Information on EC 1.2.1.10 - acetaldehyde dehydrogenase (acetylating)

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Mark a special word or phrase in this record:
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
1.2.1.10
-
RECOMMENDED NAME
GeneOntology No.
acetaldehyde dehydrogenase (acetylating)
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
oxidation
-
-
-
-
oxidation
A5JT11
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
2'-deoxy-alpha-D-ribose 1-phosphate degradation
-
2-aminoethylphosphonate degradation I
-
2-oxopentenoate degradation
-
acetylene degradation
-
Benzoate degradation
-
Butanoate metabolism
-
Dioxin degradation
-
ethanol degradation I
-
heterolactic fermentation
-
Metabolic pathways
-
Microbial metabolism in diverse environments
-
mixed acid fermentation
-
pyruvate fermentation to ethanol I
-
pyruvate fermentation to ethanol III
-
Pyruvate metabolism
-
superpathway of fermentation (Chlamydomonas reinhardtii)
-
threonine degradation IV
-
triethylamine degradation
-
Xylene degradation
-
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].
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4-hydroxy-2-ketovalerate aldolase/acylating acetaldehyde dehydrogenase
-
bifunctional enzyme
4-hydroxy-2-ketovalerate aldolase/acylating acetaldehyde dehydrogenase
-
bifunctional enzyme
-
ACDH
-
-
-
-
acetaldehyde dehydrogenase
A5JT11
-
acetaldehyde dehydrogenase
Q5RLY6
acetaldehyde dehydrogenase from Leuconostoc mesenteroides is a bifunctional enzyme possessing alcohol dehydrogenase und acetaldehyde dehydrogenase domains
acetaldehyde dehydrogenase
Leuconostoc mesenteroides LMC7
Q5RLY6
acetaldehyde dehydrogenase from Leuconostoc mesenteroides is a bifunctional enzyme possessing alcohol dehydrogenase und acetaldehyde dehydrogenase domains
-
Acetaldehyde dehydrogenase [acetylating]
-
-
-
-
acetyl-CoA reductase
-
-
-
-
acylating acetaldehyde dehydrogenase
-
-
AdhE
Leuconostoc mesenteroides LMC7
Q5RLY6
-
-
aldehyde dehydrogenase
A5JT11
-
aldehyde dehydrogenase (acylating)
-
-
-
-
CoA-dependent aldehyde dehydrogenase
-
-
-
-
coenzyme A linked aldehyde dehydrogenase
-
-
-
-
DmpF
Escherichia coli XL2-Blue
-
-
-
NAD+/CoA-dependent aldehyde dehydrogenase
-
-
NAD+/CoA-dependent aldehyde dehydrogenase
Escherichia coli XL2-Blue
-
-
-
nonphosphorylating acylating aldehyde dehydrogenase
Q79AF6
-
CAS REGISTRY NUMBER
COMMENTARY
9028-91-5
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
strain NRRL B592
-
-
Manually annotated by BRENDA team
Clostridium beijerinckii NRRL B592
strain NRRL B592
-
-
Manually annotated by BRENDA team
grown anaerobically
-
-
Manually annotated by BRENDA team
NCIB 8114
-
-
Manually annotated by BRENDA team
strain B
-
-
Manually annotated by BRENDA team
strain K-12 strain DC272
-
-
Manually annotated by BRENDA team
strain XL2-Blue
-
-
Manually annotated by BRENDA team
Escherichia coli XL2-Blue
strain XL2-Blue
-
-
Manually annotated by BRENDA team
Giardia intestinalis WB
srain WB
-
-
Manually annotated by BRENDA team
strain LMC7
SwissProt
Manually annotated by BRENDA team
Leuconostoc mesenteroides LMC7
strain LMC7
SwissProt
Manually annotated by BRENDA team
strain NCIMB9816
-
-
Manually annotated by BRENDA team
Pseudomonas sp. NCIMB9816
strain NCIMB9816
-
-
Manually annotated by BRENDA team
Thermoanaerobacter ethanolicus 39E
strain 39E
-
-
Manually annotated by BRENDA team
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Fe2+
-
