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(2E)-4-hydroxy-2-nonenal + NAD+ + H2O
(2E)-4-hydroxy-2-nonenoic acid + NADH + H+
(E)-2-nonenal + NAD+ + H2O
(E)-non-2-enoate + NADH + H+
-
-
-
-
?
(R)-N-(3-(6-(4-(1,4-dimethyl-3-oxopiperazin-2-yl)phenylamino)-4-methyl-5-oxo-4,5-dihydropyrazin-2-yl)-2-methylphenyl)-4,5,6,7-tetrahydrobenzo[b] thiophene-2-carboxamide + H2O + O2
?
i.e. GDC-0834, a Bruton's tyrosine kinase inhibitor, a potential treatment of rheumatoid arthritis. GDC-0834
compound is extensively metabolized by amide hydrolysis by both aldehyde oxidase and carboxylesterase
-
?
(R)-trans-4-hydroxy-2-nonenal + NAD+ + H2O
(2E,4R)-4-hydroxynon-2-enoic acid + NADH + H+
(S)-trans-4-hydroxy-2-nonenal + NAD+ + H2O
(2E,4S)-4-hydroxynon-2-enoic acid + NADH + H+
-
-
-
?
1,3-dihydroxyacetone + NAD+ + H2O
? + NADH + H+
-
53.93% activity compared to acetaldehyde
-
-
?
1-formyl-6-methylpyrene + NAD+
6-methylpyrene 1-carboxylate + NADH + H+
-
-
-
?
1-formyl-6-methylpyrene + NAD+ + H2O
6-methylpyrene-1-carboxylic acid + NADH + H+
-
-
-
?
1-formyl-8-methylpyrene + NAD+ + H2O
8-methylpyrene-1-carboxylic acid + NADH + H+
-
-
-
?
1-formyl-8-methylpyrene + NADP+
8-methylpyrene 1-carboxylate + NADPH + H+
-
-
-
?
1-formylpyrene + NAD+
pyrene 1-carboxylate + NADH + H+
-
-
-
?
1-formylpyrene + NAD+ + H2O
pyrene-1-carboxylic acid + NADH + H+
-
-
-
?
1-naphthaldehyde + NAD+ + H2O
1-naphthoic acid + NADH
46.9% activity compared to p-tolualdehyde
-
-
?
1-naphthaldehyde + NAD+ + H2O
1-naphthoic acid + NADH + H+
-
-
-
-
?
2,4-dinitrobenzaldehyde + NAD+ + H2O
2,4-dinitrobenzoate + NADH
-
-
-
-
?
2-chlorobenzaldehyde + NAD+ + H2O
2-chlorobenzoate + NADH + H+
-
28.35% activity compared to formaldehyde
-
-
?
2-formylpyrene + NAD+
pyrene 2-carboxylate + NADH + H+
-
-
-
?
2-formylpyrene + NAD+ + H2O
pyrene-2-carboxylic acid + NADH + H+
-
-
-
?
2-furaldehyde + NAD+ + H2O
2-furanoic acid + NADH + H+
2-hydroxy-3-nitrobenzaldehyde + NAD+ + H2O
2-hydroxy-3-nitrobenzoic acid + NADH + H+
2-naphthaldehyde + NAD+ + H2O
2-naphthalene carboxylate + NADH + H+
-
-
-
-
?
2-naphthaldehyde + NAD+ + H2O
2-naphthoate + NADH
-
-
-
-
?
2-naphthaldehyde + NAD+ + H2O
2-naphthoic acid + NADH
48.8% activity compared to p-tolualdehyde
-
-
?
2-naphthaldehyde + NAD+ + H2O
2-naphthoic acid + NADH + H+
-
-
-
-
?
2-nonenal + NAD+ + H2O
(E)-non-2-enoate + NADH + H+
-
-
-
-
?
2-phthalaldehyde + NAD+ + H2O
phthalate + NADH + H+
-
10.81% activity compared to formaldehyde
-
-
?
2-quinolinone-4-carboxaldehyde + NAD+ + H2O
2-quinolinone-4-carboxylate + NADH
-
-
-
-
?
3,4,5-trimethoxybenzaldehyde + NAD+ + H2O
3,4,5-trimethoxybenzoic acid + NADH + H+
-
-
-
-
?
3,4-dihydroxybenzaldehyde + NAD+ + H2O
3,4-dihydroxybenzoic acid + NADH + H+
-
-
-
-
?
3,4-dihydroxymandelic aldehyde + NAD+ + H2O
3,4-dihydroxymandelate + NADH
-
-
-
-
?
3,4-dihydroxyphenyl acetaldehyde + NAD+ + H2O
3,4-dihydroxyphenylacetate + NADH
-
-
-
-
?
3,4-dihydroxyphenylacetaldehyde + NAD+ + H2O
3,4-dihydroxyphenylacetate + NADH + H+
3,4-dihydroxyphenylacetaldehyde + NAD+ + H2O
3,4-dihydroxyphenylacetic acid + NADH + H+
-
-
-
-
?
3,4-dihydroxyphenylglycolaldehyde + NAD+ + H2O
3,4-dihydroxyphenylglycolate + NADH + H+
-
-
-
?
3,4-dimethoxy-5-hydroxybenzaldehyde + NAD+ + H2O
3,4-dimethoxy-5-hydroxybenzoic acid + NADH + H+
-
-
-
-
?
3,4-dimethoxybenzaldehyde + NAD+ + H2O
3,4-dimethoxybenzoate + NADH
-
-
-
-
?
3,4-dimethoxybenzaldehyde + NAD+ + H2O
3,4-dimethoxybenzoic acid + NADH + H+
-
-
-
-
?
3-hydroxy-4-methoxybenzaldehyde + NAD+ + H2O
3-hydroxy-4-methoxybenzoate + NADH + H+
-
-
-
-
?
3-hydroxypropaldehyde + NAD+ + H2O
3-hydroxypropionate + NADH + H+
-
-
-
-
?
3-hydroxypropanal + NAD+ + H2O
3-hydroxypropionate + NADH + H+
3-hydroxypropanoate + NADH + 2 H+
3-hydroxypropionaldehyde + NAD+ + H2O
-
-
-
-
r
3-hydroxypropionaldehyde + NAD+ + H2O
3-hydroxypropanoate + NADH + 2 H+
3-hydroxypropionaldehyde + NAD+ + H2O
3-hydroxypropionic acid + NADH + H+
3-methoxy-4-hydroxyphenylacetaldehyde + NAD+ + H2O
3-methoxy-4-hydroxyphenylacetate + NADH + H+
-
-
-
-
?
3-nitrobenzaldehyde + NAD+ + H2O
3-nitrobenzoate + NADH + H+
-
32.98% activity compared to acetaldehyde
-
-
?
3-oxopropyl phosphonate + NAD+ + H2O
?
-
-
-
?
3-oxopropylphosphonate + NAD+ + H2O
?
-
-
-
?
3-pyridinecarboxaldehyde + NAD+ + H2O
3-pyridinecarboxylate + NADH
-
-
-
-
?
4-aminobutyraldehyde + NAD+ + H2O
4-aminobutyrate + NADH
-
-
-
-
?
4-carboxybenzaldehyde + NAD+ + H2O
4-carboxybenzoate + NADH
-
-
-
-
?
4-chlorobenzaldehyde + NAD+ + H2O
4-chlorobenzoate + NADH
-
-
-
-
?
4-chlorophenylacetaldehyde + NAD+ + H2O
4-chlorophenylacetate + NADH + H+
-
-
-
-
?
4-cyanobenzaldehyde + NAD+ + H2O
4-cyanobenzoate + NADH
-
-
-
-
?
4-dimethylamino-1-naphthaldehyde + NAD+ + H2O
4-dimethylamino-1-naphthoic acid + NADH + H+
-
-
-
-
?
4-dimethylaminobenzaldehyde + NAD+ + H2O
4-dimethylaminobenzoate + NADH + H+
-
-
-
-
?
4-fluorophenylacetaldehyde + NAD+ + H2O
4-fluorophenylacetate + NADH + H+
-
-
-
-
?
4-formylpyrene + NAD+
pyrene 4-carboxylate + NADH + H+
-
-
-
?
4-formylpyrene + NAD+ + H2O
pyrene-4-carboxylic acid + NADH + H+
-
-
-
?
4-hydroxy-2-nonenal + NAD+ + H2O
4-hydroxy-2-nonenoate + NADH + H+
4-hydroxy-2-nonenal + NAD+ + H2O
4-hydroxynon-2-enoate + NADH + H+
-
-
-
-
?
4-hydroxy-2-nonenal + NAD+ + H2O
4-hydroxynon-2-enoic acid + NADH
4-hydroxy-3,5-dimethoxybenzaldehyde + NAD+ + H2O
4-hydroxy-3,5-dimethoxybenzoic acid + NADH + H+
-
-
-
-
?
4-hydroxy-3-methoxybenzaldehyde + NAD+ + H2O
4-hydroxy-3-methoxybenzoate + NADH + H+
-
-
-
-
?
4-hydroxy-3-methoxybenzaldehyde + NAD+ + H2O
4-hydroxy-3-methoxybenzoic acid + NADH + H+
-
-
-
-
?
4-hydroxybenzaldehyde + NAD+ + H2O
4-hydroxybenzoic acid + NADH + H+
-
-
-
-
?
4-hydroxynon-2-enal + NAD+
4-hydroxynon-2-enoic acid + NADH
-
-
-
-
?
4-hydroxynonenal + NAD+ + H2O
4-hydroxynonanoate + NADH
-
-
-
-
?
4-hydroxynonenal + NAD+ + H2O
4-hydroxynonanoate + NADH + H+
-
-
-
-
?
4-hydroxynonenal + NAD+ + H2O
? + NADH + H+
-
-
-
-
?
4-hydroxyphenyl-3-methoxyglycolaldehyde + NAD+ + H2O
4-hydroxyphenyl-3-methoxyglycolate + NADH
-
-
-
-
?
4-hydroxyphenylglycolaldehyde + NAD+ + H2O
4-hydroxyphenylglycolate + NADH
-
-
-
-
?
4-methoxy-1-naphthaldehyde + NAD+ + H2O
4-methoxy-1-naphthoate + NADH
-
-
-
-
?
4-methoxy-1-naphthaldehyde + NAD+ + H2O
4-methoxy-1-naphthoic acid + NADH + H+
-
-
-
-
?
4-methoxybenzaldehyde + NAD+ + H2O
4-methoxybenzoate + NADH + H+
-
-
-
-
?
4-nitro-1-naphthaldehyde + NAD+ + H2O
4-nitro-1-naphthoate + NADH
-
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
-
r
4-oxonon-2-enal + NAD+ + H2O
4-oxonon-2-enoic acid + NADH
-
-
-
-
?
5-(dimethylamino)-2-naphthaldehyde + NAD+ + H2O
5-(dimethylamino)-2-naphthoate + NADH + H+
-
-
-
-
r
5-bromo-1-naphthaldehyde + NAD+ + H2O
5-bromo-1-naphthoate + NADH
-
-
-
-
?
5-hydroxyindol acetaldehyde + NAD+ + H2O
5-hydroxyindol acetate + NADH + H+
-
-
-
-
?
5-methoxyindole-3-carboxaldehyde + NAD+ + H2O
5-methoxyindole-3-carboxylate + NADH
-
-
-
-
?
