Information on EC 1.2.1.10 - acetaldehyde dehydrogenase (acetylating)

Word Map on EC 1.2.1.10
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY hide
1.2.1.10
-
RECOMMENDED NAME
GeneOntology No.
acetaldehyde dehydrogenase (acetylating)
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
acetaldehyde + CoA + NAD+ = acetyl-CoA + NADH + H+
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
2'-deoxy-alpha-D-ribose 1-phosphate degradation
-
-
2-aminoethylphosphonate degradation I
-
-
2-oxopentenoate degradation
-
-
acetylene degradation
-
-
ethanol degradation I
-
-
heterolactic fermentation
-
-
L-threonine degradation IV
-
-
mixed acid fermentation
-
-
pyruvate fermentation to ethanol I
-
-
pyruvate fermentation to ethanol III
-
-
superpathway of fermentation (Chlamydomonas reinhardtii)
-
-
triethylamine degradation
-
-
3-phenylpropionate degradation
-
-
ethanol fermentation
-
-
threonine metabolism
-
-
Phenylalanine metabolism
-
-
Benzoate degradation
-
-
Pyruvate metabolism
-
-
Dioxin degradation
-
-
Xylene degradation
-
-
Butanoate metabolism
-
-
Metabolic pathways
-
-
Microbial metabolism in diverse environments
-
-
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].
CAS REGISTRY NUMBER
COMMENTARY hide
9028-91-5
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain NRRL B592
-
-
Manually annotated by BRENDA team
strain NRRL B592
-
-
Manually annotated by BRENDA team
strain XL2-Blue
-
-
Manually annotated by BRENDA team
srain WB
-
-
Manually annotated by BRENDA team
srain WB
-
-
Manually annotated by BRENDA team
strain LMC7
SwissProt
Manually annotated by BRENDA team
Moorella sp.
-
-
-
Manually annotated by BRENDA team
strain NCIMB9816
-
-
Manually annotated by BRENDA team
strain 39E
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH
show the reaction diagram
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH + H+
show the reaction diagram
acetaldehyde + CoA + NAD+ + H+
acetyl-CoA + NADH
show the reaction diagram
acetaldehyde + NAD+ + CoA
acetyl-CoA + NADH + H+
show the reaction diagram
Moorella sp.
-
-
-
-
r
acetaldehyde + NADP+ + CoA
acetyl-CoA + NADPH + H+
show the reaction diagram
Moorella sp.
-
-
-
-
r
acetyl-CoA + NADH
acetaldehyde + CoA + NAD+
show the reaction diagram
-
-
-
-
r
acetyl-CoA + NADH + H+
acetaldehyde + CoA + NAD+
show the reaction diagram
acetyl-CoA + NADH + H+
acetaldehyde + NAD+ + CoA
show the reaction diagram
Moorella sp.
-
-
-
-
r
acetyl-CoA + NADPH + H+
acetaldehyde + CoA + NADP+
show the reaction diagram
acetyl-CoA + NADPH + H+
acetaldehyde + NADP+ + CoA
show the reaction diagram
Moorella sp.
-
-
-
-
r
butyraldehyde + CoA + NAD+
butyryl-CoA + NADH + H+
show the reaction diagram
butyryl-CoA + NADH + H+
butyraldehyde + CoA + NAD+
show the reaction diagram
-
-
-
r
caprylaldehyde + CoA + NAD+
caprylyl-CoA + NADH
show the reaction diagram
-
-
-
-
?
formaldehyde + CoA + NAD+
formyl-CoA + NADH
show the reaction diagram
formaldehyde + CoA + NAD+
formyl-CoA + NADH + H+
show the reaction diagram
-
-
-
?
glutaraldehyde + CoA + NAD+
glutaryl-CoA + NADH
show the reaction diagram
-
-
-
-
?
glycolaldehyde + CoA + NAD+
hydroxyacetyl-CoA + NADH
show the reaction diagram
-
-
-
-
?
glyoxal + CoA + NAD+
glyoxyl-CoA + NADH
show the reaction diagram
-
-
-
-
?
heptylaldehyde + CoA + NAD+
heptanoyl-CoA + NADH
show the reaction diagram
hexylaldehyde + CoA + NAD+
hexanoyl-CoA + NADH
show the reaction diagram
isobutyraldehyde + CoA + NAD+
isobutyryl-CoA + NADH
show the reaction diagram
n-butyraldehyde + CoA + NAD+
n-butyryl-CoA + NADH
show the reaction diagram
pentaldehyde + CoA + NAD+
pentyl-CoA + NADH + H+
show the reaction diagram
-
-
-
r
picolinaldehyde + CoA + NAD+
picolinyl-CoA + NADH + H+
show the reaction diagram
-
-
-
r
propanal + CoA + NAD+
propionyl-CoA + NADH
show the reaction diagram
propionaldehyde + CoA + NAD+
propionyl-CoA + NADH + H+
show the reaction diagram
valeraldehyde + CoA + NAD+
valeryl-CoA + NADH
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH
show the reaction diagram
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH + H+
show the reaction diagram
formaldehyde + CoA + NAD+
formyl-CoA + NADH + H+
show the reaction diagram
A5JT11
-
-
-
?
propanal + CoA + NAD+
propionyl-CoA + NADH
show the reaction diagram
propionaldehyde + CoA + NAD+
propionyl-CoA + NADH + H+
show the reaction diagram
A5JT11
-
-
-
?