3fold activation with 0.00003 mM, 5fold activation with 0.03 mM, activation only of NADH oxidation, not NAD+ reduction
Mn2+
A5JT11
activity of the enzyme is elevated
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2-mercaptoethanol
-
reduces lag phase before attainment of steady state rate in conjunction with NAD+
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
-
requirement for reduced form
sulfhydryl compound
-
requirement for reduced form
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
6.9
-
acetaldehyde
Q79AF6
mutant enzyme I195W, at 25C in 100 mM HEPES buffer (pH 8.0)
7.6
-
acetaldehyde
Q79AF6
mutant enzyme D208A, at 25C in 100 mM HEPES buffer (pH 8.0)
7.8
-
acetaldehyde
Q79AF6
mutant enzyme I171F, at 25C in 100 mM HEPES buffer (pH 8.0)
15.4
-
acetaldehyde
Q79AF6
mutant enzyme I195F, at 25C in 100 mM HEPES buffer (pH 8.0)
15.7
-
acetaldehyde
-
at 25C in 50 mM Tris/HCl buffer, pH 8.0
17.2
-
acetaldehyde
Q79AF6
wild type enzyme, at 25C in 100 mM HEPES buffer (pH 8.0)
19.7
-
acetaldehyde
Q79AF6
mutant enzyme I195A, at 25C in 100 mM HEPES buffer (pH 8.0)
37.9
-
acetaldehyde
Q79AF6
mutant enzyme I171A, at 25C in 100 mM HEPES buffer (pH 8.0)
7.1
-
Butyraldehyde
Q79AF6
mutant enzyme I171F, at 25C in 100 mM HEPES buffer (pH 8.0)
9.5
-
Butyraldehyde
Q79AF6
wild type enzyme, at 25C in 100 mM HEPES buffer (pH 8.0)
12.6
-
Butyraldehyde
Q79AF6
mutant enzyme I195A, at 25C in 100 mM HEPES buffer (pH 8.0)
16.7
-
Butyraldehyde
Q79AF6
mutant enzyme I171A, at 25C in 100 mM HEPES buffer (pH 8.0)
13
-
pentaldehyde
Q79AF6
mutant enzyme I195A, at 25C in 100 mM HEPES buffer (pH 8.0)
1.9
-
picolinaldehyde
Q79AF6
mutant enzyme I171A, at 25C in 100 mM HEPES buffer (pH 8.0)
2.4
-
picolinaldehyde
Q79AF6
mutant enzyme I171F, at 25C in 100 mM HEPES buffer (pH 8.0)
2.8
-
picolinaldehyde
Q79AF6
wild type enzyme, at 25C in 100 mM HEPES buffer (pH 8.0)
3.2
-
picolinaldehyde
Q79AF6
mutant enzyme I195A, at 25C in 100 mM HEPES buffer (pH 8.0)
3.4
-
propionaldehyde
Q79AF6
mutant enzyme I195W, at 25C in 100 mM HEPES buffer (pH 8.0)
6
-
propionaldehyde
Q79AF6
mutant enzyme I171F, at 25C in 100 mM HEPES buffer (pH 8.0)
7.6
-
propionaldehyde
Q79AF6
mutant enzyme I195F, at 25C in 100 mM HEPES buffer (pH 8.0)
12.1
-
propionaldehyde
Q79AF6
mutant enzyme I195A, at 25C in 100 mM HEPES buffer (pH 8.0)
16.3
-
propionaldehyde
Q79AF6
wild type enzyme, at 25C in 100 mM HEPES buffer (pH 8.0)
24.9
-
propionaldehyde
Q79AF6
mutant enzyme I171A, at 25C in 100 mM HEPES buffer (pH 8.0)
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.147
-
acetaldehyde
Q79AF6
mutant enzyme I195A, at 25C in 100 mM HEPES buffer (pH 8.0)
6104
0.152
-
acetaldehyde
Q79AF6
mutant enzyme I195W, at 25C in 100 mM HEPES buffer (pH 8.0)
6104
0.223
-
acetaldehyde
Q79AF6
mutant enzyme I171F, at 25C in 100 mM HEPES buffer (pH 8.0)
6104
0.457
-
acetaldehyde
Q79AF6
mutant enzyme I195F, at 25C in 100 mM HEPES buffer (pH 8.0)
6104
0.46
-
acetaldehyde
Q79AF6
mutant enzyme D208A, at 25C in 100 mM HEPES buffer (pH 8.0)
6104
0.73
-
acetaldehyde
Q79AF6
wild type enzyme, at 25C in 100 mM HEPES buffer (pH 8.0)
6104
2.224
-
acetaldehyde
Q79AF6
mutant enzyme I171A, at 25C in 100 mM HEPES buffer (pH 8.0)
6104
0.0433
-
Butyraldehyde
Q79AF6
mutant enzyme I195F, at 25C in 100 mM HEPES buffer (pH 8.0)
8146
0.0458
-
Butyraldehyde
Q79AF6
mutant enzyme I195W, at 25C in 100 mM HEPES buffer (pH 8.0)
8146
0.3
-
Butyraldehyde
Q79AF6
wild type enzyme, at 25C in 100 mM HEPES buffer (pH 8.0)
8146
0.37
-
Butyraldehyde
Q79AF6
