longer time to reach maximal cell density. It loses more than 85% of alcohol dehydrogenase activity. Aldehyde dehydrogenase activity does not appear to be affected, although its activity is low in cell extracts. Adding ubiquinone-0 to the aldehyde dehydrogenase assay increases activity in the parent strain but does not increase activity in the adhE deletion strain
physiological function
deletion of the bifunctional alcohol and aldehyde dehydrogenase gene adhE reduces ethanol production by more than 95%. In the deletion strains, fermentation products shift from ethanol to lactate production and result in lower cell density and longer time to reach maximal cell density. The deletion strain additionally contains a point mutation in the lactate dehydrogenase gene, which appears to deregulate its activation by fructose 1,6-bisphosphate, leading to constitutive activation of lactate dehydrogenase
physiological function
deletion of adhE reduces ethanol production by more than 95%. Fermentation products shift from ethanol to lactate production and result in lower cell density and longer time to reach maximal cell density. The adhE deletion strain loses more than 85% of alcohol dehydrogenase activity. Aldehyde dehydrogenase activity does not appear to be affected
physiological function
deletion of adhE reduces ethanol production by more than 95%. Fermentation products shift from ethanol to lactate production and result in lower cell density and longer time to reach maximal cell density. The adhE deletion strain loses more than 90% of ALDH and ADH activity in cell extracts
physiological function
-
acetaldehyde-alcohol dehydrogenase (ADHE) is a bifunctional enzyme consisting of two domains of an N-terminal acetaldehyde dehydrogenase (ALDH) and a C-terminal alcohol dehydrogenase (ADH). The N-terminal domain is responsible for the conversion of acetyl-CoA to acetaldehyde and the C-terminal domain is subsequently responsible for the conversion of acetaldehyde to ethanol. The enzyme is important in the cellular alcohol metabolism. The coenzyme A-acylating ADHE from Citrobacter sp. S-77 may play a pivotal role in modulating intracellular acetaldehyde concentration
physiological function
acetaldehyde-alcohol dehydrogenase (AdhE) enzymes are a key metabolic enzyme in bacterial physiology and pathogenicity. They convert acetyl-CoA to ethanol via an acetaldehyde intermediate during ethanol fermentation in an anaerobic environment. This two-step reaction is associated to NAD+ regeneration, essential for glycolysis. The biological role of AdhE seems to go beyond alcoholic fermentation. This protein could also be directly or indirectly involved in bacterial pathogenicity
physiological function
aldehyde/alcohol dehydrogenases (ADHEs) are bifunctional enzymes that commonly produce ethanol from acetyl-CoA with acetaldehyde as intermediate and play a key role in anaerobic redox balance in many fermenting bacteria. ADHEs are also present in photosynthetic unicellular eukaryotes
physiological function
Acetivibrio thermocellus DSM 1237
-
deletion of the bifunctional alcohol and aldehyde dehydrogenase gene adhE reduces ethanol production by more than 95%. In the deletion strains, fermentation products shift from ethanol to lactate production and result in lower cell density and longer time to reach maximal cell density. The deletion strain additionally contains a point mutation in the lactate dehydrogenase gene, which appears to deregulate its activation by fructose 1,6-bisphosphate, leading to constitutive activation of lactate dehydrogenase
-
physiological function
-
deletion of the bifunctional alcohol and aldehyde dehydrogenase gene adhE reduces ethanol production by more than 95%. In the deletion strain, fermentation products shift from ethanol to lactate production and result in lower cell density and longer time to reach maximal cell density. It loses more than 85% of alcohol dehydrogenase activity. Aldehyde dehydrogenase activity does not appear to be affected, although its activity is low in cell extracts. Adding ubiquinone-0 to the aldehyde dehydrogenase assay increases activity in the parent strain but does not increase activity in the adhE deletion strain
-
physiological function
-
