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acetaldehyde + 2-mercaptoethanol + NAD+
S-acetyl-2-mercaptoethanol + NADH + H+
-
14% activity compared to CoA
-
-
r
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH + H+
acetaldehyde + CoA + NAD+ + H+
acetyl-CoA + NADH
acetaldehyde + CoA + NADP+
acetyl-CoA + NADPH + H+
-
low activity with NADP+ compared to NAD+
-
-
r
acetaldehyde + NAD+
acetate + NADH + H+
-
-
-
-
?
acetaldehyde + NAD+ + CoA
acetyl-CoA + NADH + H+
-
-
-
-
r
acetaldehyde + NADP+ + CoA
acetyl-CoA + NADPH + H+
-
-
-
-
r
acetaldehyde + pantetheine + NAD+
S-acetyl-pantetheine + NADH + H+
-
46% activity compared to CoA
-
-
r
acetyl-CoA + NADH
acetaldehyde + CoA + NAD+
-
-
-
-
r
acetyl-CoA + NADH + H+
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH + H+
acetaldehyde + NAD+ + CoA
acetyl-CoA + NADPH + H+
acetaldehyde + CoA + NADP+
acetyl-CoA + NADPH + H+
acetaldehyde + NADP+ + CoA
-
-
-
-
r
butanoyl-CoA + NADH + H+
butanal + CoA + NAD+
-
-
-
-
?, r
butyraldehyde + CoA + NAD+
butanoyl-CoA + NADH
-
21% of the activity with acetaldehyde
-
-
?
butyraldehyde + CoA + NAD+
butyryl-CoA + NADH + H+
butyryl-CoA + NADH + H+
butyraldehyde + CoA + NAD+
-
-
-
r
butyryl-CoA + NADPH + H+
butyraldehyde + CoA + NADP+
caprylaldehyde + CoA + NAD+
caprylyl-CoA + NADH
-
-
-
-
?
formaldehyde + CoA + NAD+
formyl-CoA + NADH
formaldehyde + CoA + NAD+
formyl-CoA + NADH + H+
-
-
-
?
glutaraldehyde + CoA + NAD+
glutaryl-CoA + NADH
-
-
-
-
?
glycolaldehyde + CoA + NAD+
hydroxyacetyl-CoA + NADH
-
-
-
-
?
glyoxal + CoA + NAD+
glyoxyl-CoA + NADH
-
-
-
-
?
heptylaldehyde + CoA + NAD+
heptanoyl-CoA + NADH
hexylaldehyde + CoA + NAD+
hexanoyl-CoA + NADH
isobutyraldehyde + CoA + NAD+
isobutyryl-CoA + NADH
n-butyraldehyde + CoA + NAD+
n-butyryl-CoA + NADH
pentaldehyde + CoA + NAD+
pentyl-CoA + NADH + H+
-
-
-
r
picolinaldehyde + CoA + NAD+
picolinyl-CoA + NADH + H+
-
-
-
r
propanal + CoA + NAD+
propionyl-CoA + NADH
propanoyl-CoA + NADH + H+
propanal + CoA + NAD+
-
-
-
-
r
propionaldehyde + CoA + NAD+
propanoyl-CoA + NADH
-
51.8% of the activity with acetaldehyde
-
-
?
propionaldehyde + CoA + NAD+
propionyl-CoA + NADH + H+
valeraldehyde + CoA + NAD+
valeryl-CoA + NADH
valerylaldehyde + CoA + NAD+
valeryl-CoA + NADH + H+
-
5.6% activity compared to acetaldehyde
-
-
r
additional information
?
-
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH
-
-
-
-
?
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH
-
-
-
r
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH
-
-
-
r
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH
-
-
-
?
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH
-
-
-
?
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH
-
-
-
?
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
-
-
-
?
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH
-
-
-
?
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH
-
-
-
?
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH
-
-
-
?
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH
-
-
-
r
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH
-
-
-
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
-
-
-
?
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH
-
during glucose fermentation
-
r
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH
-
-
-
r
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH
-
enzyme carries aldehyde and alcohol dehydrogenase activity
-
r
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH
-
-
-
r
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH
-
enzyme carries aldehyde and alcohol dehydrogenase activity
-
r
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH
-
-
-
r
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH
-
-
-
r
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH
-
ethanol production in aerobic glucose dissimilation
-
r
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH
-
-
-
r
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH
-
-
-
?
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH
-
-
-
?
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH
-
-
-
-
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
-
-
-
?
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH
-
-
-
-
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
-
-
-
r
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH + H+
-
-
-
r
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH + H+
-
-
-
-
?
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH + H+
-
best substrates
-
-
r
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH + H+
-
-
-
-
?
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH + H+
-
-
-
?, r
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH + H+
-
-
-
r
acetaldehyde + CoA + NAD+ + H+
acetyl-CoA + NADH
-
-
-
-
?
acetaldehyde + CoA + NAD+ + H+
acetyl-CoA + NADH
-
-
-
-
?
acetyl-CoA + NADH + H+
acetaldehyde + CoA + NAD+
-
-
-
?
acetyl-CoA + NADH + H+
acetaldehyde + CoA + NAD+
-
-
-
-
?
acetyl-CoA + NADH + H+
acetaldehyde + CoA + NAD+
-
best substrate
-
-
r
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+
-
-
-
r
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
-
-
-
-
r
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+
-
-
-
-
?
acetyl-CoA + NADPH + H+
acetaldehyde + CoA + NADP+
-
-
-
-
r
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
butyryl-CoA + NADPH + H+
butyraldehyde + CoA + NADP+
-
-
-
-
r
formaldehyde + CoA + NAD+
formyl-CoA + NADH
-
-
-
-
ir
formaldehyde + CoA + NAD+
formyl-CoA + NADH
-
-
-
-
?