mutant enzyme I171F, at 25C in 100 mM HEPES buffer (pH 8.0)
8146
1.323
-
Butyraldehyde
Q79AF6
mutant enzyme I171A, at 25C in 100 mM HEPES buffer (pH 8.0)
8146
2.763
-
Butyraldehyde
Q79AF6
mutant enzyme I195A, at 25C in 100 mM HEPES buffer (pH 8.0)
8146
0.0265
-
pentaldehyde
Q79AF6
mutant enzyme I195W, at 25C in 100 mM HEPES buffer (pH 8.0)
136620
0.0346
-
pentaldehyde
Q79AF6
mutant enzyme I195F, at 25C in 100 mM HEPES buffer (pH 8.0)
136620
0.0728
-
pentaldehyde
Q79AF6
mutant enzyme I171A, at 25C in 100 mM HEPES buffer (pH 8.0)
136620
0.076
-
pentaldehyde
Q79AF6
wild type enzyme, at 25C in 100 mM HEPES buffer (pH 8.0)
136620
1.584
-
pentaldehyde
Q79AF6
mutant enzyme I195A, at 25C in 100 mM HEPES buffer (pH 8.0)
136620
0.00011
-
picolinaldehyde
Q79AF6
mutant enzyme I195W, at 25C in 100 mM HEPES buffer (pH 8.0)
136679
0.00076
-
picolinaldehyde
Q79AF6
mutant enzyme I195F, at 25C in 100 mM HEPES buffer (pH 8.0)
136679
0.0387
-
picolinaldehyde
Q79AF6
mutant enzyme I171F, at 25C in 100 mM HEPES buffer (pH 8.0)
136679
0.154
-
picolinaldehyde
Q79AF6
wild type enzyme, at 25C in 100 mM HEPES buffer (pH 8.0)
136679
0.468
-
picolinaldehyde
Q79AF6
mutant enzyme I195A, at 25C in 100 mM HEPES buffer (pH 8.0)
136679
0.597
-
picolinaldehyde
Q79AF6
mutant enzyme I171A, at 25C in 100 mM HEPES buffer (pH 8.0)
136679
0.0425
-
propionaldehyde
Q79AF6
mutant enzyme I195W, at 25C in 100 mM HEPES buffer (pH 8.0)
15841
0.167
-
propionaldehyde
Q79AF6
mutant enzyme I195F, at 25C in 100 mM HEPES buffer (pH 8.0)
15841
0.221
-
propionaldehyde
Q79AF6
mutant enzyme I171F, at 25C in 100 mM HEPES buffer (pH 8.0)
15841
0.384
-
propionaldehyde
Q79AF6
mutant enzyme I195A, at 25C in 100 mM HEPES buffer (pH 8.0)
15841
0.7
-
propionaldehyde
Q79AF6
wild type enzyme, at 25C in 100 mM HEPES buffer (pH 8.0)
15841
1.219
-
propionaldehyde
Q79AF6
mutant enzyme I171A, at 25C in 100 mM HEPES buffer (pH 8.0)
15841
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
265
-
acetaldehyde
-
at 25C in 50 mM Tris/HCl buffer, pH 8.0
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
20
60
-
55% of maximal activity at 20C, 60% at 60C
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
Leuconostoc mesenteroides LMC7
-
-
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Giardia intestinalis WB
-
-
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Clostridium phytofermentans (strain ATCC 700394 / DSM 18823 / ISDg)
Geobacillus thermoglucosidasius (strain C56-YS93)
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5
8
-
enzyme activity falls to 50% at pH 5 and pH 8
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
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
40
-
-
15 min, 30% activity left
45
-
-
15 min, inactivation
70
-
-
3 min, inactivation above
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
C131A
Q79AF6
inactive
C131S
Q79AF6
inactive
D208A
Q79AF6
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
I171A
Q79AF6
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
Q79AF6
the mutant shows strongly reduced catalytic efficiency compared to the wild type enzyme
I195A
Q79AF6
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
Q79AF6
the mutant shows severely reduced catalytic efficiency compared to the wild type enzyme
I195W
Q79AF6
the mutant shows strongly reduced catalytic efficiency compared to the wild type enzyme
N170A
Q79AF6
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
Q79AF6
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