BRENDA - Enzyme Database
show all sequences of 1.2.1.5

Gene cloning and biochemical characterization of a NAD(P)+ -dependent aldehyde dehydrogenase from Bacillus licheniformis

Lo, H.F.; Chen, Y.J.; Mol. Biotechnol. 46, 157-167 (2010)

Data extracted from this reference:

Activating Compound
Activating Compound
Commentary
Organism
Structure
2-mercaptoethanol
246% activity at 2 mM
Bacillus licheniformis
dithiothreitol
276% activity at 2 mM
Bacillus licheniformis
Cloned(Commentary)
Commentary
Organism
expressed in Escherichia coli M15(pREP4) cells
Bacillus licheniformis
Inhibitors
Inhibitors
Commentary
Organism
Structure
1,2-Cyclohexanedione
33% residual activity at 2.5 mM
Bacillus licheniformis
2,4-Dinitro-1-fluorobenzene
11% residual activity at 2.5 mM
Bacillus licheniformis
Co2+
89% residual activity at 1 mM
Bacillus licheniformis
Cu2+
20% residual activity at 1 mM
Bacillus licheniformis
diethyl dicarbonate
2% residual activity at 2.5 mM
Bacillus licheniformis
ethyl acetimidate
71% residual activity at 250 mM
Bacillus licheniformis
Fe2+
88% residual activity at 1 mM
Bacillus licheniformis
Hg2+
complete inhibition at 0.25 mM
Bacillus licheniformis
Mg2+
89% residual activity at 1 mM
Bacillus licheniformis
Mn2+
89% residual activity at 1 mM
Bacillus licheniformis
additional information
not inhibited by EDTA
Bacillus licheniformis
N-Acetylimidazole
75% residual activity at 2.5 mM
Bacillus licheniformis
N-bromosuccinimide
66% residual activity at 0.5 mM
Bacillus licheniformis
phenylmethylsulfonyl fluoride
73% residual activity at 2.5 mM
Bacillus licheniformis
Woodward's reagent K
71% residual activity at 50 mM
Bacillus licheniformis
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.12
-
Valeraldehyde
with NAD+ as cosubstrate, in 50 mM potassium phosphate buffer (pH 7.0), 1 mM dithiothreitol, at 37°C
Bacillus licheniformis
0.34
-
Valeraldehyde
with NADP+ as cosubstrate, in 50 mM potassium phosphate buffer (pH 7.0), 1 mM dithiothreitol, at 37°C
Bacillus licheniformis
0.46
-
propionaldehyde
with NAD+ as cosubstrate, in 50 mM potassium phosphate buffer (pH 7.0), 1 mM dithiothreitol, at 37°C
Bacillus licheniformis
0.65
-
propionaldehyde
with NADP+ as cosubstrate, in 50 mM potassium phosphate buffer (pH 7.0), 1 mM dithiothreitol, at 37°C
Bacillus licheniformis
2.95
-
Butyraldehyde
with NAD+ as cosubstrate, in 50 mM potassium phosphate buffer (pH 7.0), 1 mM dithiothreitol, at 37°C
Bacillus licheniformis
4.93
-
Butyraldehyde
with NADP+ as cosubstrate, in 50 mM potassium phosphate buffer (pH 7.0), 1 mM dithiothreitol, at 37°C
Bacillus licheniformis
9.87
-
Isovaleraldehyde
with NAD+ as cosubstrate, in 50 mM potassium phosphate buffer (pH 7.0), 1 mM dithiothreitol, at 37°C
Bacillus licheniformis
10.78
-
Isovaleraldehyde
with NADP+ as cosubstrate, in 50 mM potassium phosphate buffer (pH 7.0), 1 mM dithiothreitol, at 37°C
Bacillus licheniformis
18.89
-
acetaldehyde
with NAD+ as cosubstrate, in 50 mM potassium phosphate buffer (pH 7.0), 1 mM dithiothreitol, at 37°C
Bacillus licheniformis
393.4
-
acetaldehyde
with NADP+ as cosubstrate, in 50 mM potassium phosphate buffer (pH 7.0), 1 mM dithiothreitol, at 37°C
Bacillus licheniformis
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
additional information
the enzyme does not require metal ions for its enzymatic reaction
Bacillus licheniformis
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
52682
-
4 * 52682, calculated from amino acid sequence
Bacillus licheniformis
53000
-
4 * 53000, calculated from amino acid sequence
Bacillus licheniformis
220000
-
gel filtration
Bacillus licheniformis
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Bacillus licheniformis
-
-
-
Bacillus licheniformis ATCC 14580
-
-
-
Purification (Commentary)
Commentary
Organism
Ni2+-NTA resin column chromatography
Bacillus licheniformis
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
acetaldehyde + NAD+
-
725948
Bacillus licheniformis
acetate + NADH + H+
-
-
-
?
acetaldehyde + NADP+
-
725948
Bacillus licheniformis
acetate + NADPH + H+
-
-
-
?
butyraldehyde + NAD+
-
725948
Bacillus licheniformis
butyrate + NADH + H+
-
-
-
?
butyraldehyde + NADP+
-
725948
Bacillus licheniformis
butyrate + NADPH + H+
-
-
-
?
isovaleraldehyde + NAD+
-
725948
Bacillus licheniformis
isovalerate + NADH + H+
-
-
-
?
isovaleraldehyde + NADP+
-
725948
Bacillus licheniformis
isovalerate + NADPH + H+
-
-
-
?
isovaleraldehyde + NADP+
-
725948
Bacillus licheniformis ATCC 14580
isovalerate + NADPH + H+
-
-
-
?
additional information
no activity with formaldehyde and benzaldehyde
725948
Bacillus licheniformis
?