aldehyde/alcohol dehydrogenases (ADHEs) are bifunctional enzymes that commonly produce ethanol from acetyl-CoA with acetaldehyde as intermediate and play a key role in anaerobic redox balance in many fermenting bacteria. ADHEs are also present in photosynthetic unicellular eukaryotes
-
additional information
-
the enzyme's two functional domains are fused into a single polypeptide by a linker amino acid region
additional information
filamentation of the bacterial bifunctional alcohol/aldehyde dehydrogenase AdhE is essential for substrate channeling and enzymatic regulation. Incubation with NAD+ and Fe2+ is sufficient to extend the filaments. The addition of coenzyme A does not impair the conformational change triggered by NAD+ and Fe2+. In the same conditions, NADH and Fe2+ are not able to trigger a conformational change from the compact to the extended form. Comparison of the structure of AdhE in its extended conformation with monofunctional ADH and AlDH enzymes, overview. The substrate/product channels of both the AlDH and ADH domains lead to the two cavities located at the AlDH-ADH interfaces within the AdhE dimer. The loops 2 and 3 seal this cavity by mediating the interactions between the AlDH and ADH domains. This allows a direct channeling between the AlDH and ADH domain active sites
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
100000
148000
-
gel filtration, molecular mass of enzyme complex, occurs in complex with 4-hydroxy-2-ketovalerate
32500
-
2 * 32500 + 2 * 39000, determined by nucleotide sequence, SDS-PAGE, two subunits of aldehyde dehydrogenase (acylating) and two of 4-hydroxy-2-ketovalerate
39000
-
2 * 32500 + 2 * 39000, determined by nucleotide sequence, SDS-PAGE, two subunits of aldehyde dehydrogenase (acylating) and two of 4-hydroxy-2-ketovalerate
400000
96000
96000
-
ca. 40 * 96000, pyruvate-formate-lyase-deactivase with alcohol and aldehyde dehydrogenase activity, nucleotide sequence
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
homotetramer
oligomer
the enzyme occurs in an oligomeric form called spirosomes. Incubation with NAD+ and Fe2+ is sufficient to extend the filaments. The addition of coenzyme A does not impair the conformational change triggered by NAD+ and Fe2+. In the same conditions, NADH and Fe2+ are not able to trigger a conformational change from the compact to the extended form. CryoEM analysis of the AdhE spirosomes in their compact and extended forms, enzyme filaments and quarternary structure analysis, overview
polymer
-
ca. 40 * 96000, pyruvate-formate-lyase-deactivase with alcohol and aldehyde dehydrogenase activity, nucleotide sequence
tetramer
additional information
tetramer
-
2 * 32500 + 2 * 39000, determined by nucleotide sequence, SDS-PAGE, two subunits of aldehyde dehydrogenase (acylating) and two of 4-hydroxy-2-ketovalerate
tetramer
-
composed of two dimers, one dimer accounts for 4-hydroxy-2-ketovalerate aldolase, subunit size 37500, and one for acylating acetaldehyde dehydrogenase, subunit size 32500
tetramer
-
2 * 32500 + 2 * 39000, determined by nucleotide sequence, SDS-PAGE, two subunits of aldehyde dehydrogenase (acylating) and two of 4-hydroxy-2-ketovalerate
-
tetramer
-
composed of two dimers, one dimer accounts for 4-hydroxy-2-ketovalerate aldolase, subunit size 37500, and one for acylating acetaldehyde dehydrogenase, subunit size 32500
-
additional information
the enzyme is associated in dimers and higher order oligomers in the chloroplast. Domain structure, overview. In contrast to the native enzyme, the recombinant ADHE associates most predominantly into dimers. The native enzyme mostly occurs in multiple oligomeric forms
additional information
-
the enzyme is associated in dimers and higher order oligomers in the chloroplast. Domain structure, overview. In contrast to the native enzyme, the recombinant ADHE associates most predominantly into dimers. The native enzyme mostly occurs in multiple oligomeric forms
-
additional information
DmpFG is a microbial enzyme comprised of two subunits DmpG and DmpF
additional information
-
DmpFG is a microbial enzyme comprised of two subunits DmpG and DmpF
-
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, in the absence of cofactor or in the presence of either 5 mM NAD+ or CoA using 22% PEG 4000, 0.1 M HEPES/NaOH pH 7.5, 0.1 M sodium acetate
-
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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