5-nitro-1-naphthaldehyde + NAD+ + H2O
5-nitro-1-naphthoate + NADH + H+
-
-
-
-
r
6,7-dimethoxycoumarin-3-carboxaldehyde + NAD+ + H2O
6,7-dimethoxycoumarin-3-carboxylate + NADH + H+
-
-
-
-
r
6,7-dimethoxycoumarin-4-carboxaldehyde + NAD+ + H2O
6,7-dimethoxycoumarin-4-carboxylate + NADH
-
-
-
-
?
6-(dimethylamino)-2-naphthaldehyde + NAD+ + H2O
6-(dimethylamino)-2-naphthoate + NADH
-
-
-
-
?
6-dimethylamino-2-naphthaldehyde + NAD+ + H2O
6-dimethylamino-2-naphthalene carboxylate + NADH + H+
-
activity assay
-
-
?
6-dimethylamino-2-naphthaldehyde + NAD+ + H2O
6-dimethylamino-2-naphthoic acid + NADH + H+
-
-
-
-
?
6-methoxy-2-naphthaldehyde + NAD+ + H2O
6-methoxy-2-naphthalene carboxylate + NADH + H+
-
activity assay
-
-
?
6-methoxy-2-naphthaldehyde + NAD+ + H2O
6-methoxy-2-naphthoate + NADH + H+
6-methoxy-2-naphthaldehyde + NAD+ + H2O
6-methoxy-2-naphthoic acid + NADH + H+
-
-
-
-
?
6-methoxy-2-quinolinone-4-carboxaldehyde + NAD+ + H2O
6-methoxy-2-quinolinone-4-carboxylate + NADH
-
-
-
-
?
7-(dimethylamino)-2-quinolinone-4-carboxaldehyde + NAD+ + H2O
7-(dimethylamino)-2-quinolinone-4-carboxylate + NADH
-
-
-
-
?
7-(dimethylamino)-coumarin-3-carboxaldehyde + NAD+ + H2O
7-(dimethylamino)-coumarin-3-carboxylate + NADH + H+
-
-
-
-
r
7-(dimethylamino)coumarin-4-carboxaldehyde + NAD+ + H2O
7-(dimethylamino)coumarin-4-carboxylate + NADH
-
-
-
-
?
7-acetoxycoumarin-3-carboxaldehyde + NAD+ + H2O
7-acetoxycoumarin-3-carboxylate + NADH + H+
-
-
-
-
r
7-acetoxycoumarin-4-carboxaldehyde + NAD+ + H2O
7-acetoxycoumarin-4-carboxylate + NADH
-
-
-
-
?
7-hydroxycoumarin-3-carboxaldehyde + NAD+ + H2O
7-hydroxycoumarin-3-carboxylate + NADH + H+
-
-
-
-
r
7-hydroxycoumarin-4-carboxaldehyde + NAD+ + H2O
7-hydroxycoumarin-4-carboxylate + NADH
-
-
-
-
?
7-methoxy-1-naphthaldehyde + NAD+ + H2O
7-methoxy-1-naphthoic acid + NADH + H+
7-methoxy-2-quinolinone-4-carboxaldehyde + NAD+ + H2O
7-methoxy-2-quinolinone-4-carboxylate + NADH
-
-
-
-
?
7-methoxycoumarin-3-carboxaldehyde + NAD+ + H2O
7-methoxycoumarin-3-carboxylate + NADH + H+
-
-
-
-
r
7-methoxycoumarin-4-carboxaldehyde + NAD+ + H2O
7-methoxycoumarin-4-carboxylate + NADH
-
-
-
-
?
9-cis retinal + NAD+ + H2O
9-cis retinoic acid + NADH
-
-
-
-
?
9-cis-retinal + NAD+ + H2O
9-cis-retinoic acid + NADH + H+
-
-
-
-
?
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
acetaldehyde + NADP+ + H2O
acetate + NADPH + H+
-
low activity with NADP+
-
-
?
acetate + NADH + H+
acetaldehyde + NAD+ + H2O
acrolein + NAD+ + H2O
? + NADH + H+
-
-
-
-
?
aldophosphamide + NAD+ + H2O
? + NADH + H+
-
-
-
-
?
all-trans retinal + NAD+ + H2O
all-trans retinoic acid + NADH
-
-
-
-
?
all-trans-retinal + NAD+ + H2O
all-trans-retinoic acid + NADH + H+
-
-
-
-
?
alpha-aminoadipate semialdehyde + NAD+ + H2O
alpha-aminoadipate + NADH + H+
alpha-aminoadipate semialdehyde + NAD+ + H2O
alpha-aminoadipic acid + NADH + H+
-
-
-
-
?
alpha-phenylpropanal + NAD+ + H2O
alpha-phenylpropionate + NADH
-
-
-
-
?
an aldehyde + NAD+ + H2O
an acid + NADH + H+
-
-
-
-
?
anisaldehyde + NAD+ + H2O
? + NADH
-
-
-
-
?
benzaldehyde + NAD(P)+ + H2O
benzoate + NAD(P)H + H+
-
-
-
-
?
benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
benzaldehyde + NADP+
benzoate + NADPH
-
-
-
-
?
benzaldehyde + NADP+ + H2O
benzoate + NADPH + H+
-
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + H+
-
-
-
-
?
butanal + NAD+ + H2O
butyrate + NADH + H+
butyraldehyde + NAD+ + H2O
butanoate + NADH + H+
-
the activity on butyraldehyde is about 95% of that on valeraldehyde
-
-
?
butyraldehyde + NAD+ + H2O
butanoic acid + NADH + H+
-
-
-
-
?
butyraldehyde + NAD+ + H2O
butyrate + NADH + H+
chloral + NAD+ + H2O
trichloroacetate + NADH + H+
-
2.67% activity compared to acetaldehyde
-
-
?
chloroacetaldehyde + NAD+ + H2O
chloroacetate + NADH + H+
cinnamaldehyde + NAD+ + H2O
cinnamate + NADH + H+
cinnamic aldehyde + NAD+ + H2O
cinnamic acid + NADH + H+
-
-
-
-
?
citral + NAD+ + H2O
(2E)-3,7-dimethylocta-2,6-dienoic acid + NADH
-
-
-
-
?
crotonaldehyde + NAD+ + H2O
crotonate + NADH
-
-
-
-
?
cyclohexanaldehyde + NAD+ + H2O
cyclohexanoate + NADH
-
-
-
-
?
D-glucose + NAD+ + H2O
D-glucuronic acid + NADH
-
-
-
-
?
D-glyceraldehyde + NAD+ + H2O
D-glycerate + NADH + H+
dansyl-aminoacetaldehyde + ?
dansylglycine + ?
-
the fluorescent substrate is used to monitor aldehyde dehydrogenase activity in fluorescence-activated cell sorting
-
-
?
decanal + NAD+ + H2O
decanaote + NADH
-
-
-
?
decanal + NAD+ + H2O
decanoate + NADH
decanaldehyde + NAD+ + H2O
decanoate + NADH + H+
-
50.3% activity compared to formaldehyde
-
-
?
DL-glyceraldehyde + NAD+ + H2O
DL-glycerate + NADH + H+
DL-glyceraldehyde 3-phosphate + NAD+ + H2O
DL-glycerate 3-phosphate + NADH + H+
-
52.7% activity compared to acetaldehyde
-
-
?
dodecanal + NAD+ + H2O
dodecanoate + NADH
-
n-dodecylaldehyde
-
-
?
dodecanal + NAD+ + H2O
dodecanoate + NADH + H+
dodecanaldehyde + NAD+ + H2O
dodecanoate + NADH + H+
-
42.02% activity compared to formaldehyde
-
-
?
eicosanoic aldehyde + NAD+ + H2O
eicosanoate + NADH + H+
-
8.79% activity compared to formaldehyde
-
-
?
fluorene-2-carboxaldehyde + NAD+ + H2O
fluorene-2-carboxylate + NADH
-
-
-
-
?
formaldehyde + NAD+
formate + NADH + H+
-
-
-
?
formaldehyde + NAD+ + H2O
formate + NADH
formaldehyde + NAD+ + H2O
formate + NADH + H+
glutaraldehyde + NAD+ + H2O
glutarate + NADH
-
-
-
-
?
glutathione-4-oxonon-2-enal + NAD+ + H2O
glutathione-4-oxonon-2-enoic acid + NADH
-
-
-
-
?
glyceraldehyde + NAD+ + H2O
glycerate + NADH
glyceraldehyde + NAD+ + H2O
glycerate + NADH + H+
glyceraldehyde 3-phosphate + NAD+ + H2O
?
-
-
-
?
glyceraldehyde 3-phosphate + NAD+ + H2O
glycerate 3-phosphate + NADH
-
-
-
-
?
glyceraldehyde-3-phosphate + NAD+ + H2O
?
-
-
-
?
glyceryl trinitrate + NADH + H+
1,2-glyceryl dinitrate + nitrite + NAD+
-
-
-
-
?
glyceryl trinitrate + NADH + H+
1,3-glyceryl dinitrate + nitrite + NAD+
-
-
-
-
?
glycolaldehyde + NAD+ + H2O
glycolate + NADH
glycolaldehyde + NAD+ + H2O
glycolate + NADH + H+
-
75.43% activity compared to acetaldehyde
-
-
?
glyoxal + NAD+ + H2O
oxalate + NADH
-
-
-
-
?
heptanal + NAD+ + H2O
heptanoate + NADH
hexadecanal + NAD+ + H2O
hexadecanoate + NADH + H+
-
15.77% activity compared to formaldehyde
-
-
?
hexaldehyde + NAD+ + H2O
hexanoate + NADH + H+
-
76.21% activity compared to formaldehyde
-
-
?
hexanal + NAD+ + H2O
hexanoate + NADH + H+
hexanaldehyde + NAD+ + H2O
hexanoate + NADH + H+
-
-
-
?
hydrocinnamaldehyde + NAD+ + H2O
hydrocinnamate + NADH
-
-
-
-
?
indole-3-acetaldehyde + NAD+ + H2O
indole-3-acetate + NADH + H+
indole-3-aldehyde + NAD+ + H2O
indole-3-carboxylate + NADH
isobutanal + NAD+ + H2O
isobutyrate + NADH
-
-
-
-
?
isovaleraldehyde + NAD+ + H2O
isovalerate + NADH + H+
m-chlorobenzaldehyde + NAD+ + H2O
m-chlorobenzoic acid + NADH + H+
44.7% activity compared to p-tolualdehyde
-
-
?
m-fluorobenzaldehyde + NAD+ + H2O
m-fluorobenzoic acid + NADH + H+
m-hydroxybenzaldehyde + NAD+ + H2O
m-hydroxybenzoate + NADH + H+
-
-
-
-
?
m-hydroxybenzaldehyde + NAD+ + H2O
m-hydroxybenzoic acid + NADH + H+
23.6% activity compared to p-tolualdehyde
-
-
?
m-methoxybenzaldehyde + NAD+ + H2O
m-methoxybenzoate + NADH + H+
m-methoxybenzaldehyde + NAD+ + H2O
m-methoxybenzoic acid + NADH + H+
88.5% activity compared to p-tolualdehyde
-
-
?
m-methylbenzaldehyde + NAD+ + H2O
m-methylbenzoate + NADH
-
-
-
-
?
m-nitrobenzaldehyde + NAD+ + H2O
m-nitrobenzoate + NADH
m-nitrobenzaldehyde + NAD+ + H2O
m-nitrobenzoic acid + NADH
46.8% activity compared to p-tolualdehyde
-
-
?
m-tolualdehyde + NAD+ + H2O
m-methylbenzoic acid + NADH
70.8% activity compared to p-tolualdehyde
-
-
?
malondialdehyde + NAD+ + H2O
?
malondialdehyde + NAD+ + H2O
? + NADH
malondialdehyde + NAD+ + H2O
? + NADH + H+
-
-
-
-
?
methylglyoxal + NAD+ + H2O
methylglyoxalate + NADH
-
-
-
-
?
monochloroacetaldehyde + NAD+ + H2O
monochloroacetate + NADH
-
-
-
-
?