-
-
-
-
additional information
no activity with formaldehyde and benzaldehyde
725948
Bacillus licheniformis ATCC 14580
?
-
-
-
-
n-propanal + NADP+
-
725948
Bacillus licheniformis
propionate + NADPH + H+
-
-
-
?
propionaldehyde + NAD+ + H2O
best substrate combination
725948
Bacillus licheniformis
propionate + NADH + H+
-
-
-
?
propionaldehyde + NAD+ + H2O
best substrate combination
725948
Bacillus licheniformis ATCC 14580
propionate + NADH + H+
-
-
-
?
propionaldehyde + NADP+ + H2O
-
725948
Bacillus licheniformis
propionate + NADPH + H+
-
-
-
?
propionaldehyde + NADP+ + H2O
-
725948
Bacillus licheniformis ATCC 14580
propionate + NADPH + H+
-
-
-
?
valeraldehyde + NAD+
-
725948
Bacillus licheniformis
valerate + NADH + H+
-
-
-
?
valeraldehyde + NADP+
-
725948
Bacillus licheniformis
valerate + NADPH + H+
-
-
-
?
valeraldehyde + NADP+
-
725948
Bacillus licheniformis ATCC 14580
valerate + NADPH + H+
-
-
-
?
Subunits
Subunits
Commentary
Organism
homotetramer
4 * 52682, calculated from amino acid sequence; 4 * 53000, calculated from amino acid sequence
Bacillus licheniformis
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
37
-
-
Bacillus licheniformis
Temperature Stability [°C]
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
20
40
the enzyme appears to be stable at 20°C, but becomes very unstable at a temperature above 37°C, most likely due to thermal denaturation
Bacillus licheniformis
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.91
-
Isovaleraldehyde
with NADP+ as cosubstrate, in 50 mM potassium phosphate buffer (pH 7.0), 1 mM dithiothreitol, at 37°C
Bacillus licheniformis
1.11
-
acetaldehyde
with NADP+ as cosubstrate, in 50 mM potassium phosphate buffer (pH 7.0), 1 mM dithiothreitol, at 37°C
Bacillus licheniformis
3.58
-
Isovaleraldehyde
with NAD+ as cosubstrate, in 50 mM potassium phosphate buffer (pH 7.0), 1 mM dithiothreitol, at 37°C
Bacillus licheniformis
4.46
-
acetaldehyde
with NAD+ as cosubstrate, in 50 mM potassium phosphate buffer (pH 7.0), 1 mM dithiothreitol, at 37°C
Bacillus licheniformis
11.5
-
Butyraldehyde
with NADP+ as cosubstrate, in 50 mM potassium phosphate buffer (pH 7.0), 1 mM dithiothreitol, at 37°C
Bacillus licheniformis
13.36
-
propionaldehyde
with NADP+ as cosubstrate, in 50 mM potassium phosphate buffer (pH 7.0), 1 mM dithiothreitol, at 37°C
Bacillus licheniformis
19.41
-
Valeraldehyde
with NADP+ as cosubstrate, in 50 mM potassium phosphate buffer (pH 7.0), 1 mM dithiothreitol, at 37°C
Bacillus licheniformis
30.99
-
Valeraldehyde
with NAD+ as cosubstrate, in 50 mM potassium phosphate buffer (pH 7.0), 1 mM dithiothreitol, at 37°C
Bacillus licheniformis
32.8
-
Butyraldehyde
with NAD+ as cosubstrate, in 50 mM potassium phosphate buffer (pH 7.0), 1 mM dithiothreitol, at 37°C
Bacillus licheniformis
49.38
-
propionaldehyde
with NAD+ as cosubstrate, in 50 mM potassium phosphate buffer (pH 7.0), 1 mM dithiothreitol, at 37°C
Bacillus licheniformis
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7
-
-
Bacillus licheniformis
pH Stability
pH Stability
pH Stability Maximum
Commentary
Organism
4
6
pH 6.0 attenuates more than 39% of enzymatic activity. At pH 5.0, 3% of the activity remains. The enzymatic activity is completely abolished at pH values of or below 4.0
Bacillus licheniformis
Cofactor
Cofactor
Commentary
Organism
Structure
NAD+
preferred cofactor
Bacillus licheniformis
NADP+
-
Bacillus licheniformis
Activating Compound (protein specific)
Activating Compound
Commentary
Organism
Structure
2-mercaptoethanol
246% activity at 2 mM
Bacillus licheniformis
dithiothreitol
276% activity at 2 mM
Bacillus licheniformis
Cloned(Commentary) (protein specific)
Commentary
Organism
expressed in Escherichia coli M15(pREP4) cells
Bacillus licheniformis
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NAD+
preferred cofactor
Bacillus licheniformis
NADP+
-
Bacillus licheniformis
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
1,2-Cyclohexanedione