-
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
-
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
-
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
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
-
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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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7
-
more stable at pH 7 than at pH 6, 8 or 9 in either Tris acetate or potassium phosphate test buffer, at the same pH more stable in Tris acetate test buffer
390174
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40
45
50
-
purified native enzyme, 30 min, complete inactivation and thermal degradation
45
-
purified native enzyme, 30 min, loss of 60% activity and partial thermal degradation
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
activity is highest in HEPES buffer and somewhat lower in phosphate buffer, activity in Tris buffer is about half the rate in HEPES buffer
-
no stabilization by detergents, acetone, ethanol, NAD+, glycerol, CoA, anaerobic conditions
-
sensitive to O2, can be protected against O2 inactivation by dithiothreitol
-
with Tris acetate buffer at pH 7, less stable at higher buffer concentration between 10 and 150 mM
-
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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-70°C, 10 mM Tris-HCl buffer, pH 8, 3 mM dithioerythritol, 2 weeks, 15% loss of activity
-
-70°C, 3 mM dithioerythritol, 85% of enzymatic activity remains after 2 weeks
-
5 mM dithiothreitol protects enzyme in crude extracts from O2-inactivation for at least 2 hours
-
addition of 140 mM KCl to 10 mM Tris acetate stabilizes as no activity is lost after 3 days
-
CoA and dithiothreitol restore a higher activity than one of these compounds alone
-
glycerol at 20%, vol/vol, stabilizes in 50 mM Tris acetate buffer at pH 7, as no activity is lost after 3 days at 4°C under argon
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ADHE cannot be solubilized from membrane with detergents such as 1% Triton X-100 or 1% sulfobetaine 3-12. The enzyme is easily dissociated from membrane by high-salt buffers containing either 1.0 M NaCl or (NH4)2SO4 without detergents
-
native enzyme from chloroplast stroma by anion exchange chromatography and affinity chromatography, followed by ultracentrifugation
native enzyme from plasma membrane by ultracentrifugation, hydroxyapatite and hydrophobic interaction chromatography, followed by ultrafiltration and gel filtration. The enzyme cannot be solubilized from membrane with detergents, either 1% Triton X-100 or 1% sulfobetaine 3-12
-
on DEAE and NAD+-linked affinity columns, combined with an ammonium sulfate fractionation step
-
partial
Q-Sepharose column chromatography, phenyl Sepharose column chromatography, and Superdex 200 gel filtration
-
recombinant N-terminally His6-tagged AdhE from Escherichia coli strain BL21 by nickel affinity chromatography and gel filtration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
expression in Pyrococcus furiosus from which the native aldehyde oxidoreductase (AOR) gene is deleted. A strain containing the Thermoanaerobacter ethanolicus AdhE in a synthetic operon with AdhA is constructed. The AdhA gene is amplified from Thermoanaerobacter sp. X514. The amino acid sequence of AdhA from Thermoanaerobacter sp. X514 is identical to that of AdhA from Thermoanaerobacter ethanolicus. Of the bacterial strains expressing the various heterologous AdhE genes, only those containing AdhE and AdhA from Thermoanaerobacter sp. produced ethanol above background. The Thermoanaerobacter ethanolicus AdhEA strain containing both AdhE and AdhA produces the most ethanol (4.2 mM), followed by Thermoanaerobacter ethanolicus AdhE strain (2.6 mM), Thermoanaerobacter ethanolicus AdhA strain (1.8 mM) and Thermoanaerobacter sp. X514 AdhE strain (1.5 mM). Ethanol and acetate are the only major carbon end-products from glucose under these conditions. For these four strains, the amount of ethanol produced per estimated glucose consumed is increased from the background level to 1.2, 1.0, 0.8 and 0.7 respectively
C7IV28