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADPH
additional information
-
enzyme is able to acetylate other thiols than CoA, e.g. pantetheine, 2-mercaptoethanol, dithioerythritol, glutathione, cysteamine
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Fe2+
-
3fold activation with 0.00003 mM, 5fold activation with 0.03 mM, activation only of NADH oxidation, not NAD+ reduction
Mn2+
activity of the enzyme is elevated
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
acetaldehyde
-
competitive inhibition
acetyl-CoA
-
competitive inhibitor with respect to NAD+; competitive to NAD+
ADP
-
1 mM 42% inhibition, competitive to NAD+
ADP-ribose
-
-
AgNO3
-
1 mM 20% inhibition
ATP
-
1 mM 38% inhibition, competitive to NAD+
benzaldehyde
-
-
Ca2+
-
5 mM causes 51% inhibition
Chloroethanol
-
-
CuSO4
-
1 mM 49% inhibition
Disulfiram
-
0.01 mM causes 70% inhibition
HgCl2
-
1 mM 31% inhibition
iodoacetamide
-
1 mM causes 88-96% inhibition
iodoacetate
-
-
Mg2+
-
5 mM causes 51% inhibition
Mn2+
-
5 mM causes 84% inhibition
Na2HAsO4
-
1 mM 100% inhibition, 0.1 mM 32% inhibition
NAD+
-
double competitive, NAD+/CoA ratio is kept at 1:0.24
NADH
-
competitive inhibitor with respect to CoA; competitive to CoA
p-chloromercuribenzoate
-
0.01 mM causes 88-96% inhibition
Tris
-
rate of reaction falls off rapidly in Tris
Valproate
-
50 mM causes 20-46% inhibition
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
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-mercaptoethanol
3-pyridinecarboxaldehyde adenine dinucleotide
-
NAD+ analogue, activates by binding strongly to activator site, binds weakly to catalytic site
dithiothreitol
-
does require dithiothreitol for optimum activity
GSH
-
7fold activation
NAD+
-
reduces lag phase before attainment of steady state rate in conjunction with 2-mercaptoethanol
sulfhydryl compound
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
22
2-mercaptoethanol
-
-
0.01518 - 133
acetaldehyde
0.007 - 1.6
acetyl-CoA
2.3 - 11
Butanal
3.23 - 31.7
Butyraldehyde
0.0057 - 0.0272
Butyryl-CoA
0.008 - 0.16
CoA
0.00212
formaldehyde
-
20
glycolaldehyde
-
-
0.029 - 0.166
n-Butyryl-CoA
0.05 - 0.44
NAD+
0.0076 - 0.1
NADH
0.0673 - 0.206
NADPH
11
pantetheine
-
-
8.2
pentaldehyde
mutant enzyme I195A, at 25C in 100 mM HEPES buffer (pH 8.0)
3.2 - 18.2
picolinaldehyde
0.603 - 6.9
propanal
0.00049 - 79.5
propionaldehyde
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
6.9 - 37.9
acetaldehyde
7.1 - 16.7
Butyraldehyde
13
pentaldehyde
Paraburkholderia xenovorans
Q79AF6
mutant enzyme I195A, at 25C in 100 mM HEPES buffer (pH 8.0)
1.9 - 3.2
picolinaldehyde
3.4 - 24.9
propionaldehyde
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.147 - 2.224
acetaldehyde
90
55.3 - 381
acetyl-CoA
29
0.0433 - 7.11
Butyraldehyde
499
394 - 833
Butyryl-CoA
270
0.0265 - 1.584
pentaldehyde
3401
0.00011 - 0.597
picolinaldehyde
7490
0.0425 - 1.219
propionaldehyde
273
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
265
acetaldehyde
-
at 25C in 50 mM Tris/HCl buffer, pH 8.0
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.04
gene AdhE deletion mutant, cosubstrate NADH, pH 7.0, 55C
0.05
wild-type, cosubstrate NADPH, pH 7.0, 55C
0.09
gene AdhE deletion mutant, cosubstrate NADH, pH 7.0, 55C; gene AdhE deletion mutant, cosubstrate NADPH, pH 7.0, 55C; wild-type, cosubstrate NADH, pH 7.0, 55C
0.1
gene AdhE deletion mutant, cosubstrate NADPH, pH 7.0, 55C
0.16
wild-type, cosubstrate NADPH, pH 7.0, 55C
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
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
2.18
wild-type, cosubstrate NADH, pH 7.0, 55C
2.8
Moorella sp.