formaldehyde + CoA + NAD+
formyl-CoA + NADH
-
-
-
-
?
heptylaldehyde + CoA + NAD+
heptanoyl-CoA + NADH
-
-
-
-
?
heptylaldehyde + CoA + NAD+
heptanoyl-CoA + NADH
-
-
-
-
?
hexylaldehyde + CoA + NAD+
hexanoyl-CoA + NADH
-
-
-
-
?
hexylaldehyde + CoA + NAD+
hexanoyl-CoA + NADH
-
-
-
-
?
isobutyraldehyde + CoA + NAD+
isobutyryl-CoA + NADH
-
-
-
r
isobutyraldehyde + CoA + NAD+
isobutyryl-CoA + NADH
-
-
-
r
isobutyraldehyde + CoA + NAD+
isobutyryl-CoA + NADH
-
-
-
-
?
isobutyraldehyde + CoA + NAD+
isobutyryl-CoA + NADH
-
-
-
-
?
isobutyraldehyde + CoA + NAD+
isobutyryl-CoA + NADH
-
-
-
-
?
isobutyraldehyde + CoA + NAD+
isobutyryl-CoA + NADH
-
-
-
-
?
n-butyraldehyde + CoA + NAD+
n-butyryl-CoA + NADH
-
-
-
-
r
n-butyraldehyde + CoA + NAD+
n-butyryl-CoA + NADH
-
-
-
-
r
n-butyraldehyde + CoA + NAD+
n-butyryl-CoA + NADH
-
-
-
-
r
n-butyraldehyde + CoA + NAD+
n-butyryl-CoA + NADH
-
-
-
-
r
n-butyraldehyde + CoA + NAD+
n-butyryl-CoA + NADH
-
-
-
?
n-butyraldehyde + CoA + NAD+
n-butyryl-CoA + NADH
-
-
-
?
n-butyraldehyde + CoA + NAD+
n-butyryl-CoA + NADH
-
-
-
-
r
n-butyraldehyde + CoA + NAD+
n-butyryl-CoA + NADH
-
-
-
-
r
n-butyraldehyde + CoA + NAD+
n-butyryl-CoA + NADH
-
-
-
-
?
n-butyraldehyde + CoA + NAD+
n-butyryl-CoA + NADH
-
-
-
-
?
n-butyraldehyde + CoA + NAD+
n-butyryl-CoA + NADH
-
-
-
r
propanal + CoA + NAD+
propionyl-CoA + NADH
-
-
-
-
?
propanal + CoA + NAD+
propionyl-CoA + NADH
-
-
-
-
?
propanal + CoA + NAD+
propionyl-CoA + NADH
-
is used 63% as efficiently as acetaldehyde
-
r
propanal + CoA + NAD+
propionyl-CoA + NADH
-
is used 63% as efficiently as acetaldehyde
-
r
propanal + CoA + NAD+
propionyl-CoA + NADH
-
-
-
-
?
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
-
-
?
valeraldehyde + CoA + NAD+
valeryl-CoA + NADH
-
-
-
-
?
valeraldehyde + CoA + NAD+
valeryl-CoA + NADH
-
-
-
-
?
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 benzaldehyde
-
-
?
additional information
?
-
-
not 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
?
-
-
not benzaldehyde
-
-
?
additional information
?
-
-
not: benzaldehyde
-
-
?
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
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH + H+
acetyl-CoA + NADH + H+
acetaldehyde + CoA + NAD+
butanoyl-CoA + NADH + H+
butanal + CoA + NAD+
-
-
-
-
r
formaldehyde + CoA + NAD+
formyl-CoA + NADH + H+
-
-
-
?
propanal + CoA + NAD+
propionyl-CoA + NADH
propanoyl-CoA + NADH + H+
propanal + CoA + NAD+
-
-
-
-
r
propionaldehyde + CoA + NAD+
propionyl-CoA + NADH + H+
-
-
-
?
additional information
?
-
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH
-
-
-
r
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH
-
-
-
r
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH
-
-
-
?
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH
-
-
-
?
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
-
-
-
?
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH
-
-
-
?
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH
-
-
-
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
-
during glucose fermentation
-
r
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH
-
-
-
r
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH
-
-
-
r
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH
-
ethanol production in aerobic glucose dissimilation
-
r
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH
-
-
-
?
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH
-
-
-
?
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH
-
involved in degradation of toxic aromatic compounds via the intermediate catechol
-
-
r
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH
-
-
-
?
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH
-
involved in degradation of toxic aromatic compounds via the intermediate catechol
-
-
r
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH
-
-
-
r
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH + H+
-
-
-
r
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH + H+
-
-
-
-
?
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH + H+
-
-
-
-
?
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH + H+
-
-
-
?
acetyl-CoA + NADH + H+
acetaldehyde + CoA + NAD+
-
best substrate
-
-
r
acetyl-CoA + NADH + H+
acetaldehyde + CoA + NAD+
-
-
-
r
acetyl-CoA + NADH + H+
acetaldehyde + CoA + NAD+
-
-
-
r
propanal + CoA + NAD+
propionyl-CoA + NADH
-
is used 63% as efficiently as acetaldehyde
-
r
propanal + CoA + NAD+
propionyl-CoA + NADH
-
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
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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malfunction
cells with increased ADHE abundance exhibit better survival under dark anoxia
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
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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
-
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
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additional information
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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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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)
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synthesis
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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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