expression of the enzyme from Thermoanaerobacter sp. X514 in Pyrococcus furiosus from which the native aldehyde oxidoreductase (AOR) gene is deleted. Ethanol and acetate are the only major carbon end-products from glucose under these conditions. The amount of ethanol produced per estimated glucose consumed is increased from the background level 0.7 respectively
gene adhE, phylogenetic analysis, quantitative RT-PCR enzyme expression analysis
gene adhE, pyruvate-formate-lyase-deactivase with alcohol and acetaldehyde dehydrogenase activity
-
gene adhe, recombinant expression of N-terminally His6-tagged AdhE in Escherichia coli strain Bl21
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
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
ADHE is upregulated under oxic conditions. Upregulation is observed in cells exposed to diverse physiological stresses, including zinc deficiency, nitrogen starvation, and inhibition of carbon concentration/fixation capacity. Cells with increased ADHE abundance exhibit better survival under dark anoxia. Zinc deficiency increases ADHE accumulation and fermentative abilities. Lack of RubisCO carboxylase activity or carbonic anhydrase 3, and impaired starch synthesis also induce the enzyme
expression is strongly influenced by the pH of the culture medium. Expression in cells grown on ethanol is higher at pH 6.0 than at pH 3.7
ADHE is upregulated under oxic conditions. Upregulation is observed in cells exposed to diverse physiological stresses, including zinc deficiency, nitrogen starvation, and inhibition of carbon concentration/fixation capacity. Cells with increased ADHE abundance exhibit better survival under dark anoxia. Zinc deficiency increases ADHE accumulation and fermentative abilities. Lack of RubisCO carboxylase activity or carbonic anhydrase 3, and impaired starch synthesis also induce the enzyme
ADHE is upregulated under oxic conditions. Upregulation is observed in cells exposed to diverse physiological stresses, including zinc deficiency, nitrogen starvation, and inhibition of carbon concentration/fixation capacity. Cells with increased ADHE abundance exhibit better survival under dark anoxia. Zinc deficiency increases ADHE accumulation and fermentative abilities. Lack of RubisCO carboxylase activity or carbonic anhydrase 3, and impaired starch synthesis also induce the enzyme
-
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
biofuel production
synthesis
biofuel production
ethanol production by the hyperthermophilic archaeon Pyrococcus furiosus by expression of bacterial bifunctional alcohol dehydrogenase from Thermoanaerobacter sp. X514. Ethanol and acetate are the only major carbon end-products from glucose under these conditions. The amount of ethanol produced per estimated glucose consumed is increased from the background level 0.7 respectively. Although ethanol production from acetyl-CoA is demonstrated in Pyrococcus furiosus, the highest ethanol yield (from strain Te-AdhEA) is still lower than that of the AAA pathway in Pyrococcus furiosus, which functions via the native enzymes acetyl-CoA synthetase (ACS) and aldehyde oxidoreductase (AOR) along with heterologously expressed alcohol dehydrogenase (AdhA)
biofuel production
C7IV28
expression in Pyrococcus furiosus from which the native aldehyde oxidoreductase (AOR) gene is deleted supports ethanol production. The highest amount of ethanol (estimated 61% theoretical yield) is produced when adhE and adhA from Thermoanaerobacter are co-expressed. A strain containing the Thermoanaerobacter ethanolicus AdhE in a synthetic operon with AdhA is constructed. The AdhA gene is amplified from Thermoanaerobacter sp. X514. The amino acid sequence of AdhA from Thermoanaerobacter sp. X514 is identical to that of AdhA from Thermoanaerobacter ethanolicus. Of the bacterial strains expressing the various heterologous AdhE genes, only those containing AdhE and AdhA from Thermoanaerobacter sp. produced ethanol above background. The Thermoanaerobacter ethanolicus AdhEA strain containing both AdhE and AdhA produces the most ethanol (4.2 mM), followed by Thermoanaerobacter ethanolicus AdhE strain (2.6 mM), Thermoanaerobacter ethanolicus AdhA strain (1.8 mM) and Thermoanaerobacter sp. X514 AdhE strain (1.5 mM). Ethanol and acetate are the only major carbon end-products from glucose under these conditions. For these four strains, the amount of ethanol produced per estimated glucose consumed is increased from the background level to 1.2, 1.0, 0.8 and 0.7 respectively. Although ethanol production from acetyl-CoA is demonstrated in Pyrococcus furiosus, the highest ethanol yield (from strain Thermoanaerobacter ethanolicus AdhEA) is still lower than that of the previously reported AAA pathway in Pyrococcus furiosus, which functions via native enzymes acetyl-CoA synthetase (ACS) and aldehyde oxidoreductase (AOR) along with heterologously expressed alcohol dehydrogenase (AdhA)