33% residual activity at 2.5 mM
Bacillus licheniformis
2,4-Dinitro-1-fluorobenzene
11% residual activity at 2.5 mM
Bacillus licheniformis
Co2+
89% residual activity at 1 mM
Bacillus licheniformis
Cu2+
20% residual activity at 1 mM
Bacillus licheniformis
diethyl dicarbonate
2% residual activity at 2.5 mM
Bacillus licheniformis
ethyl acetimidate
71% residual activity at 250 mM
Bacillus licheniformis
Fe2+
88% residual activity at 1 mM
Bacillus licheniformis
Hg2+
complete inhibition at 0.25 mM
Bacillus licheniformis
Mg2+
89% residual activity at 1 mM
Bacillus licheniformis
Mn2+
89% residual activity at 1 mM
Bacillus licheniformis
additional information
not inhibited by EDTA
Bacillus licheniformis
N-Acetylimidazole
75% residual activity at 2.5 mM
Bacillus licheniformis
N-bromosuccinimide
66% residual activity at 0.5 mM
Bacillus licheniformis
phenylmethylsulfonyl fluoride
73% residual activity at 2.5 mM
Bacillus licheniformis
Woodward's reagent K
71% residual activity at 50 mM
Bacillus licheniformis
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.12
-
Valeraldehyde
with NAD+ as cosubstrate, in 50 mM potassium phosphate buffer (pH 7.0), 1 mM dithiothreitol, at 37°C
Bacillus licheniformis
0.34
-
Valeraldehyde
with NADP+ as cosubstrate, in 50 mM potassium phosphate buffer (pH 7.0), 1 mM dithiothreitol, at 37°C
Bacillus licheniformis
0.46
-
propionaldehyde
with NAD+ as cosubstrate, in 50 mM potassium phosphate buffer (pH 7.0), 1 mM dithiothreitol, at 37°C
Bacillus licheniformis
0.65
-
propionaldehyde
with NADP+ as cosubstrate, in 50 mM potassium phosphate buffer (pH 7.0), 1 mM dithiothreitol, at 37°C
Bacillus licheniformis
2.95
-
Butyraldehyde
with NAD+ as cosubstrate, in 50 mM potassium phosphate buffer (pH 7.0), 1 mM dithiothreitol, at 37°C
Bacillus licheniformis
4.93
-
Butyraldehyde
with NADP+ as cosubstrate, in 50 mM potassium phosphate buffer (pH 7.0), 1 mM dithiothreitol, at 37°C
Bacillus licheniformis
9.87
-
Isovaleraldehyde
with NAD+ as cosubstrate, in 50 mM potassium phosphate buffer (pH 7.0), 1 mM dithiothreitol, at 37°C
Bacillus licheniformis
10.78
-
Isovaleraldehyde
with NADP+ as cosubstrate, in 50 mM potassium phosphate buffer (pH 7.0), 1 mM dithiothreitol, at 37°C
Bacillus licheniformis
18.89
-
acetaldehyde
with NAD+ as cosubstrate, in 50 mM potassium phosphate buffer (pH 7.0), 1 mM dithiothreitol, at 37°C
Bacillus licheniformis
393.4
-
acetaldehyde
with NADP+ as cosubstrate, in 50 mM potassium phosphate buffer (pH 7.0), 1 mM dithiothreitol, at 37°C
Bacillus licheniformis
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
additional information
the enzyme does not require metal ions for its enzymatic reaction
Bacillus licheniformis
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
52682
-
4 * 52682, calculated from amino acid sequence
Bacillus licheniformis
53000
-
4 * 53000, calculated from amino acid sequence
Bacillus licheniformis
220000
-
gel filtration
Bacillus licheniformis
Purification (Commentary) (protein specific)
Commentary
Organism
Ni2+-NTA resin column chromatography
Bacillus licheniformis
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
acetaldehyde + NAD+
-
725948
Bacillus licheniformis
acetate + NADH + H+
-
-
-
?
acetaldehyde + NADP+
-
725948
Bacillus licheniformis
acetate + NADPH + H+
-
-
-
?
butyraldehyde + NAD+
-
725948
Bacillus licheniformis
butyrate + NADH + H+
-
-
-
?
butyraldehyde + NADP+
-
725948
Bacillus licheniformis
butyrate + NADPH + H+
-
-
-
?
isovaleraldehyde + NAD+
-
725948
Bacillus licheniformis
isovalerate + NADH + H+
-
-
-
?
isovaleraldehyde + NADP+
-
725948
Bacillus licheniformis
isovalerate + NADPH + H+
-
-
-
?
isovaleraldehyde + NADP+
-
725948
Bacillus licheniformis ATCC 14580
isovalerate + NADPH + H+
-
-
-
?
additional information
no activity with formaldehyde and benzaldehyde
725948
Bacillus licheniformis
?
-
-
-
-
additional information
no activity with formaldehyde and benzaldehyde
725948
Bacillus licheniformis ATCC 14580
?