-
cleavage of thioester, cofactor NADPH, pH 8.0, 60C
3.7
Moorella sp.
-
condensation of thioester, cofactor NADP+, pH 10.0, 60C
4.88
-
undialyzed, anaerobically purified
8.75
-
bifunctional fusion protein of aldehyde and alcohol dehydrogenase
9.62
-
dialyzed, incubated with dithiothreitol and CoA
18.8
Moorella sp.
-
cleavage of thioester, cofactor NADH, pH 8.0, 60C
29.9
Moorella sp.
-
condensation of thioester, cofactor NAD+, pH 10.0, 60C
60.6
recombinant enzyme
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.8
-
NADH oxidation; NADH oxidation, with potassium phosphate buffer
8.8
-
in cyclohexylaminoethanesulfonic acid or Tris-(hydroxymethyl)-methyl-amino-propanesulfonic acid buffer
9
-
NAD+ reduction
9.1
-
NAD+ reduction
10
Moorella sp.
-
condensation of thiopester
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 8
-
less than 50% of maximal activity above and below
6 - 7
-
NAD+ reduction
6.2 - 7.4
-
67% of maximal activity at pH 6.2, 79% of maximal activity at pH 7.4
6.5 - 9.5
-
activity of NADH oxidation increases between 6.5-9.5
6.5 - 8.5
-
activity increases gradually over pH range from 6.5 to 8.5
7 - 9.5
-
30% of maximal activity at pH 7.0, 100% at pH 9.5
8.5 - 10
-
70% of maximal activity at pH 8.5, 80% of maximal activity at pH 10
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60
Moorella sp.
-
at pH 8.0
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 60
-
55% of maximal activity at 20C, 60% at 60C
50
Moorella sp.
-
71% of maximum activity
70
Moorella sp.
-
52% of maximum activity
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Clostridium phytofermentans (strain ATCC 700394 / DSM 18823 / ISDg)
Geobacillus thermoglucosidasius (strain C56-YS93)
Geobacillus thermoglucosidasius (strain C56-YS93)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35300
-
gel filtration
96600
deduced from sequence
100000
-
gel filtration under anaerobic conditions
120000
-
one of four isozymes, gel filtration
140000
-
-
148000
-
gel filtration, molecular mass of enzyme complex, occurs in complex with 4-hydroxy-2-ketovalerate
188000
-
gel filtration
265000
gel filtration
290000
-
gel filtration and sedimentation coefficient
360000
-
gel filtration
370000
-
one of four isozymes, gel filtration
520000
-
one of four isozymes, gel filtration
555000
gel filtration
900000
-
one of four isozymes, gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexamer
6 * 97700, calculated, 6 * 94900, SDS-PAGE
monomer
-
1 * 33344, electrospray ionization mass spectrometry
pentamer
5 * 51700, calculated, 5 * 52400, SDS-PAGE
polymer
-
ca. 40 * 96000, pyruvate-formate-lyase-deactivase with alcohol and aldehyde dehydrogenase activity, nucleotide sequence
tetramer
additional information
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
-
hanging drop method, streak-seeding
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 8
-
enzyme activity falls to 50% at pH 5 and pH 8
390176
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
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40
-
15 min, 30% activity left
45
-
15 min, inactivation
70
-
3 min, inactivation above
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
-
dithioerythritol stabilizes
-
extremely unstable in absence of 2-mercaptoethanol
-
labile during purification, stabilization by 2-hydroxyethyldisulfide
-
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
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-60C, 20 mM MOPS-KOH pH 7.6, 0.1 mM EDTA, up to one year
-
-70C, 10 mM Tris-HCl buffer, pH 8, 3 mM dithioerythritol, 2 weeks, 15% loss of activity
-
-70C, 3 mM dithioerythritol, 85% of enzymatic activity remains after 2 weeks
-
-80C, 10 mM phosphate buffer, pH 7.5, 1 mM dithiothreitol
-
3C, ammonium sulfate step of purification, several months
-
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 4C under argon
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
by affinity chromatography by means of a Ni-Sepharose column
from anaerobically grown cells, rod-shaped
-
Ni-NTA column chromatography
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
-
under anaerobic conditions
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Escherichia coli strain W1485
-
expressed in Escherichia coli C41 (DE3) cells
-
expression in Escherichia coli
expression in Escherichia coli BL21 and DH5alpha
expression in Escherichia coli; expression in Escherichia coli
gene adhE, pyruvate-formate-lyase-deactivase with alcohol and acetaldehyde dehydrogenase activity
-
in Escherichia coli BL21 cells
overexpression in Escherichia coli
-
pT7.5-dmpFG plasmid expressed in Escherichia coli C41(DE3)
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
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
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis
Show AA Sequence (2688 entries)
Please use the Sequence Search for a certain query.