N-acetyl-4-aminobutyraldehyde + NAD+ + H2O
N-acetyl-4-aminobutyrate + NADH
-
-
-
-
?
n-nonanal + NAD+ + H2O
n-nonanoate + NADH + H+
nitroglycerin + NAD+ + H2O
1,2-glyceryl dinitrate + NO + NADH + H+
-
-
-
-
?
nonanal + NAD+ + H2O
nonanoate + NADH + H+
o-chlorobenzaldehyde + NAD+ + H2O
o-chlorobenzoic acid + NADH + H+
3.4% activity compared to p-tolualdehyde
-
-
?
o-fluorobenzaldehyde + NAD+ + H2O
o-fluorobenzoic acid + NADH + H+
o-hydroxybenzaldehyde + NAD+ + H2O
o-hydroxybenzoate + NADH + H+
-
-
-
-
?
o-hydroxybenzaldehyde + NAD+ + H2O
o-hydroxybenzoic acid + NADH + H+
65.2% activity compared to p-tolualdehyde
-
-
?
o-methoxybenzaldehyde + NAD+ + H2O
o-methoxybenzoate + NADH + H+
-
-
-
-
?
o-methoxybenzaldehyde + NAD+ + H2O
o-methoxybenzoic acid + NADH + H+
2.6% activity compared to p-tolualdehyde
-
-
?
o-methylbenzaldehyde + NAD+ + H2O
o-methylbenzoate + NADH
-
-
-
-
?
o-nitrobenzaldehyde + NAD+ + H2O
o-nitrobenzoate + NADH
-
-
-
-
?
o-nitrobenzaldehyde + NAD+ + H2O
o-nitrobenzoic acid + NADH
17.8% activity compared to p-tolualdehyde
-
-
?
o-tolualdehyde + NAD+ + H2O
o-methylbenzoic acid + NADH
3.7% activity compared to p-tolualdehyde
-
-
?
octadecanal + NAD+ + H2O
octadecanoate + NADH + H+
-
12% activity compared to formaldehyde
-
-
?
octanal + NAD+ + H2O
octanoate + NADH
octanal + NAD+ + H2O
octanoate + NADH + H+
octyl aldehyde + NAD+ + H2O
octanoate + NADH + H+
-
72.27% activity compared to formaldehyde
-
-
?
p-(dimethylamino)-benzaldehyde + NAD+ + H2O
p-(dimethylamino)benzoate + NADH
-
-
-
-
?
p-(dimethylamino)cinnamaldehyde + NAD+ + H2O
p-(dimethylamino)cinnamate + NADH
p-carboxybenzaldehyde + NAD+ + H2O
p-carboxybenzoate + NADH
-
-
-
-
?
p-chlorobenzaldehyde + NAD+ + H2O
p-chlorobenzoic acid + NADH + H+
79.6% activity compared to p-tolualdehyde
-
-
?
p-fluorobenzaldehyde + NAD+ + H2O
p-fluorobenzoic acid + NADH + H+
p-hydroxybenzaldehyde + NAD+ + H2O
p-hydroxybenzoic acid + NADH + H+
4.2% activity compared to p-tolualdehyde
-
-
?
p-hydroxyphenylacetaldehyde + NAD+ + H2O
p-hydroxyphenylacetate + NADH
p-methoxybenzaldehyde + NAD+ + H2O
p-methoxybenzoate + NADH + H+
p-methoxybenzaldehyde + NAD+ + H2O
p-methoxybenzoic acid + NADH + H+
6.2% activity compared to p-tolualdehyde
-
-
?
p-methylbenzaldehyde + NAD+ + H2O
p-methylbenzoate + NADH
-
-
-
-
?
p-nitrobenzaldehyde + NAD+ + H2O
p-nitrobenzoate + NADH
p-nitrobenzaldehyde + NAD+ + H2O
p-nitrobenzoic acid + NADH
69% activity compared to p-tolualdehyde
-
-
?
p-nitrocinnamaldehyde + NAD+ + H2O
p-nitrocinnamate + NADH
-
-
-
-
?
p-nitrophenyl acetate + H2O
p-nitrophenol + acetate
-
esterase activity of the various isoenzymes is less than 7% of the activity with propanal and NAD+
-
-
?
p-tolualdehyde + NAD+ + H2O
p-methylbenzoic acid + NADH
highest activity
-
-
?
pentanal + NAD+ + H2O
pentanoate + NADH
pentanaldehyde + NAD+ + H2O
pentanoate + NADH + H+
-
-
-
?
phenanthrene-9-carboxaldehyde + NAD+ + H2O
phenanthrene-9-carboxylate + NADH
-
-
-
-
?
phenylacetaldehyde + NAD+ + H2O
phenylacetate + NADH + H+
phosphonoacetaldehyde + NAD+
?
-
-
-
-
?
phosphonoacetaldehyde + NAD+ + H2O
phosphonoacetate + NADH + H+
-
-
-
?
pimelic semialdehyde + NAD+ + H2O
?
pivaldehyde + NAD+ + H2O
pivalate + NADH
-
-
-
-
?
propanal + 1,N6-ethenoadenine dinucleotide + H2O
propionate + ?
-
isoenzyme E3
-
-
?
propanal + 3-acetylpyridine-adenine dinucleotide + H2O
propionate + ?
-
isoenzyme E3
-
-
?
propanal + 3-acetylpyridine-NAD+ + H2O
propionate + 3-acetylpyridine-NADH
-
-
-
-
?
propanal + 3-thionicotinamide-adenine dinucleotide + H2O
propionate + ?
-
isoenzyme E3
-
-
?
propanal + deamino-NAD+ + H2O
propionate + deamino-NADH
-
-
-
-
?
propanal + N-guanine dinucleotide + H2O
propionate + ?
-
isoenzyme E3
-
-
?
propanal + NAD+ + H2O
propanoate + NADH + H+
propanal + NAD+ + H2O
propanoic acid + NADH + H+
-
activity assay
-
-
?
propanal + NAD+ + H2O
propionate + NADH
propanal + NAD+ + H2O
propionate + NADH + H+
propanal + oxidized nicotinamide hypoxanthine dinucleotide + H2O
propionate + reduced nicotinamide hypoxanthine dinucleotide
-
isoenzyme E3
-
-
?
propanal + [5-(3-acetylpyridino)pentyl]diphosphoadenosine + H2O
propanoate + ?
-
-
-
-
?
propionaldehyde + NAD+
propionate + NADH + H+
-
-
-
?
propionaldehyde + NAD+ + H2O
propanoate + NADH + H+
propionaldehyde + NAD+ + H2O
propanoic acid + NADH + H+
-
-
-
-
?
propionaldehyde + NAD+ + H2O
propionate + NADH
-
-
-
-
?
propionaldehyde + NAD+ + H2O
propionate + NADH + H+
protocatechaldehyde + NAD+ + H2O
protocatechuic acid + NADH
4.5% activity compared to p-tolualdehyde
-
-
?
pyridine 3-aldehyde + NAD+ + H2O
pyridine-3-carboxylate + NADH
-
-
-
-
?
pyridine-3-aldehyde adenine dinucleotide + NAD+ + H2O
pyridine-3-carboxylate adenine dinucleotide + NADH
-
-
-
-
?
pyruvic aldehyde + NAD+ + H2O
pyruvate + NADH
-
-
-
-
?
quinoline-3-carboxaldehyde + NAD+ + H2O
quinoline-3-carboxylate + NADH
-
-
-
-
?
quinoline-4-carboxaldehyde + NAD+ + H2O
quinoline-4-carboxylate + NADH
-
-
-
-
?
retinal + NAD+ + H2O
retinoic acid + NADH + H+
-
-
-
?
retinol + NAD+ + H2O
retinoic acid + NADH + H+
-
-
-
-
?
succinic semialdehyde + NAD+ + H2O
succinate + NADH
syringaldehyde + NAD+ + H2O
syringic acid + NADH
65.1% activity compared to p-tolualdehyde
-
-
?
tetradecanal + NAD+ + H2O
tetradecanoate + NADH
tetradecyl aldehyde + NAD+ + H2O
tetradecanoate + NADH + H+
-
11.71% activity compared to formaldehyde
-
-
?
trans-2-hexenal + NAD+ + H2O
(E)-hex-2-enoate + NADH + H+
trans-2-nonenal + NAD+ + H2O
(E)-non-2-enoate + NADH + H+
-
-
-
?
trans-cinnamaldehyde + NAD+ + H2O
trans-cinnamate + NADH
valeraldehyde + NAD+ + H2O
valerate + NADH + H+
vanillin + NAD+ + H2O
vanillic acid + NADH + H+
additional information
?
-
(2E)-4-hydroxy-2-nonenal + NAD+ + H2O
(2E)-4-hydroxy-2-nonenoic acid + NADH + H+
-
-
-
-
?
(2E)-4-hydroxy-2-nonenal + NAD+ + H2O
(2E)-4-hydroxy-2-nonenoic acid + NADH + H+
-
-
-
-
?
(R)-trans-4-hydroxy-2-nonenal + NAD+ + H2O
(2E,4R)-4-hydroxynon-2-enoic acid + NADH + H+
-
-
-
?
(R)-trans-4-hydroxy-2-nonenal + NAD+ + H2O
(2E,4R)-4-hydroxynon-2-enoic acid + NADH + H+
ALDH5A enantioselectively oxidizes (R)-trans-4-hydroxy-2-nonenal
-
-
?
2-furaldehyde + NAD+ + H2O
2-furanoic acid + NADH + H+
-
-
-
-
?
2-furaldehyde + NAD+ + H2O
2-furanoic acid + NADH + H+
-
the activity on 2-furaldehyde is 22% of that on 3-hydroxypropionaldehyde
-
-
?
2-hydroxy-3-nitrobenzaldehyde + NAD+ + H2O
2-hydroxy-3-nitrobenzoic acid + NADH + H+
-
-
-
-
?
2-hydroxy-3-nitrobenzaldehyde + NAD+ + H2O
2-hydroxy-3-nitrobenzoic acid + NADH + H+
-
-
-
?
3,4-dihydroxyphenylacetaldehyde + NAD+ + H2O
3,4-dihydroxyphenylacetate + NADH + H+
-
-
-
-
?
3,4-dihydroxyphenylacetaldehyde + NAD+ + H2O
3,4-dihydroxyphenylacetate + NADH + H+
-
-
-
?
3,4-dihydroxyphenylacetaldehyde + NAD+ + H2O
3,4-dihydroxyphenylacetate + NADH + H+
-
-
-
-
?