-
-
-
-
n-propanal + NADP+
-
725948
Bacillus licheniformis
propionate + NADPH + H+
-
-
-
?
propionaldehyde + NAD+ + H2O
best substrate combination
725948
Bacillus licheniformis
propionate + NADH + H+
-
-
-
?
propionaldehyde + NAD+ + H2O
best substrate combination
725948
Bacillus licheniformis ATCC 14580
propionate + NADH + H+
-
-
-
?
propionaldehyde + NADP+ + H2O
-
725948
Bacillus licheniformis
propionate + NADPH + H+
-
-
-
?
propionaldehyde + NADP+ + H2O
-
725948
Bacillus licheniformis ATCC 14580
propionate + NADPH + H+
-
-
-
?
valeraldehyde + NAD+
-
725948
Bacillus licheniformis
valerate + NADH + H+
-
-
-
?
valeraldehyde + NADP+
-
725948
Bacillus licheniformis
valerate + NADPH + H+
-
-
-
?
valeraldehyde + NADP+
-
725948
Bacillus licheniformis ATCC 14580
valerate + NADPH + H+
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
homotetramer
4 * 52682, calculated from amino acid sequence; 4 * 53000, calculated from amino acid sequence
Bacillus licheniformis
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
37
-
-
Bacillus licheniformis
Temperature Stability [°C] (protein specific)
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
20
40
the enzyme appears to be stable at 20°C, but becomes very unstable at a temperature above 37°C, most likely due to thermal denaturation
Bacillus licheniformis
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.91
-
Isovaleraldehyde
with NADP+ as cosubstrate, in 50 mM potassium phosphate buffer (pH 7.0), 1 mM dithiothreitol, at 37°C
Bacillus licheniformis
1.11
-
acetaldehyde
with NADP+ as cosubstrate, in 50 mM potassium phosphate buffer (pH 7.0), 1 mM dithiothreitol, at 37°C
Bacillus licheniformis
3.58
-
Isovaleraldehyde
with NAD+ as cosubstrate, in 50 mM potassium phosphate buffer (pH 7.0), 1 mM dithiothreitol, at 37°C
Bacillus licheniformis
4.46
-
acetaldehyde
with NAD+ as cosubstrate, in 50 mM potassium phosphate buffer (pH 7.0), 1 mM dithiothreitol, at 37°C
Bacillus licheniformis
11.5
-
Butyraldehyde
with NADP+ as cosubstrate, in 50 mM potassium phosphate buffer (pH 7.0), 1 mM dithiothreitol, at 37°C
Bacillus licheniformis
13.36
-
propionaldehyde
with NADP+ as cosubstrate, in 50 mM potassium phosphate buffer (pH 7.0), 1 mM dithiothreitol, at 37°C
Bacillus licheniformis
19.41
-
Valeraldehyde
with NADP+ as cosubstrate, in 50 mM potassium phosphate buffer (pH 7.0), 1 mM dithiothreitol, at 37°C
Bacillus licheniformis
30.99
-
Valeraldehyde
with NAD+ as cosubstrate, in 50 mM potassium phosphate buffer (pH 7.0), 1 mM dithiothreitol, at 37°C
Bacillus licheniformis
32.8
-
Butyraldehyde
with NAD+ as cosubstrate, in 50 mM potassium phosphate buffer (pH 7.0), 1 mM dithiothreitol, at 37°C
Bacillus licheniformis
49.38
-
propionaldehyde
with NAD+ as cosubstrate, in 50 mM potassium phosphate buffer (pH 7.0), 1 mM dithiothreitol, at 37°C
Bacillus licheniformis
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7
-
-
Bacillus licheniformis
pH Stability (protein specific)
pH Stability
pH Stability Maximum
Commentary
Organism
4
6
pH 6.0 attenuates more than 39% of enzymatic activity. At pH 5.0, 3% of the activity remains. The enzymatic activity is completely abolished at pH values of or below 4.0
Bacillus licheniformis
KCat/KM [mM/s]
kcat/KM Value [1/mMs-1]
kcat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
0.003
-
acetaldehyde
with NADP+ as cosubstrate, in 50 mM potassium phosphate buffer (pH 7.0), 1 mM dithiothreitol, at 37°C
Bacillus licheniformis
0.09
-
Isovaleraldehyde
with NADP+ as cosubstrate, in 50 mM potassium phosphate buffer (pH 7.0), 1 mM dithiothreitol, at 37°C
Bacillus licheniformis
0.24
-
acetaldehyde
with NAD+ as cosubstrate, in 50 mM potassium phosphate buffer (pH 7.0), 1 mM dithiothreitol, at 37°C
Bacillus licheniformis
0.36
-
Isovaleraldehyde
with NAD+ as cosubstrate, in 50 mM potassium phosphate buffer (pH 7.0), 1 mM dithiothreitol, at 37°C
Bacillus licheniformis
2.39
-
Butyraldehyde
with NADP+ as cosubstrate, in 50 mM potassium phosphate buffer (pH 7.0), 1 mM dithiothreitol, at 37°C