biofuel production
proteome analysis as well as enzyme assays performed in cell-free extracts demonstrates that glycerol is degraded via glyceraldehyde-3-phosphate, which is further metabolized through the lower part of glycolysis leading to formation of mainly ethanol and hydrogen. Fermentation of glycerol to ethanol and hydrogen by this bacterium represents a remarkable option to add value to the biodiesel industries by utilization of surplus glycerol
biofuel production
-
expression in Pyrococcus furiosus from which the native aldehyde oxidoreductase (AOR) gene is deleted supports ethanol production. The highest amount of ethanol (estimated 61% theoretical yield) is produced when adhE and adhA from Thermoanaerobacter are co-expressed. A strain containing the Thermoanaerobacter ethanolicus AdhE in a synthetic operon with AdhA is constructed. The AdhA gene is amplified from Thermoanaerobacter sp. X514. The amino acid sequence of AdhA from Thermoanaerobacter sp. X514 is identical to that of AdhA from Thermoanaerobacter ethanolicus. Of the bacterial strains expressing the various heterologous AdhE genes, only those containing AdhE and AdhA from Thermoanaerobacter sp. produced ethanol above background. The Thermoanaerobacter ethanolicus AdhEA strain containing both AdhE and AdhA produces the most ethanol (4.2 mM), followed by Thermoanaerobacter ethanolicus AdhE strain (2.6 mM), Thermoanaerobacter ethanolicus AdhA strain (1.8 mM) and Thermoanaerobacter sp. X514 AdhE strain (1.5 mM). Ethanol and acetate are the only major carbon end-products from glucose under these conditions. For these four strains, the amount of ethanol produced per estimated glucose consumed is increased from the background level to 1.2, 1.0, 0.8 and 0.7 respectively. Although ethanol production from acetyl-CoA is demonstrated in Pyrococcus furiosus, the highest ethanol yield (from strain Thermoanaerobacter ethanolicus AdhEA) is still lower than that of the previously reported AAA pathway in Pyrococcus furiosus, which functions via native enzymes acetyl-CoA synthetase (ACS) and aldehyde oxidoreductase (AOR) along with heterologously expressed alcohol dehydrogenase (AdhA)
-
synthesis
-
50 microg of alcohol dehydrogenase AdhA, EC 1.1.1.2, and 50 microg actaldehyde dehydrogenase AldH, EC 1.2.1.10, in buffer solution (pH 8.0) containing NADPH, NADH and acetyl-CoA at 60°C, produce 1.6 mM ethanol from 3 mM acetyl-CoA after 90 min
synthesis
construction of a bypassed pyruvate decarboxylation pathway, through which pyruvate can be converted to acetyl-CoA, by using a coupled enzyme system consisting of pyruvate decarboxylase from Acetobacter pasteurianus and the CoA-acylating aldehyde dehydrogenase from Thermus thermophilus. A cofactor-balanced and CoA-recycling synthetic pathway for N-acetylglutamate production is designed by coupling the bypassed pathway with the glutamate dehydrogenase from Thermus thermophilus and N-acetylglutamate synthase from Thermotoga maritima. N-Acetylglutamate can be produced from an equimolar mixture of pyruvate and alpha-ketoglutarate with a molar yield of 55% through the synthetic pathway consisting of a mixture of four recombinant Escherichia coli strains having either one of the thermostable enzymes. The overall recycling number of CoA is 27
synthesis
synthetic pathway for n-butanol production from acetyl coenzyme at 70°C, using beta-ketothiolase Thl, 3-hydroxybutyryl-CoA dehydrogenase Hbd, and 3-hydroxybutyryl-CoA dehydratase Crt from Caldanaerobacter subterraneus subsp. tengcongensis, trans-2-enoyl-CoA reductase Ter from Spirochaeta thermophila and bifunctional aldehyde dehydrogenase AdhE and and butanol dehydrogenase in vitro. n-Butanol is produced at 70°C, but with different amounts of ethanol as a coproduct, because of the broad substrate specificities of AdhE, Bad, and Bdh. A reaction kinetics model, validated via comparison to in vitro experiments, is used to determine relative enzyme ratios needed to maximize n-butanol production. By using large relative amounts of Thl and Hbd and small amounts of Bad and Bdh, >70% conversion to n-butanol is observed in vitro, but with a 60% decrease in the predicted pathway flux