3,4-dihydroxyphenylacetaldehyde + NAD+ + H2O
3,4-dihydroxyphenylacetate + NADH + H+
-
-
-
-
?
3-hydroxypropanal + NAD+ + H2O
3-hydroxypropionate + NADH + H+
-
-
-
-
?
3-hydroxypropanal + NAD+ + H2O
3-hydroxypropionate + NADH + H+
-
-
-
-
?
3-hydroxypropionaldehyde + NAD+ + H2O
3-hydroxypropanoate + NADH + 2 H+
-
-
-
-
r
3-hydroxypropionaldehyde + NAD+ + H2O
3-hydroxypropanoate + NADH + 2 H+
-
the activity on 3-hydroxypropionaldehyde is about 70% of that on valeraldehyde
-
-
?
3-hydroxypropionaldehyde + NAD+ + H2O
3-hydroxypropionic acid + NADH + H+
-
-
-
-
?
3-hydroxypropionaldehyde + NAD+ + H2O
3-hydroxypropionic acid + NADH + H+
-
-
-
-
?
3-hydroxypropionaldehyde + NAD+ + H2O
3-hydroxypropionic acid + NADH + H+
specific substrate
-
-
?
3-hydroxypropionaldehyde + NAD+ + H2O
3-hydroxypropionic acid + NADH + H+
specific substrate
-
-
?
3-hydroxypropionaldehyde + NAD+ + H2O
3-hydroxypropionic acid + NADH + H+
-
-
-
?
3-hydroxypropionaldehyde + NAD+ + H2O
3-hydroxypropionic acid + NADH + H+
-
-
-
?
4-hydroxy-2-nonenal + NAD+ + H2O
4-hydroxy-2-nonenoate + NADH + H+
-
low affinity for substrate binding and poor catalytic efficiency
-
-
?
4-hydroxy-2-nonenal + NAD+ + H2O
4-hydroxy-2-nonenoate + NADH + H+
-
-
-
?
4-hydroxy-2-nonenal + NAD+ + H2O
4-hydroxynon-2-enoic acid + NADH
-
-
-
?
4-hydroxy-2-nonenal + NAD+ + H2O
4-hydroxynon-2-enoic acid + NADH
poor substrate of isoform ALDH3A1
-
-
?
6-methoxy-2-naphthaldehyde + NAD+ + H2O
6-methoxy-2-naphthoate + NADH + H+
-
-
-
-
?
6-methoxy-2-naphthaldehyde + NAD+ + H2O
6-methoxy-2-naphthoate + NADH + H+
-
activity assay
-
-
?
7-methoxy-1-naphthaldehyde + NAD+ + H2O
7-methoxy-1-naphthoic acid + NADH + H+
-
-
-
-
?
7-methoxy-1-naphthaldehyde + NAD+ + H2O
7-methoxy-1-naphthoic acid + NADH + H+
-
-
-
-
?
7-methoxy-1-naphthaldehyde + NAD+ + H2O
7-methoxy-1-naphthoic acid + NADH + H+
-
-
-
-
?
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
-
-
-
-
?
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
-
-
-
-
?
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
-
-
-
-
?
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
-
-
-
-
?
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
-
-
-
-
?
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
-
-
-
-
?
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
-
-
-
-
?
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
-
-
-
-
?
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
-
-
-
-
?
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
-
-
-
-
?
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
-
-
-
-
ir
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
-
-
-
-
?
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
-
-
-
-
?
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
-
77.68% activity compared to formaldehyde
-
-
?
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
-
77.68% activity compared to formaldehyde
-
-
?
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
-
-
-
-
?
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
-
-
-
?
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
-
-
-
-
?
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
-
-
-
?
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
-
-
691603, 691867, 691973, 692542, 692781, 693946, 694110, 710796, 711691, 711836, 712497, 741427 -
-
?
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
-
-
-
-
ir
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
-
-
-
?
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
-
-
-
-
?
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
-
-
-
?
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
-
preferred substrate
-
-
?
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
-
activity assay
-
-
?
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
preferred substrate of isozyme ALDH2
-
-
?
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
-
-
-
-
?
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
-
the activity on acetaldehyde is about 50% of that on valeraldehyde
-
-
?
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
-
the activity on acetaldehyde is about 50% of that on valeraldehyde
-
-
?
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
-
-
-
?
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
-
-
-
-
?
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
-
-
-
?
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
-
-
-
?
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
-
-
-
-
?
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
-
-
-
-
?
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
-
activity with cytosolic enzyme, no activity with microsomal enzyme
-
-
?
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
-
-
-
?
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
-
-
-
-
?
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
-
-
-
-
?
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
-
-
-
-
ir
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
-
-
-
-
?
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
-
-
-
-
?
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
-
-
348682, 348690, 348695, 348700, 348707, 348715, 348717, 348791, 692281, 692337, 692623, 695139, 711651 -
-
?
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
-
-
-
?
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
-
mutations in Aldh2 strongly segregate with the phenotypes of low and high alcohol consumption and with kinetic differences in ALDH2, suggesting that pharmacogenetic differences affect voluntary alcohol consumption. Bases mutated in the coding region suggest that aldh2(2) in low drinkers is ancestral to the coding changes of either aldh2(1) or aldh2(3), which segregate with higher ethanol consumption
-
-
?
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
rats with an mutated allele for aldehyde dehydrogenase (ALDH2-2) show a low alcohol consumption phenotype. Homozygous ALDH2-2 rats derived from high-drinker F0 females showed a remarkly higher ethanol consumption than homozygous animals derived from low-drinker females. Mitochondria of F2 rats derived from high alcohol-consuming females were more active in oxidizing substrates that generate NADH for complex I
-
-
?
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
-
-
-
-
?
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
-
activity assay
-
-
?
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
-
100% activity with acetaldehyde and NAD+
-
-
?
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
-
100% activity with acetaldehyde and NAD+
-
-
?
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
-
-
-
-
?
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
-
-
-
-
?
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
-
-
-
-
?
acetate + NADH + H+
acetaldehyde + NAD+ + H2O
-
-
-
-
?
acetate + NADH + H+
acetaldehyde + NAD+ + H2O
-
-
-
-
?
acetate + NADH + H+
acetaldehyde + NAD+ + H2O
-
-
-
-
?
acetate + NADH + H+
acetaldehyde + NAD+ + H2O
-
-
-
-
?
alpha-aminoadipate semialdehyde + NAD+ + H2O
alpha-aminoadipate + NADH + H+
-
-
-
-
?
alpha-aminoadipate semialdehyde + NAD+ + H2O
alpha-aminoadipate + NADH + H+
-
-
-
?
benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
-
-
-
-
?
benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
-
-
-
-
?
benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
-
-
-
-
?
benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
-
72.38% activity compared to formaldehyde
-
-
?
benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
-
72.38% activity compared to formaldehyde
-
-
?
benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
-
-
-
-
?
benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
-
-
-
?
benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
-
-
-
-
?
benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
-
-
-
?
benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
-
-
-
-
?
benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
-
-
-
?
benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
-
low affinity for benzaldehyde
-
-
?
benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
-
-
-
-
?
benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
-
-
-
-
?
benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
-
the activity on benzaldehyde is 35% of that on 3-hydroxypropionaldehyde
-
-
?
benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
-
-
-
-
?
benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
-
the activity on benzaldehyde is 35% of that on 3-hydroxypropionaldehyde
-
-
?
benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
-
-
-
-
?
benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
-
-
-
-
?
benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
-
-
-
-
?
benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
-
best substrate, isoform ALDH1 shows 2fold greater catalytic activity against benzaldehyde than against other substrates, while isoform ALDH2 shows no substrate preferences
-
-
?
benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
-
-
-
-
?
benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
-
promotion-associated enzyme, no activity with phenobarbital-inducible enzyme
-
-
?
benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
73.9% activity compared to p-tolualdehyde
-
-
?
benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
73.9% activity compared to p-tolualdehyde
-
-
?
benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
-
35.5% activity compared to acetaldehyde
-
-
?
benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
-
35.5% activity compared to acetaldehyde
-
-
?
butanal + NAD+ + H2O
butyrate + NADH + H+
-
n-butanal
-
-
?
butanal + NAD+ + H2O
butyrate + NADH + H+
-
-
-
-
?
butanal + NAD+ + H2O
butyrate + NADH + H+
-
-
-
-
?
butanal + NAD+ + H2O
butyrate + NADH + H+
-
-
-
-
?
butanal + NAD+ + H2O
butyrate + NADH + H+
-
n-butanal
-
-
?
butanal + NAD+ + H2O
butyrate + NADH + H+
-
-
-
?
butanal + NAD+ + H2O
butyrate + NADH + H+
-
-
-
?
butanal + NAD+ + H2O
butyrate + NADH + H+
-
-
-
-
?
butyraldehyde + NAD+ + H2O
butyrate + NADH + H+
-
71.65% activity compared to formaldehyde
-
-
?
butyraldehyde + NAD+ + H2O
butyrate + NADH + H+
-
71.65% activity compared to formaldehyde
-
-
?
butyraldehyde + NAD+ + H2O
butyrate + NADH + H+
-
-
-
?
butyraldehyde + NAD+ + H2O
butyrate + NADH + H+
-
48.15% activity compared to acetaldehyde
-
-
?
butyraldehyde + NAD+ + H2O
butyrate + NADH + H+
-
48.15% activity compared to acetaldehyde
-
-
?
butyraldehyde + NAD+ + H2O
butyrate + NADH + H+
-
-
-
?
butyraldehyde + NAD+ + H2O
butyrate + NADH + H+
-
-
-
?
chloroacetaldehyde + NAD+ + H2O
chloroacetate + NADH + H+
-
-
-
-
?
chloroacetaldehyde + NAD+ + H2O
chloroacetate + NADH + H+
-
-
-
?
chloroacetaldehyde + NAD+ + H2O
chloroacetate + NADH + H+
-
activity is twice as fast as with acetaldehyde, native enzyme and mutant enzyme E487K
-
-
?
chloroacetaldehyde + NAD+ + H2O
chloroacetate + NADH + H+
-
activity is twice as fast as with acetaldehyde, native enzyme and mutant enzyme E487K
-
-
?
cinnamaldehyde + NAD+ + H2O
cinnamate + NADH + H+
15.5% activity compared to p-tolualdehyde
-
-
?
cinnamaldehyde + NAD+ + H2O
cinnamate + NADH + H+
15.5% activity compared to p-tolualdehyde
-
-
?
D-glyceraldehyde + NAD+ + H2O
D-glycerate + NADH + H+
-
-
-
-
r
D-glyceraldehyde + NAD+ + H2O
D-glycerate + NADH + H+
-
50.25% activity compared to acetaldehyde
-
-
?
decanal + NAD+ + H2O
decanoate + NADH
-
-
-
-
?
decanal + NAD+ + H2O
decanoate + NADH
-
n-decylaldehyde
-
-
?
decanal + NAD+ + H2O
decanoate + NADH
-
n-decylaldehyde
-
-
?
decanal + NAD+ + H2O
decanoate + NADH
-
-
-
-
?
decanal + NAD+ + H2O
decanoate + NADH
-
-
-
-
?
decanal + NAD+ + H2O
decanoate + NADH
-
-
-
-
?
decanal + NAD+ + H2O
decanoate + NADH
-
-
-
-
?