Bacillus licheniformis
11.89
-
Butyraldehyde
with NAD+ as cosubstrate, in 50 mM potassium phosphate buffer (pH 7.0), 1 mM dithiothreitol, at 37°C
Bacillus licheniformis
20.67
-
propionaldehyde
with NADP+ as cosubstrate, in 50 mM potassium phosphate buffer (pH 7.0), 1 mM dithiothreitol, at 37°C
Bacillus licheniformis
56.66
-
Valeraldehyde
with NADP+ as cosubstrate, in 50 mM potassium phosphate buffer (pH 7.0), 1 mM dithiothreitol, at 37°C
Bacillus licheniformis
107.5
-
propionaldehyde
with NAD+ as cosubstrate, in 50 mM potassium phosphate buffer (pH 7.0), 1 mM dithiothreitol, at 37°C
Bacillus licheniformis
257
-
Valeraldehyde
with NAD+ as cosubstrate, in 50 mM potassium phosphate buffer (pH 7.0), 1 mM dithiothreitol, at 37°C
Bacillus licheniformis
KCat/KM [mM/s] (protein specific)
KCat/KM Value [1/mMs-1]
KCat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
0.003
-
acetaldehyde
with NADP+ as cosubstrate, in 50 mM potassium phosphate buffer (pH 7.0), 1 mM dithiothreitol, at 37°C
Bacillus licheniformis
0.09
-
Isovaleraldehyde
with NADP+ as cosubstrate, in 50 mM potassium phosphate buffer (pH 7.0), 1 mM dithiothreitol, at 37°C
Bacillus licheniformis
0.24
-
acetaldehyde
with NAD+ as cosubstrate, in 50 mM potassium phosphate buffer (pH 7.0), 1 mM dithiothreitol, at 37°C
Bacillus licheniformis
0.36
-
Isovaleraldehyde
with NAD+ as cosubstrate, in 50 mM potassium phosphate buffer (pH 7.0), 1 mM dithiothreitol, at 37°C
Bacillus licheniformis
2.39
-
Butyraldehyde
with NADP+ as cosubstrate, in 50 mM potassium phosphate buffer (pH 7.0), 1 mM dithiothreitol, at 37°C
Bacillus licheniformis
11.89
-
Butyraldehyde
with NAD+ as cosubstrate, in 50 mM potassium phosphate buffer (pH 7.0), 1 mM dithiothreitol, at 37°C
Bacillus licheniformis
20.67
-
propionaldehyde
with NADP+ as cosubstrate, in 50 mM potassium phosphate buffer (pH 7.0), 1 mM dithiothreitol, at 37°C
Bacillus licheniformis
56.66
-
Valeraldehyde
with NADP+ as cosubstrate, in 50 mM potassium phosphate buffer (pH 7.0), 1 mM dithiothreitol, at 37°C
Bacillus licheniformis
107.5
-
propionaldehyde
with NAD+ as cosubstrate, in 50 mM potassium phosphate buffer (pH 7.0), 1 mM dithiothreitol, at 37°C
Bacillus licheniformis
257
-
Valeraldehyde
with NAD+ as cosubstrate, in 50 mM potassium phosphate buffer (pH 7.0), 1 mM dithiothreitol, at 37°C
Bacillus licheniformis
Other publictions for EC 1.2.1.5
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
735898
Alam
Human salivary aldehyde dehydr ...
Homo sapiens
Cell Biochem. Biophys.
74
307-315
2016
3
-
-
-
-
-
-
4
-
-
-
-
-
1
-
-
1
-
-
1
-
-
5
-
1
-
2
-
1
-
-
1
-
-
-
3
-
-
1
-
-
-
-
-
-
4
-
-
-
-
-
-
-
1
-
1
-
-
5
-
1
-
2
-
1
-
-
-
-
-
-
-
-
-
739913
Hong
Alternative biotransformation ...
Bacillus cereus, Bacillus cereus ATCC 10876
Appl. Environ. Microbiol.
82
3940-3946
2016
-
-
1
-
4
-
-
7
-
-
2
-
-
3
-
-
1
-
-
-
-
-
10
1
-
-
-
7
-
-
-
2
-
-
-
-
-
1
2
-
4
-
-
-
-
7
-
-
2
-
-
-
-
1
-
-
-
-
10
1
-
-
-
7
-
-
-
-
-
-
-
-
7
7
740279
Mali
Impaired ALDH2 activity decrea ...
Rattus norvegicus
Cell. Signal.
28
1-6
2016
-
-
-
-
-
-
2
-
1
-
-
-
-
1
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
1
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
741087
Tomita
Aldehyde dehydrogenase 1A1 in ...
Homo sapiens
Oncotarget
7
11018-11032
2016
-
1
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
1
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
741167
Jimenez-Lopez
-
Narrow-leafed lupin (Lupinus a ...
Lupinus angustifolius
Plant Gene
6
67-76
2016
-
-
-
-
-
-
-
-
5
-
-
2
-
1
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
2
-
-
-
-
-
-
-
5
-
-
2
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
740294
Gonzalez-Segura
Residues that influence coenzy ...
Sulfurisphaera tokodaii, Sulfurisphaera tokodaii DSM 16993
Chem. Biol. Interact.
234
59-74
2015
-
-
-
-
-
-
-
2
-
-
-
4
-
2
-
-
-
-
-
-
-
-
4
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
2
-
-
-
-
-
-
2
-
-
-
4
-
-
-
-
-
-
-
-
4
-
-
-
-
-
-
-
-
-
-
-
-
-
2
2
722210
Liu
Molecular characterization of ...