synthesis
synthetic pathway for n-butanol production from acetyl-CoA at 70°C, using beta-ketothiolase Thl, 3-hydroxybutyryl-CoA dehydrogenase Hbd, and 3-hydroxybutyryl-CoA dehydratase Crt from Caldanaerobacter subterraneus subsp. tengcongensis, trans-2-enoyl-CoA reductase Ter from Spirochaeta thermophila and bifunctional aldehyde dehydrogenase AdhE and and butanol dehydrogenase in vitro. n-Butanol is produced at 70°C, but with different amounts of ethanol as a coproduct, because of the broad substrate specificities of AdhE, Bad, and Bdh. A reaction kinetics model, validated via comparison to in vitro experiments, is used to determine relative enzyme ratios needed to maximize n-butanol production. By using large relative amounts of Thl and Hbd and small amounts of Bad and Bdh, >70% conversion to n-butanol is observed in vitro, but with a 60% decrease in the predicted pathway flux
synthesis
-
construction of a bypassed pyruvate decarboxylation pathway, through which pyruvate can be converted to acetyl-CoA, by using a coupled enzyme system consisting of pyruvate decarboxylase from Acetobacter pasteurianus and the CoA-acylating aldehyde dehydrogenase from Thermus thermophilus. A cofactor-balanced and CoA-recycling synthetic pathway for N-acetylglutamate production is designed by coupling the bypassed pathway with the glutamate dehydrogenase from Thermus thermophilus and N-acetylglutamate synthase from Thermotoga maritima. N-Acetylglutamate can be produced from an equimolar mixture of pyruvate and alpha-ketoglutarate with a molar yield of 55% through the synthetic pathway consisting of a mixture of four recombinant Escherichia coli strains having either one of the thermostable enzymes. The overall recycling number of CoA is 27
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YEAR
ORGANISM (UNIPROT)
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Clostridium beijerinckii, Clostridium beijerinckii NRRL B592
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Pseudomonas sp., Pseudomonas sp. CF 600
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Clostridium kluyveri
brenda
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brenda
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Escherichia coli, Escherichia coli XL2-Blue
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Paraburkholderia xenovorans (Q79AF6)
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Escherichia coli
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Tsuji, K.; Yoon, K.S.; Ogo, S.
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10
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Thermoanaerobacter ethanolicus (C7IV28), Thermoanaerobacter ethanolicus JW200 (C7IV28), Thermoanaerobacter sp. X514 (B0K4A2)
brenda
Atteia, A.; van Lis, R.; Mendoza-Hernández, G.; Henze, K.; Martin, W.; Riveros-Rosas, H.; González-Halphen, D.
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53
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Polytomella sp. Pringsheim 198.80 (Q70YJ9)
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Aeromonas hydrophila
-
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Tsuji, K.; Yoon, K.S.; Ogo, S.
Biochemical characterization of a bifunctional acetaldehyde-alcohol dehydrogenase purified from a facultative anaerobic bacterium Citrobacter sp. S-77
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121
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Citrobacter sp. S-77
brenda
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10
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brenda
Van Lis, R.; Popek, M.; Coute, Y.; Kosta, A.; Drapier, D.; Nitschke, W.; Atteia, A.
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Chlamydomonas reinhardtii (Q1RS84), Chlamydomonas reinhardtii CC-124 (Q1RS84)
brenda
Pony, P.; Rapisarda, C.; Terradot, L.; Marza, E.; Fronzes, R.
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11
1426
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Escherichia coli (P0A9Q7)
brenda
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