DL-glyceraldehyde + NAD+ + H2O
DL-glycerate + NADH + H+
-
77.27% activity compared to acetaldehyde
-
-
?
DL-glyceraldehyde + NAD+ + H2O
DL-glycerate + NADH + H+
-
low activity with NADP+
-
-
?
dodecanal + NAD+ + H2O
dodecanoate + NADH + H+
-
-
-
-
?
dodecanal + NAD+ + H2O
dodecanoate + NADH + H+
-
best substrate
-
-
?
formaldehyde + NAD+ + H2O
formate + NADH
-
activity with enzyme ALDH-2, no activity with enzyme ALDH-1
-
-
?
formaldehyde + NAD+ + H2O
formate + NADH
-
-
-
-
ir
formaldehyde + NAD+ + H2O
formate + NADH
-
-
-
-
ir
formaldehyde + NAD+ + H2O
formate + NADH
-
activity with cytosolic enzyme, no activity with microsomal enzyme
-
-
?
formaldehyde + NAD+ + H2O
formate + NADH
-
-
-
-
?
formaldehyde + NAD+ + H2O
formate + NADH
-
-
-
-
?
formaldehyde + NAD+ + H2O
formate + NADH
-
no activity
-
-
?
formaldehyde + NAD+ + H2O
formate + NADH
-
-
-
?
formaldehyde + NAD+ + H2O
formate + NADH
-
-
-
?
formaldehyde + NAD+ + H2O
formate + NADH + H+
-
100% activity
-
-
?
formaldehyde + NAD+ + H2O
formate + NADH + H+
-
-
-
-
?
formaldehyde + NAD+ + H2O
formate + NADH + H+
-
-
-
?
formaldehyde + NAD+ + H2O
formate + NADH + H+
-
-
-
?
formaldehyde + NAD+ + H2O
formate + NADH + H+
-
-
-
?
formaldehyde + NAD+ + H2O
formate + NADH + H+
-
7.77% activity compared to acetaldehyde
-
-
?
glyceraldehyde + NAD+ + H2O
glycerate + NADH
-
-
-
-
?
glyceraldehyde + NAD+ + H2O
glycerate + NADH
-
-
-
-
?
glyceraldehyde + NAD+ + H2O
glycerate + NADH
-
-
-
-
?
glyceraldehyde + NAD+ + H2O
glycerate + NADH
-
-
-
-
?
glyceraldehyde + NAD+ + H2O
glycerate + NADH + H+
-
-
-
-
?
glyceraldehyde + NAD+ + H2O
glycerate + NADH + H+
-
-
-
?
glycolaldehyde + NAD+ + H2O
glycolate + NADH
-
-
-
-
?
glycolaldehyde + NAD+ + H2O
glycolate + NADH
-
the aldehyde dehydrogenase is a halophilic enzyme with the highest activity at 1 M NaCl
-
-
?
glycolaldehyde + NAD+ + H2O
glycolate + NADH
-
-
-
-
?
glycolaldehyde + NAD+ + H2O
glycolate + NADH
-
-
-
-
?
heptanal + NAD+ + H2O
heptanoate + NADH
-
-
-
-
?
heptanal + NAD+ + H2O
heptanoate + NADH
-
n-heptanal
-
-
?
heptanal + NAD+ + H2O
heptanoate + NADH
-
-
-
-
?
hexanal + NAD+ + H2O
hexanoate + NADH + H+
-
-
-
-
?
hexanal + NAD+ + H2O
hexanoate + NADH + H+
-
-
-
?
hexanal + NAD+ + H2O
hexanoate + NADH + H+
-
-
-
-
?
hexanal + NAD+ + H2O
hexanoate + NADH + H+
-
high specificity
-
-
?
hexanal + NAD+ + H2O
hexanoate + NADH + H+
-
n-hexanal
-
-
?
hexanal + NAD+ + H2O
hexanoate + NADH + H+
-
-
-
-
?
hexanal + NAD+ + H2O
hexanoate + NADH + H+
-
-
-
-
?
hexanal + NAD+ + H2O
hexanoate + NADH + H+
-
n-hexanal
-
-
?
hexanal + NAD+ + H2O
hexanoate + NADH + H+
-
-
-
-
?
hexanal + NAD+ + H2O
hexanoate + NADH + H+
-
-
-
-
?
hexanal + NAD+ + H2O
hexanoate + NADH + H+
-
-
-
?
hexanal + NAD+ + H2O
hexanoate + NADH + H+
-
-
-
?
hexanal + NAD+ + H2O
hexanoate + NADH + H+
-
-
-
?
hexanal + NAD+ + H2O
hexanoate + NADH + H+
-
-
-
?
hexanal + NAD+ + H2O
hexanoate + NADH + H+
-
-
-
?
indole-3-acetaldehyde + NAD+ + H2O
indole-3-acetate + NADH + H+
-
-
-
-
?
indole-3-acetaldehyde + NAD+ + H2O
indole-3-acetate + NADH + H+
-
-
-
-
?
indole-3-aldehyde + NAD+ + H2O
indole-3-carboxylate + NADH
-
-
-
-
?
indole-3-aldehyde + NAD+ + H2O
indole-3-carboxylate + NADH
-
-
-
-
?
isovaleraldehyde + NAD+ + H2O
isovalerate + NADH + H+
-
-
-
-
?
isovaleraldehyde + NAD+ + H2O
isovalerate + NADH + H+
-
the activity on isovaleraldehyde is about 80% of that on valeraldehyde
-
-
?
m-fluorobenzaldehyde + NAD+ + H2O
m-fluorobenzoic acid + NADH + H+
52.6% activity compared to p-tolualdehyde
-
-
?
m-fluorobenzaldehyde + NAD+ + H2O
m-fluorobenzoic acid + NADH + H+
52.6% activity compared to p-tolualdehyde
-
-
?
m-methoxybenzaldehyde + NAD+ + H2O
m-methoxybenzoate + NADH + H+
-
-
-
-
?
m-methoxybenzaldehyde + NAD+ + H2O
m-methoxybenzoate + NADH + H+
-
-
-
-
?
m-nitrobenzaldehyde + NAD+ + H2O
m-nitrobenzoate + NADH
-
-
-
-
?
m-nitrobenzaldehyde + NAD+ + H2O
m-nitrobenzoate + NADH
-
-
-
-
?
malondialdehyde + NAD+ + H2O
?
-
low affinity for substrate binding and poor catalytic efficiency
-
-
?
malondialdehyde + NAD+ + H2O
?
-
-
-
?
malondialdehyde + NAD+ + H2O
?
-
poor substrate of isoform ALDH3A1
-
-
?
malondialdehyde + NAD+ + H2O
?
-
-
-
?
malondialdehyde + NAD+ + H2O
? + NADH
-
-
-
-
?
malondialdehyde + NAD+ + H2O
? + NADH
-
-
-
-
?
malondialdehyde + NAD+ + H2O
? + NADH
-
-
-
-
?
n-nonanal + NAD+ + H2O
n-nonanoate + NADH + H+
-
-
-
-
?
n-nonanal + NAD+ + H2O
n-nonanoate + NADH + H+
-
high specificity
-
-
?
n-nonanal + NAD+ + H2O
n-nonanoate + NADH + H+
-
-
-
-
?
nonanal + NAD+ + H2O
nonanoate + NADH + H+
-
-
-
-
?
nonanal + NAD+ + H2O
nonanoate + NADH + H+
-
-
-
?
o-fluorobenzaldehyde + NAD+ + H2O
o-fluorobenzoic acid + NADH + H+
81.6% activity compared to p-tolualdehyde
-
-
?
o-fluorobenzaldehyde + NAD+ + H2O
o-fluorobenzoic acid + NADH + H+
81.6% activity compared to p-tolualdehyde
-
-
?
octanal + NAD+ + H2O
octanoate + NADH
-
-
-
-
?
octanal + NAD+ + H2O
octanoate + NADH
-
-
-
-
?
octanal + NAD+ + H2O
octanoate + NADH
-
n-octylaldehyde
-
-
?
octanal + NAD+ + H2O
octanoate + NADH
-
-
-
-
?
octanal + NAD+ + H2O
octanoate + NADH
-
-
-
?
octanal + NAD+ + H2O
octanoate + NADH
-
-
-
?
octanal + NAD+ + H2O
octanoate + NADH + H+
-
-
-
-
?
octanal + NAD+ + H2O
octanoate + NADH + H+
-
high specificity
-
-
?
p-(dimethylamino)cinnamaldehyde + NAD+ + H2O
p-(dimethylamino)cinnamate + NADH
-
-
-
-
?
p-(dimethylamino)cinnamaldehyde + NAD+ + H2O
p-(dimethylamino)cinnamate + NADH
-
-
-
-
?
p-fluorobenzaldehyde + NAD+ + H2O
p-fluorobenzoic acid + NADH + H+
65.5%activity compared to p-tolualdehyde
-
-
?
p-fluorobenzaldehyde + NAD+ + H2O
p-fluorobenzoic acid + NADH + H+
65.5%activity compared to p-tolualdehyde
-
-
?
p-hydroxyphenylacetaldehyde + NAD+ + H2O
p-hydroxyphenylacetate + NADH
-
-
-
-
?
p-hydroxyphenylacetaldehyde + NAD+ + H2O
p-hydroxyphenylacetate + NADH
-
-
-
-
?
p-methoxybenzaldehyde + NAD+ + H2O
p-methoxybenzoate + NADH + H+
-
-
-
-
?
p-methoxybenzaldehyde + NAD+ + H2O
p-methoxybenzoate + NADH + H+
-
-
-
-
?
p-methoxybenzaldehyde + NAD+ + H2O
p-methoxybenzoate + NADH + H+
-
-
-
-
?
p-nitrobenzaldehyde + NAD+ + H2O
p-nitrobenzoate + NADH
-
-
-
-
?
p-nitrobenzaldehyde + NAD+ + H2O
p-nitrobenzoate + NADH
-
-
-
-
?
p-nitrobenzaldehyde + NAD+ + H2O
p-nitrobenzoate + NADH
-
-
-
-
?
p-nitrobenzaldehyde + NAD+ + H2O
p-nitrobenzoate + NADH
-
-
-
-
?
p-nitrobenzaldehyde + NAD+ + H2O
p-nitrobenzoate + NADH
-
-
-
-
?
pentanal + NAD+ + H2O
pentanoate + NADH
-
-
-
-
?
pentanal + NAD+ + H2O
pentanoate + NADH
-
n-pentanal
-
-
?
pentanal + NAD+ + H2O
pentanoate + NADH
-
-
-
-
?
phenylacetaldehyde + NAD+ + H2O
phenylacetate + NADH + H+
-
-
-
-
?
phenylacetaldehyde + NAD+ + H2O
phenylacetate + NADH + H+
-
best substrate
-
-
?
phenylacetaldehyde + NAD+ + H2O
phenylacetate + NADH + H+
-
37.86% activity compared to formaldehyde
-
-
?
phenylacetaldehyde + NAD+ + H2O
phenylacetate + NADH + H+
-
-
-
-
?
phenylacetaldehyde + NAD+ + H2O
phenylacetate + NADH + H+
-
-
-
-
?
phenylacetaldehyde + NAD+ + H2O
phenylacetate + NADH + H+
-
4.21% activity compared to acetaldehyde
-
-
?
pimelic semialdehyde + NAD+ + H2O
?