Sulfurisphaera tokodaii, Sulfurisphaera tokodaii 7
Extremophiles
17
181-190
2013
1
-
1
-
-
1
11
5
-
4
3
-
11
3
-
-
1
-
-
-
-
-
17
1
1
1
3
5
1
1
-
2
-
-
-
1
-
1
2
-
-
1
-
11
-
5
-
4
3
-
11
-
-
1
-
-
-
-
17
1
1
1
3
5
1
1
-
-
-
-
-
-
5
5
723877
Ngo
Expression, crystallization an ...
Bacillus cereus, Bacillus cereus ATCC 10876
Acta Crystallogr. Sect. F
69
528-531
2013
-
-
1
1
-
-
-
-
-
-
1
-
-
3
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
-
2
-
-
-
-
-
1
2
1
-
-
-
-
-
-
-
-
1
-
-
-
-
1
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
724620
Zhou
Production of 3-hydroxypropion ...
Klebsiella pneumoniae, Klebsiella pneumoniae DSM 2026
Biotechnol. Bioeng.
110
3177-3187
2013
-
1
-
-
-
-
-
-
-
-
-
-
-
6
-
-
-
-
-
-
1
-
2
-
-
-
-
-
-
-
-
2
-
-
-
-
1
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
724720
Gonzalez-Segura
Catalytic contribution of thre ...
Homo sapiens
Chem. Biol. Interact.
202
32-40
2013
-
-
1
1
4
-
-
10
1
1
1
2
-
1
-
-
1
-
-
-
-
-
2
1
-
-
-
10
-
-
-
1
-
-
-
-
-
1
1
1
4
-
-
-
-
10
1
1
1
2
-
-
-
1
-
-
-
-
2
1
-
-
-
10
-
-
-
-
-
-
-
-
10
10
725085
Zhou
Aldehyde dehydrogenase protein ...
Zea mays
Funct. Integr. Genomics
12
683-691
2012
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
1
1
2
-
-
747332
Aquino Neto
Development of nanostructured ...
Saccharomyces cerevisiae
Biosens. Bioelectron.
26
2922-2926
2011
-
1
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
711110
Koenig
Aldehyde dehydrogenase 1A3 is ...
Homo sapiens
Biochem. Biophys. Res. Commun.
400
207-211
2010
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
4
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
4
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
1
-
-
711635
Stagos
Corneal aldehyde dehydrogenase ...
Mus musculus
Brain Res. Bull.
81
211-218
2010
-
-
-
-
-
-
-
-
1
-
-
2
-
1
-
-
-
-
-
2
-
-
2
1
-
-
-
-
-
-
-
2
-
-
-
-
-
-
2
-
-
-
-
-
-
-
1
-
-
2
-
-
-
-
-
2
-
-
2
1
-
-
-
-
-
-
-
-
-
1
1
-
-
-
725948
Lo
Gene cloning and biochemical c ...
Bacillus licheniformis, Bacillus licheniformis ATCC 14580
Mol. Biotechnol.
46
157-167
2010
2
-
1
-
-
-
15
10
-
1
3
-
-
3
-
-
1
-
-
-
-
-
17
1
1
-
1
10
1
-
1
2
-
-
-
2
-
1
2
-
-
-
-
15
-
10
-
1
3
-
-
-
-
1
-
-
-
-
17
1
1
-
1
10
1
-
1
-
-
-
-
-
10
10
698095
Gao
Evolutionary and expression st ...
Oryza sativa
Gene
431
86-94
2009
-
-
1
-
-
-
-
-
2
-
11
9
-
9
-
-
-
-
-
1
-
-
9
-
-
-
-
-
-
-
-
2
-
-
-
-
-
9
18
-
-
-
-
-
-
-
5
-
13
9
-
-
-
-
-
9
-
-
9
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
684586
Maestre
Effects of ADH2 overexpression ...
Lactobacillus casei BL23
Appl. Environ. Microbiol.
74
702-707
2008
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
684721
Glatt
Detoxification of promutagenic ...
Homo sapiens
Arch. Biochem. Biophys.
477
196-205
2008
-
-
1
-
-
-
-
8
1
-
-
-
-
1
-
-
1
-
-
3
-
-
9
-
-
-
-
-
1
-
1
1
-
-
-
-
-
1
1
-
-
-
-
-
-
8
1
-
-
-
-
-
-
1
-
3
-
-
9
-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
685040
Ho
A point mutation produced a cl ...
Homo sapiens
Biochem. Pharmacol.
76
690-696
2008
-
-
1
-
1
-
-
-
-
-
-
-
-
2
-
-
1
-
-
1
-
-
4
-
-
-
-
-
-
-
-
1
-
-
-
-
-
1
1
-
1
-
-
-
-
-
-
-
-
-
-
-
-
1
-
1
-
-
4
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
686531
Quash
Aldehyde dehydrogenase inhibit ...
Homo sapiens
Eur. J. Med. Chem.
43
906-916
2008
-
-
-
-
-
-
2
-
-
-
-
-
-
4
-
-
-
-
-
4
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
4
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
688414
Bajns J.
Structural and biochemical cha ...
Paraburkholderia xenovorans, Paraburkholderia xenovorans LB400
J. Mol. Biol.
379
597-608
2008
-
-
1
1
-
-
-
8
-
-
1
-
-
2
-
-
1
-
-
-
-
-
8
1
-
-
-
-
-
-
-
2
-
-
-
-
-
1
2
1
-
-
-
-
-
8
-
-
1
-
-
-
-
1
-
-
-
-
8
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
690142
Alnouti
Tissue distribution, ontogeny, ...
Mus musculus
Toxicol. Sci.
101
51-64
2008
-
-
-
-
-
-
-
-
2
-
-
-
-
3
-
-
-
-
-
15
-
-
3
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
3
-
-
-
-
-
-
-
6
-
-
-
-
-
-
-
-
45
-
-
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
692251
Marchitti
Non-P450 aldehyde oxidizing en ...
Homo sapiens
Expert. Opin. Drug Metab. Toxicol.
4
697-720
2008
-
1
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
688446
Szoecs
Increased superoxide productio ...
Rattus norvegicus, Saccharomyces cerevisiae
J. Mol. Cell. Cardiol.
42
1111-1118
2007
-
2
-
-
-
-
2
-
-
-
-
-
-
2
-
-
-
-
-
3
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
3
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
689379
Marchitti
Neurotoxicity and metabolism o ...
Homo sapiens
Pharmacol. Rev.
59
125-150
2007
-
-
-
-
-
-
1
5
3
-
-
-
-
3
-
-
-
-
-
2
-
-
7
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
3
-
-
-
-
3
-
6
5
-
-
-
-
-
-
-
-
6
-
-
7
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
671511
Ohta
A novel nicotinoprotein aldehy ...
Sphingopyxis macrogoltabida 103, Sphingopyxis macrogoltabida
Appl. Microbiol. Biotechnol.
68
639-646
2005
-
1
1
-
-
-
8
1
-
1
2
2
-
3
-
-
1
-
-
1
2
-
24
1
1
-
-
-
1
-
-
2
-
-
-
-
1
1
2
-
-
-
-
8
-
1
-
1
2
2
-
-
-
1
-
1
2
-
24
1
1
-
-
-
1
-
-
-
-
-
-
-
-
-
656571
Oikawa
-
Paradoxical thermostable enzym ...
Cytophaga sp.
J. Mol. Catal. B
23
65-70
2003
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
22
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
22
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
654425
Yamanaka
Thermostable aldehyde dehydrog ...
Cytophaga sp.
Biochem. Biophys. Res. Commun.
298
632-637
2002
-
-
1
-
-
-
-
3
-
-
2
-
-
3
-
-
1
-
-
-
1
1
24
1
1
-
2
-
1
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
-
3
-
-
2
-
-
-
-
1
-
-
1
1
24
1
1
-
2
-
1
-
1
-
-
-
-
-
-
-
348696
Izaguirre
Human aldehyde dehydrogenase c ...
Homo sapiens
J. Biomol. Struct. Dyn.
19
429-447
2001
-
-
-
-
-
-
2
13
2
-
-
-
-
3
-
-
-
-
-
-
-
-
9
-
-
-
-
-
-
-
-
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2
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13
2
-
-
-
-
-
-
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-
-
-
-
9
-
-
-
-
-
-
-
-
-
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-
-
-
-
348798
Schraeder
NAD(P)-dependent aldehyde dehy ...
Cupriavidus necator, Cupriavidus necator Bo
J. Bacteriol.
183
7408-7411
2001
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2
1
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3
2
-
2
-
-
1
-
-
-
-
1
12
1
-
-
-
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
-
2
1
1
-
-
3
2
-
-
-
1
-
-
-
1
12
1
-
-
-
-
1
-
-
-
-
-
-
-
-
-
655423
Boubekeur
Participation of acetaldehyde ...
Saccharomyces cerevisiae
Eur. J. Biochem.
268
5057-5065
2001
-
-
-
-
-
-
-
-
1
1
-
1
-
2
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
1
-
1
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
348797
Perozich
Shifting the NAD/NADP preferen ...
Rattus norvegicus
Eur. J. Biochem.
267
6197-6203
2000
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-
-
-
6
-
1
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
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-
-
-
-
-
-
-
-
-
-
6
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
348783
Wang
Molecular cloning, characteriz ...
Saccharomyces cerevisiae
J. Bacteriol.
180
822-830
1998
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-
1
-
-
-
1
18
2
4
2
-
-
1
-
-
1
-
-
-
-
-
3
1
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
1
-
18
2
4
2
-
-
-
-
1
-
-
-
-
3
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
348780
Downes
Purification and properties of ...
Mus musculus
Biochem. Mol. Biol. Int.
30
525-535
1993
-
-
-
-
-
-
1
7
-
-
2
1
-
1
-
-
1
-
-
1
1
-
8
1
-
-
-
7
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
7
-
-
2
1
-
-
-
1
-
1
1
-
8
1
-
-
-
7
-
-
-
-
-
-
-
-
-
-
348782
King
Human corneal aldehyde dehydro ...
Homo sapiens
Biochem. Mol. Biol. Int.
31
49-63
1993
-
-
-
-
-
-
1
6
-
-
-
1
-
3
-
-
1
-
-
1
1
-
7
-
-
-
-
6
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
6
-
-
-
1
-
-
-
1
-
1
1
-
7
-
-
-
-
6
-
-
-
-
-
-
-
-
-
-
348784
Sreerama
Identification and characteriz ...