-
-
-
-
?
pimelic semialdehyde + NAD+ + H2O
?
-
-
-
-
?
propanal + NAD+ + H2O
propanoate + NADH + H+
-
-
-
-
?
propanal + NAD+ + H2O
propanoate + NADH + H+
-
-
-
-
?
propanal + NAD+ + H2O
propanoate + NADH + H+
-
-
-
?
propanal + NAD+ + H2O
propanoate + NADH + H+
-
-
-
?
propanal + NAD+ + H2O
propanoate + NADH + H+
-
-
-
-
?
propanal + NAD+ + H2O
propionate + NADH
-
-
-
-
?
propanal + NAD+ + H2O
propionate + NADH
-
-
-
-
?
propanal + NAD+ + H2O
propionate + NADH
-
-
-
-
?
propanal + NAD+ + H2O
propionate + NADH
-
-
-
-
?
propanal + NAD+ + H2O
propionate + NADH
-
-
-
-
?
propanal + NAD+ + H2O
propionate + NADH
-
-
-
?
propanal + NAD+ + H2O
propionate + NADH
-
-
-
-
?
propanal + NAD+ + H2O
propionate + NADH
-
-
-
?
propanal + NAD+ + H2O
propionate + NADH
-
-
-
-
?
propanal + NAD+ + H2O
propionate + NADH
-
-
-
-
?
propanal + NAD+ + H2O
propionate + NADH
-
-
-
-
?
propanal + NAD+ + H2O
propionate + NADH
-
-
-
-
?
propanal + NAD+ + H2O
propionate + NADH
-
-
-
-
?
propanal + NAD+ + H2O
propionate + NADH
-
-
-
-
?
propanal + NAD+ + H2O
propionate + NADH
-
-
-
-
?
propanal + NAD+ + H2O
propionate + NADH + H+
-
-
-
-
?
propanal + NAD+ + H2O
propionate + NADH + H+
-
-
-
-
?
propanal + NAD+ + H2O
propionate + NADH + H+
-
-
-
?
propanal + NAD+ + H2O
propionate + NADH + H+
-
-
-
?
propanal + NAD+ + H2O
propionate + NADH + H+
-
-
-
?
propionaldehyde + NAD+ + H2O
propanoate + NADH + H+
-
-
-
-
?
propionaldehyde + NAD+ + H2O
propanoate + NADH + H+
-
-
-
?
propionaldehyde + NAD+ + H2O
propanoate + NADH + H+
-
-
-
?
propionaldehyde + NAD+ + H2O
propanoate + NADH + H+
-
-
-
?
propionaldehyde + NAD+ + H2O
propionate + NADH + H+
-
-
-
-
?
propionaldehyde + NAD+ + H2O
propionate + NADH + H+
-
-
-
-
?
propionaldehyde + NAD+ + H2O
propionate + NADH + H+
-
-
-
-
?
propionaldehyde + NAD+ + H2O
propionate + NADH + H+
-
-
-
?
propionaldehyde + NAD+ + H2O
propionate + NADH + H+
-
-
-
-
?
propionaldehyde + NAD+ + H2O
propionate + NADH + H+
-
-
-
?
propionaldehyde + NAD+ + H2O
propionate + NADH + H+
-
the activity on propionaldehyde is about 55% of that on valeraldehyde
-
-
?
propionaldehyde + NAD+ + H2O
propionate + NADH + H+
-
the activity on propionaldehyde is about 55% of that on valeraldehyde
-
-
?
propionaldehyde + NAD+ + H2O
propionate + NADH + H+
-
-
-
-
?
propionaldehyde + NAD+ + H2O
propionate + NADH + H+
-
-
-
?
propionaldehyde + NAD+ + H2O
propionate + NADH + H+
-
-
-
-
?
propionaldehyde + NAD+ + H2O
propionate + NADH + H+
-
56.22% activity compared to acetaldehyde
-
-
?
propionaldehyde + NAD+ + H2O
propionate + NADH + H+
-
56.22% activity compared to acetaldehyde
-
-
?
succinic semialdehyde + NAD+ + H2O
succinate + NADH
-
-
-
-
?
succinic semialdehyde + NAD+ + H2O
succinate + NADH
-
-
-
?
tetradecanal + NAD+ + H2O
tetradecanoate + NADH
-
high activity
-
-
?
tetradecanal + NAD+ + H2O
tetradecanoate + NADH
-
high activity
-
-
?
trans-2-hexenal + NAD+ + H2O
(E)-hex-2-enoate + NADH + H+
-
-
-
-
?
trans-2-hexenal + NAD+ + H2O
(E)-hex-2-enoate + NADH + H+
-
-
-
?
trans-cinnamaldehyde + NAD+ + H2O
trans-cinnamate + NADH
-
-
-
-
?
trans-cinnamaldehyde + NAD+ + H2O
trans-cinnamate + NADH
-
-
-
-
?
valeraldehyde + NAD+ + H2O
valerate + NADH + H+
-
-
-
-
?
valeraldehyde + NAD+ + H2O
valerate + NADH + H+
-
most preferred substrate, 100% activity
-
-
?
valeraldehyde + NAD+ + H2O
valerate + NADH + H+
-
most preferred substrate, 100% activity
-
-
?
vanillin + NAD+ + H2O
vanillic acid + NADH + H+
-
-
-
-
?
vanillin + NAD+ + H2O
vanillic acid + NADH + H+
62.3% activity compared to p-tolualdehyde
-
-
?
additional information
?
-
-
no activity with benzaldehyde
-
-
?
additional information
?
-
no activity with NADP+
-
-
?
additional information
?
-
-
no activity with NADP+
-
-
?
additional information
?
-
-
no activity with NADP+. Saturated aldehydes are preferred over unsaturated aldehydes, irrespective of chain length
-
-
?
additional information
?
-
-
the enzyme also catalyzes esterase reaction with p-nitrophenylacetate + H2O
-
-
?
additional information
?
-
-
enzyme also posseses esterase activity
-
-
?
additional information
?
-
-
the enzyme may play a role in insecticide resistance
-
-
?
additional information
?
-
-
no activity towards 3-hydroxypropionic acid in the presence of NADPH and formaldehyde
-
-
?
additional information
?
-
-
the enzyme shows 11% activity with NADP+ compared to NAD+. No activity with phenazine methosulfate
-
-
?
additional information
?
-
-
no activity towards NADP+, tetracosaldehyde, 2-hydroxylbenzaldehyde, ethanol, hexadecanol, acetate, and hexadecanoic acid
-
-
?
additional information
?
-
-
the ALDH has no reductive activity on acetate or hexadecanoic acid
-
-
?
additional information
?
-
-
no activity towards NADP+, tetracosaldehyde, 2-hydroxylbenzaldehyde, ethanol, hexadecanol, acetate, and hexadecanoic acid
-
-
?
additional information
?
-
-
the ALDH has no reductive activity on acetate or hexadecanoic acid
-
-
?
additional information
?
-
-
the enzyme may contribute to corneal cellular defense against oxidative damage by metabolizing toxic aldehydes produced during UV-induced lipid peroxidation
-
-
?
additional information
?
-
-
no activity with formaldehyde
-
-
?
additional information
?
-
no activity with formaldehyde
-
-
?
additional information
?
-
-
involved in detoxication of a variety of aldehydes of plant origin, as well as those formed during food processing, or applied as food additives
-
-
?
additional information
?
-
-
ALDH2 is a direct downstream substrate of epsilon protein kinase C
-
-
?
additional information
?
-
ALDH2 denitrates nitroglycerin to 1,2-glyceryl dinitrate and nitrite but also catalyzes reduction of nitroglycerin to NO. In addition to aldehyde oxidation, ALDH2 catalyzes ester hydrolysis. The esterase activity is stimulated by NAD+, but the cofactor is not essential for the reaction
-
-
?
additional information
?
-
-
no activity with NADP+ and unsaturated aldehydes like trans-2-hexenal, trans-2-nonenal, and trans-2 dodecenal
-
-
?
additional information
?
-
-
the enzyme shows esterase activity with 4-nitrophenyl acetate
-
-
?
additional information
?
-
the enzyme shows esterase activity with 4-nitrophenyl acetate
-
-
?
additional information
?
-
-
no activity with aromatic aldehydes such as benzaldehyde, nitrobenzaldehyde, methoxybenzaldehyde, or phenylacetaldehyde
-
-
?
additional information
?
-
no activity with hexanal, propanal, nonanal, acetaldehyde and aminoadipate semialdehyde
-
-
-
additional information
?
-
-
no activity with hexanal, propanal, nonanal, acetaldehyde and aminoadipate semialdehyde
-
-
-
additional information
?
-
-
no appreciable activity is observed on formaldehyde
-
-
?
additional information
?
-
no activity with propionaldehyde, butyraldehyde, valeraldehyde, isovaleraldehyde, and furaldehyde
-
-
?
additional information
?
-
-
no appreciable activity is observed on formaldehyde
-
-
?
additional information
?
-
no activity with propionaldehyde, butyraldehyde, valeraldehyde, isovaleraldehyde, and furaldehyde
-
-
?
additional information
?
-
-
enzyme LsALDH16 also exhibits esterase activity with 4-nitrophenylacetate (pNPA) as substrate in the absence of NAD+, kinetics, overview
-
-
-
additional information
?
-
-
Aldh3a1 metabolizes toxic aldehydes produced by light-induced lipid peroxidation
-
-
?
additional information
?
-
-
the enzyme may contribute to corneal cellular defense against oxidative damage by metabolizing toxic aldehydes produced during UV-induced lipid peroxidation
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
the enzyme also catalyzes esterase reaction with p-nitrophenylacetate + H2O
-
-
?
additional information
?
-
-
enzyme also catalyzes esterase reaction with p-nitrophenyl pivalate + H2O
-
-
?
additional information
?
-
-
constitutive enzyme
-
-
?
additional information
?
-
-
the enzyme is only marginally active with acetaldehyde, while longer-chain aliphatic aldehydes are poor substrates
-
-
?
additional information
?
-
-
the microsomal membrane-bound enzyme is expected to catalyze the oxidation of such water-insoluble aldehydes produced on the surface of the microsomal membrane. The enzyme may also be involved in the conversion of fatty acids to alpha,omega-dicarboxylic acids
-
-
?
additional information
?
-
-
the majority of the vascular ALDH2 is present in the cytoplasm, suggesting that mitochondrial biotransformation of glyceryl trinitrate by ALDH2 plays a minor role in the overall vascular biotransformation
-
-
?
additional information
?
-
-
enzyme ALD2 and ALD3 are stress-induced and glucose-repressed
-
-
?
additional information
?
-
to assess the degree of formaldehyde degradation, luminescence measurements in Vibrio fischeri for formaldehyde toxicity are conducted
-
-
-
additional information
?
-
-
to assess the degree of formaldehyde degradation, luminescence measurements in Vibrio fischeri for formaldehyde toxicity are conducted
-
-
-
additional information
?
-
to assess the degree of formaldehyde degradation, luminescence measurements in Vibrio fischeri for formaldehyde toxicity are conducted
-
-
-
additional information
?
-
-
no activity is detected when NADP+ is used as the oxidant instead of NAD+
-
-
?
additional information
?