Homo sapiens
Biochem. Pharmacol.
45
2487-2505
1993
-
-
-
-
-
1
-
17
-
-
5
-
-
2
-
-
1
-
-
3
2
1
7
1
1
-
-
-
2
-
2
-
-
-
-
-
-
-
-
-
-
1
-
-
-
17
-
-
5
-
-
-
-
1
-
3
2
1
7
1
1
-
-
-
2
-
2
-
-
-
-
-
-
-
348781
Choi
-
Purification and characterizat ...
Bos taurus
Korean Biochem. J.
24
224-230
1991
-
-
-
-
-
-
-
8
1
-
2
1
-
1
-
1
1
-
-
1
1
-
7
1
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
8
1
-
2
1
-
-
1
1
-
1
1
-
7
1
-
-
-
-
1
-
-
-
-
-
-
-
-
-
348788
Jeng
Purification and characterizat ...
Rattus norvegicus
Arch. Biochem. Biophys.
289
214-222
1991
-
-
1
-
-
-
-
2
1
-
-
-
-
1
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-
-
1
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-
1
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-
1
-
-
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-
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-
1
-
-
-
-
-
-
-
2
1
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-
-
-
-
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-
-
1
-
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
348787
Evces
Characterization of rat cornea ...
Rattus norvegicus
Arch. Biochem. Biophys.
274
518-524
1989
-
-
-
-
-
-
1
10
-
-
2
1
-
2
-
-
1
-
-
3
1
-
16
1
-
-
1
1
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
10
-
-
2
1
-
-
-
1
-
3
1
-
16
1
-
-
1
1
2
-
-
-
-
-
-
-
-
-
348786
Senior
Purification and characterizat ...
Rattus norvegicus
Arch. Biochem. Biophys.
262
211-220
1988
-
-
-
-
-
-
2
-
1
-
2
-
-
1
-
-
1
-
-
1
2
1
12
1
-
-
1
-
1
1
-
-
4
-
-
-
-
-
-
-
-
-
-
2
4
-
1
-
2
-
-
-
-
1
-
1
2
1
12
1
-
-
1
-
1
1
-
-
-
-
-
-
-
-
348789
Rietveld
Substituent effects during the ...
Rattus norvegicus, Saccharomyces cerevisiae
Biochim. Biophys. Acta
914
162-169
1987
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-
-
-
-
-
-
27
2
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-
-
-
2
-
-
-
-
-
1
-
-
11
-
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-
-
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-
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-
-
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-
-
-
-
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-
-
27
2
-
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-
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-
1
-
-
11
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
348790
Lindahl
Characterization of aldehyde d ...
Rattus norvegicus
Biochim. Biophys. Acta
843
180-185
1985
-
-
-
-
-
-
1
4
-
-
1
-
-
1
-
-
1
-
-
1
1
-
2
-
-
-
1
-
1
-
-
2
-
-
-
-
-
-
2
-
-
-
-
1
-
4
-
-
1
-
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-
-
1
-
1
1
-
2
-
-
-
1
-
1
-
-
-
-
-
-
-
-
-
348792
Eckfeldt
Isozymes of aldehyde dehydroge ...
Equus caballus
Methods Enzymol.
89
474-479
1982
-
-
-
-
-
-
4
17
-
-
4
-
-
1
-
-
1
-
-
-
1
-
10
1
-
-
-
-
-
-
-
2
-
-
-
-
-
-
2
-
-
-
-
4
-
17
-
-
4
-
-
-
-
1
-
-
1
-
10
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
348793
Tamaki
Aldehyde dehydrogenase from ba ...
Saccharomyces cerevisiae
Methods Enzymol.
89
469-473
1982
-
-
-
-
-
-
-
-
-
-
1
-
-
1
-
-
1
-
-
-
1
1
11
-
-
-
-
-
1
-
-
2
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
1
-
-
-
-
1
-
-
1
1
11
-
-
-
-
-
1
-
-
-
-
-
-
-
-
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348795
Bostian
Kinetics and reaction mechanis ...
Saccharomyces cerevisiae
Biochem. J.
173
787-798
1978
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-
-
-
-
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2
1
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-
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1
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-
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1
-
-
-
-
3
-
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-
1
-
-
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-
-
-
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-
-
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-
-
-
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2
-
1
-
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-
-
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-
-
-
-
-
-
3
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
348794
Tamaki
Purification and properties of ...
Saccharomyces cerevisiae
J. Biochem.
82
73-79
1977
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-
-
-
-
-
-
-
-
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2
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1
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-
1
-
-
-
1
1
13
1
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
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-
-
1
-
-
1
1
13
1
-
-
-
-
1
-
-
-
-
-
-
-
-
-
348796
Eckfeldt
Horse liver aldehyde dehydroge ...
Equus caballus
J. Biol. Chem.
251
236-240
1976
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-
-
-
-
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2
17
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4
1
-
1
-
-
1
-
-
1
3
-
12
1
-
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
2
-
17
-
-
4
1
-
-
-
1
-
1
3
-
12
1
-
-
-
-
-
-
-
-
-
-
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-
-
-