-
-
no activity is detected when NADP+ is used as the oxidant instead of NAD+
-
-
?
additional information
?
-
-
no activity with methanol, ethanol and isopropanol
-
-
?
additional information
?
-
-
no activity with methanol, ethanol and isopropanol
-
-
?
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1-(4-chlorophenyl)-3-(1-piperidinyl)-1-propanone
-
-
1-ethoxycyclopropanol
-
-
2,3,5,6,9-pentamethyl-7H-furo[3,2-g][1]benzopyran-7-one
12.8% inhibition at 0.01 mM
-
2,3,5,6-tetramethyl-7H-furo[3,2-g][1]benzopyran-7-one
80.5% inhibition at 0.01 mM
-
2,3,5-trimethyl-6-propyl-7H-furo[3,2-g][1]benzopyran-7-one
98.5% inhibition at 0.01 mM
-
2,3,5-trimethyl-6-[3-oxo-3-(piperidin-1-yl)propyl]-7H-furo[3,2-g][1]benzopyran-7-one
competitve, 96.2% inhibition at 0.01 mM
-
2,3-dimethyl-5-propyl-7H-furo[3,2-g][1]benzopyran-7-one
76.2% inhibition at 0.01 mM
-
2,4-dinitrobenzaldehyde
-
substrate inhibition
2,6-Dichloro-4-nitrophenol
-
primarily inhibits isoform ALDH2 (non-competitive), but does not affect isoform ALDH3A1
2-naphthaldehyde
-
substrate inhibition
2-[(4-methyl-2-oxo-2H-1-benzopyran-7-yl)oxy]acetamide
10.5 inhibition at 0.01 mM
-
3,4,10-trimethyl-2H,6H-benzo[1,2-b:5,4-b']dipyran-2,6-dione
19.8% inhibition at 0.01 mM
-
3,4,8,9-tetramethyl-7H-furo[2,3-f][1]benzopyran-7-one
53.6% inhibition at 0.01 mM
-
3,4-dimethyl-6,7,8,9-tetrahydro-2H-[1]benzofuro[3,2-g][1]benzopyran-2-one
38.7% inhibition at 0.01 mM
-
3,5-dimethyl-6-propyl-7H-furo[3,2-g][1]benzopyran-7-one
93.75% inhibition at 0.01 mM
-
3-(1-azepanyl)-1-phenyl-1-propanone
-
-
3-(7-hydroxy-4-methyl-2-oxo-2H-1-benzopyran-3-yl)propanoic acid
-
-
3-(dimethylamino)-1-(3-fluoro-4-methoxyphenyl)-1-propanone
-
-
3-(dimethylamino)-1-(4-ethylphenyl)-1-propanone
-
-
3-benzyl-4-methyl-2-oxo-2H-1-benzopyran-7-yl methanesulfonate
-
-
3-hydroxyanthranilic acid
-
46% inhibition at 0.002 mM
3-hydroxykynurenine
-
55% inhibition at 0.002 mM
3-tert-butyl-5,6-dimethyl-7H-furo[3,2-g][1]benzopyran-7-one
30.3% inhibition at 0.01 mM
-
3-[(3-oxobutan-2-yl)oxy]-6H-dibenzo[b,d]pyran-6-one
35.6% inhibition at 0.01 mM
-
4-amino-4-methyl-pent-2-ynthioic acid S-methylester
-
i.e. ampal thiolester, inhibits ALDH1 activity in ALDH1-transfected L1210T cells resistant to hydroperoxycyclophosphamide
4-diethylaminobenzaldehyde
4-dimethylamino-4-methyl-pent-2-ynthioic acid S-methylester
-
competitive, 0.4 mM, 30 min, 80% inhibition
4-hydroxy-2-nonenal
-
4-hydroxy-2-nonenal completely inactivates ALDH2 activity in vitro at 100 mM
4-hydroxynon-2-enal
-
10% inhibition at 0.05 mM
4-methyl-4-morpholin-4-yl-pent-2-ynthioic acid S-methylester
-
0.6 mM, 60 min, 15% inhibition
4-methyl-7-[(3-methylbut-2-en-1-yl)oxy]-2H-1-benzopyran-2-one
6.7% inhibition at 0.01 mM
-
4-methyl-7-[(prop-2-en-1-yl)oxy]-2H-1-benzopyran-2-one
5.4% inhibition at 0.01 mM
-
4-nitrophenylacetate
-
substrate inhibition of esterase activity
4-oxonon-2-enal
-
90% inhibition at 0.05 mM
4-oxonon-2-enoic acid
-
90% inhibition at 0.05 mM
4-tetramethylammonium-4-methyl-pent-2-ynthioic acid S-methylester
-
0.6 mM, 60 min, 15% inhibition
5,5'-dithio-bis-(2-nitrobenzoic acid)
-
-
5-benzyl-2,3-dimethyl-7H-furo[3,2-g][1]benzopyran-7-one
16.3% inhibition at 0.01 mM
-
5-hydroxytryptophan
-
23% inhibition at 0.1 mM
5-methyl-2-[(3-oxobutan-2-yl)oxy]-7H-furo[3,2-g][1]benzopyran-7-one
5.6% inhibition at 0.01 mM
-
6-benzyl-3,5-dimethyl-7H-furo[3,2-g][1]benzopyran-7-one
16.4% inhibition at 0.01 mM; 7.2% inhibition at 0.01 mM
-
6-bromo-3-[(1E)-N-hydroxyethanimidoyl]-2H-1-benzopyran-2-one
51.8% inhibition at 0.01 mM
-
6-methyl-3,4-dihydro-2H,8H-benzo[1,2-b:5,4-b']dipyran-2,8-dione
74.5% inhibition at 0.01 mM
-
6-[O-(CH2)5-COOH]-2-naphthaldehyde
-
substrate inhibition
7-(2-oxopropoxy)-2H-1-benzopyran-2-one
6.7% inhibition at 0.01 mM
-
7-methoxy-4-methyl-2H-1-benzopyran-2-one
5.2% inhibition at 0.01 mM
-
8,9-dimethyl-2,3-dihydrocyclopenta[c]furo[3,2-g][1]benzopyran-4(1H)-one
91.75% inhibition at 0.01 mM
-
8-[[4-(3-furoyl)-1-piperazinyl]methyl]-1,3-dimethyl-7-(3-methylbutyl)-3,7-dihydro-1H-purine-2,6-dione
i.e. CM026
-
9,10-dimethyl-1,2,3,4-tetrahydro-5H-6,8-dioxacyclopenta[b]phenanthren-5-one
83.7% inhibition at 0.01 mM
-
9,10-dimethyl-5H-6,8-dioxacyclopenta[b]phenanthren-5-one
57.8% inhibition at 0.01 mM
-
adenosine 5'-monophosphate
-
competitive with NAD+ and noncompetitive with acetaldehyde
arsenite
-
47% residual activity at 1 mM arsenite at pH 9.5, 28% residual activity at 2 mM arsenite at pH 7.4
BaCl2
-
0.1 mM, 10% inhibition of cytosolic enzyme
Butanal
-
substrate inhibition
c-Jun N-terminal protein kinase
incubation with catalytically active JNK leads to significant inhibition of ALDH2 activity. CCl4 exposure activates JNK which translocates to mitochondria and phosphorylates ALDH2 contributing to inhibition of ALDH2 activity
-
Ca2+
-
0.4 mM, 50% inhibition
Chloroacetaldehyde
-
86% residual activity at 1 mM chloroacetaldehyde at pH 9.5
Chlorpropamide
-
this inhibition may play a role in cataract formation in patients maintained on systemic corticosteroids and in tablet-dependent diabetics
CsCl2
-
0.1 mM, 19% inhibition of cytosolic enzyme
cyclohexanal
-
substrate inhibition at elevated aldehyde concentration, increase of NAD+ concentration from 0.85 mM to 2.55 mM removes substrate inhibition
D-glyceraldehyde
-
substrate inhibition
deoxycorticosterone
-
this inhibition may play a role in cataract formation in patients maintained on systemic corticosteroids and in tablet-dependent diabetics
diethylaminobenzaldehyde
0.025 mM diethylaminobenzaldehyde inhibits about 80% of the enzymatic activity
dimethyl ampal thiolester
-
78% inhibition of isozyme ALDH1 at 0.0075 mM
Fe3+
-
complete inhibition at 1 mM
formaldehyde
-
substrate inhibition
glyceraldehyde
-
substrate inhibition
harman
-
18% inhibition at 0.1 mM
hexanal
-
substrate inhibition
Indole-3-acetaldehyde
-
substrate inhibition at elevated aldehyde concentration, increase of NAD+ concentration from 0.85 mM to 2.55 mM removes substrate inhibition
iodacetamide
10-20% inhibition at 1 mM
Iodosobenzoate
-
0.1 mM, 3 min, complete inhibition
Isobutanal
-
substrate inhibition
K+
-
95.3% residual activity at 1 mM
KCN
10-20% inhibition at 1 mM
Kynurenic acid
-
40% inhibition at 0.002 mM
kynurenine
-
24% inhibition at 0.1 mM
m-methylbenzaldehyde
-
substrate inhibition
methyl 2-[(4-methyl-2-oxo-2H-1-benzopyran-7-yl)oxy]propanoate
-
-
methyl ampal thiolester
-
32% inhibition of isozyme ALDH1 at 0.0075 mM
methylglyoxal
-
substrate inhibition
Mn2+
-
84.8% residual activity at 1 mM
molinate
-
irreversible inhibition of ALDH2
molinate sulfoxide
-
i.e. S-ethyl-hexahydro-1H-azepine-1-carbothioate sulfoxide, irreversible inhibition of ALDH2
N'-methylnicotinamide
-
-
N,N-diethylaminobenzaldehyde
-
DEAB, complete inhibition
-
N-(2-(trifluoromethyl)benzyl)-N-(1,3-dimethyl-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)-3-(4-(4-isopropylbenzoyl)piperazin-1-yl)propanamide
-
-
N-(2-chlorobenzyl)-N-(1,3-dimethyl-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)-3-(4-(4-isopropylbenzoyl)piperazin-1-yl)propanamide
-
-
N-(2-fluorobenzyl)-N-(1,3-dimethyl-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)-3-(4-(4-isopropylbenzoyl)piperazin-1-yl)propanamide
-
-
N-(2-methoxybenzyl)-N-(1,3-dimethyl-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)-3-(4-(4-isopropylbenzoyl)piperazin-1-yl)propanamide
-
-
N-(2-methylbenzyl)-N-(1,3-dimethyl-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)-3-(4-(4-isopropylbenzoyl)piperazin-1-yl)propanamide
-
-
N-(3-(trifluoromethyl)benzyl)-N-(1,3-dimethyl-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)-3-(4-(4-isopropylbenzoyl)piperazin-1-yl)propanamide
-
-
N-(3-chlorobenzyl)-N-(1,3-dimethyl-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)-3-(4-(4-isopropylbenzoyl)piperazin-1-yl)propanamide
-
-
N-(3-fluorobenzyl)-N-(1,3-dimethyl-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)-3-(4-(4-isopropylbenzoyl)piperazin-1-yl)propanamide
-
-
N-(3-methoxybenzyl)-N-(1,3-dimethyl-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)-3-(4-(4-isopropylbenzoyl)piperazin-1-yl)propanamide
-
-
N-(3-methylbenzyl)-N-(1,3-dimethyl-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)-3-(4-(4-isopropylbenzoyl)piperazin-1-yl)propanamide
-
-
N-benzyl-3-(2,3,5-trimethyl-7-oxo-7H-furo[3,2-g][1]benzopyran-6-yl)propanamide
30.2% inhibition at 0.01 mM
-
NiCl2
-
0.1 mM, 24% inhibition of cytosolic enzyme
norharman
-
23% inhibition at 0.1 mM
o-nitrobenzaldehyde
-
substrate inhibition
p-hydroxyacetophenone
-
-
p-hydroxyphenylacetaldehyde
-
substrate inhibition at elevated aldehyde concentration, increase of NAD+ concentration from 0.85 mM to 2.55 mM removes substrate inhibition
p-methylbenzaldehyde
-
substrate inhibition
p-nitrocinnamaldehyde
-
substrate inhibition
p-nitrophenyl pivalate
-
inhibits dehydrogenase activity with propanal and D-glyceraldehyde
pentanal
-
substrate inhibition
pivaldehyde
-
substrate inhibition at elevated aldehyde concentration, increase of NAD+ concentration from 0.85 mM to 2.55 mM removes substrate inhibition
pyridine 3-aldehyde
-
substrate inhibition at elevated aldehyde concentration, increase of NAD+ concentration from 0.85 mM to 2.55 mM removes substrate inhibition
Semicarbazide hydrochloride
-
86.7% residual activity at 1 mM
Sodium bisulfite
-
1.8% residual activity at 1 mM
Tetraethylthiuram disulfide
-
disulfiram
xanthurenic acid
-
56% inhibition at 0.1 mM
[(4-methyl-2-oxo-2H-1-benzopyran-7-yl)oxy]acetonitrile
58.7% inhibition at 0.01 mM
-
[5-[3-(bromoacetyl)-pyridino]pentyl]diphosphoadenosine
-
-
1-propanol
-
-
1-propanol
7% inhibition at 1 mM
4-diethylaminobenzaldehyde
-
-
4-diethylaminobenzaldehyde
-
potent inhibitor
4-diethylaminobenzaldehyde
-
DEAB
acetaldehyde
-
0.02 mM, substrate inhibition of isoenzyme I, no inhibition of isoenzyme II and III
acetaldehyde
-
substrate inhibition
acetaldehyde
-
acetaldehyde inhibition of the enzyme is initiated below concentrations of 0.05 mM in the presence of 0.5 mM NAD or less
ADPribose
-
-
Ag+
-
complete inhibition at 1 mM
Ag+
-
complete inhibition at 1 mM
Alda-1
-
0.01 mM Alda-1 inhibits the apparent formaldehyde oxidation activity of the wild type enzyme by about 90%
Alda-1
-
acts as inhibitor at low concentrations of aldehyde
benomyl
-
benzaldehyde
-
substrate inhibition
benzaldehyde
-
substrate inhibition
Chloral hydrate
-
-
Chloral hydrate
-
competitive with aldehyde
Chloral hydrate
-
competitive with respect to acetaldehyde
Chloral hydrate
-
competitive inhibition of hydrolysis of p-nitrophenyl acetate, mixed inhibition with p-nitrophenyl pivalate
Chloral hydrate
-
inhibition of isoenzyme I and II from mitochondria and isoenzyme II from microsomes, no inhibition of isoenzyme I from microsomes
Co2+
-
50.3% residual activity at 1 mM
Co2+
-
complete inhibition at 1 mM
Co2+
-
89.01% residual activity at 1 mM
Cu2+
-
2.9% residual activity at 1 mM
Cu2+
-
complete inhibition at 1 mM
Cu2+
-
complete inhibition at 1 mM
Cu2+
-
0.1 mM CuSO4, 7% inhibition of microsomal enzyme, 81% inhibition of the cytosolic enzyme
cyanamide
-
-
cyanamide
-
complete inhibition at 0.5 mM
daidzin
-
-
Disulfiram
-
-
Disulfiram
-
38% inhibition at 0.05 mM, 93% inhibition at 0.1 mM
Disulfiram
-
non-competitive
Disulfiram
-
inhibition of isoenzyme III, isoenzyme I is extremely sensitive, isoenzyme II is totally insensitive
Disulfiram
-
strong inhibition of isoenzyme 1, no inhibition of isoenzyme 2
Disulfiram
0.01 mM; 0.01 mM; 0.01 mM; 0.01 mM
Disulfiram
-
at higher concentrations of propionaldehyde (0.5 and 1 mM), ALDH1B1 activity is inhibited by disulfiram, with the extent of inhibition being about 40% at 0.01 mM disulfiram
Disulfiram
0.025 mM diethylaminobenzaldehyde inhibits about 20-30% of the enzymatic activity
Disulfiram
-
no effect on microsomal enzyme, complete inhibition of the cytosolic enzyme
Disulfiram
-
inhibits activity of mitochondrial isoenzyme I with NAD+ and activity of isoenzyme I and II from microsomes and mitochondria with NADP+
Disulfiram
-
42% inhibition at 0.002 mM
Disulfiram
-
72% inhibition at 0.002 mM
EDTA
-
85.3% residual activity at 1 mM
EDTA
10-20% inhibition at 1 mM
ethanol
-
-
ethanol
-
chronic or binge ethanol-exposure significantly decreases ALDH1 activity via S-nitrosylation, activity is restored by addition of dithiothreitol, ALDH1 activity (using 0.015 mM propionaldehyde as a substrate) is significantly inhibited (by 61%) in chronically ethanol-fed rats
Fe2+
-
57.5% residual activity at 1 mM
Fe2+
-
26.34% residual activity at 1 mM
H2O2
-
-
Hg2+
-
complete inhibition at 1 mM
Hg2+
-
complete inhibition at 1 mM
indol-3-ylpyruvic acid
-
30% inhibition at 0.002 mM
indol-3-ylpyruvic acid
-
55% inhibition at 0.002 mM
iodoacetamide
-
0.1 mM
KCl
-
200 mM, 55% inhibition
KCl
-
0.1 mM, 16% inhibition
Li+
-
2.8% residual activity at 1 mM
Li+
-
90.64% residual activity at 1 mM
methanol
-
-
methanol
17% inhibition at 1 mM
Mg2+
-
80.6% residual activity at 1 mM
Mg2+
85% inhibition at 0.5 mM
Mg2+
70% inhibition at 0.2 mM; 85% inhibition at 0.5 mM
Mg2+
-
wild type enzyme activity is inhibited (64%) by Mg2+ at pH 7.4, whereas the GFP-tagged enzyme activity is not affected by Mg2+
Mg2+
-
93.64% residual activity at 1 mM
Mg2+
-
0.1 mM MgCl2, 63% inhibition of cytosolic enzyme
Mg2+
-
0.4 mM, 50% inhibition
Mg2+
Mg2+ ions suppresses (R)-trans-4-hydroxy-2-nonenal oxidation by ALDH5A to a greater extent than that of (S)-trans-4-hydroxy-2-nonenal
Na+
-
83.6% residual activity at 1 mM
Na+
-
89.17% residual activity at 1 mM
NAD+
-
pronounced inhibition occurs at above 5 mM
NAD+
-
0.1 mM, significant inhibition of esterase activity
NADH
-
competitive with respect to NAD+, non-competitive with respect to acetaldehyde
NADH
-
competitive with NAD+ at high and low concentrations of acetaldehyde, product inhibitor
NADH
-
product inhibition
NADH
-
while acetaldehyde alone (1.6 mM) as an inhibiting factor yields a relative rate around 38% of the maximum experimental rate, the result with 0.18 mM initial NADH is 13% of the maximum experimental rate and further declines to 6.5% at 0.4 mM NADH
NH3
-
79.8% residual activity at 1 mM
NH3
-
92.06% residual activity at 1 mM
Ni2+
-
72.4% residual activity at 1 mM
Ni2+
-
complete inhibition at 1 mM
Ni2+
-
89.54% residual activity at 1 mM
Ni2+
52% inhibition at 1 mM
nitroglycerin
intravenous nitroglycerin treatment inhibits ALDH-2 activity, activity can be restored using dithiothreitol
nitroglycerin
-
ALDH2 dehydrogenase activity is inhibited by about 50% by large doses of nitroglycerin
nitroglycerin
complete inhibition at 0.05 mM nitroglycerin which can be reversed by the addition of 0.4 mM dithiothreitol
nitroglycerin
-
exposure of ALDH2 to nitroglycerin results in mechanism-based oxidative inactivation of the enzyme that is partially reversed by dithiothreitol
nitroglycerin
-
more than half of the original activity retained in the presence of 5.5 mM and approximate 80% of the activity is lost by the addition of 11 mM nitroglycerin
p-hydroxymercuribenzoate
-
-
p-hydroxymercuribenzoate
-
0.1 mM, 3 min, complete inhibition
p-hydroxymercuribenzoate
-
-
p-hydroxymercuribenzoate
-
0.05 mM, potent inhibition of isoenzyme I from microsomes and mitochondria, isoenzyme II from microsomes and mitochondria is less sensitive
p-hydroxymercuribenzoate
complete inhibition at 0.1 mM
p-nitrobenzaldehyde
-
substrate inhibition
p-nitrobenzaldehyde
-
substrate inhibition at elevated aldehyde concentration, increase of NAD+ concentration from 0.85 mM to 2.55 mM removes substrate inhibition
PCMB
-
-
progesterone
-
this inhibition may play a role in cataract formation in patients maintained on systemic corticosteroids and in tablet-dependent diabetics
propanal
-
substrate inhibition
propanal
-
competitive inhibition of hydrolysis of p-nitrophenyl acetate, mixed inhibition with p-nitrophenyl pivalate
thio-NAD+
-
-
Zn2+
-
7% residual activity at 1 mM
Zn2+
-
35.91% residual activity at 1 mM
Zn2+
73% inhibition at 1 mM
additional information
-
EDTA has no effect on ALDH activity
-
additional information
-
inclusion of protease inhibitors, 1 mM benzamidine and 1 mM phenylmethylsulfonyl fluoride, in preparation of homogenate supernatants slightly inhibit ALDH activity
-
additional information
-
at the lowest concentration of substrate tested (propionaldehyde 0.1 mM), ALDH1B1 is not affected by disulfiram
-
additional information
-
activities of isoforms ALDH2 and ALDH3A1 are unaffected by pentachlorophenol (up to a concentration of 1 mM)
-
additional information
-
not influenced by acetaldehyde
-
additional information
design, synthesis of 1,3-dimethylpyrimidine-2,4-diones as potent and selective aldehyde dehydrogenase 1A1 (ALDH1A1, EC 1.2.1.36) inhibitors and comparison of inhibitory activities on different ALDH isozymes, overview
-
additional information
inhibition of the aldehyde dehydrogenase 1/2 family by psoralen and coumarin derivatives, structure-function relationships, overview. Poor or no inhibition by 4-methyl-7-(2-oxopropoxy)-2H-1-benzopyran-2-one, 2-[(4-methyl-2-oxo-2H-1-benzopyran-7-yl)oxy]propanoic acid, 2H-furo[2,3-h][1]benzopyran-2-one, 4-methyl-7-(2-oxo-2-phenylethoxy)-2H-1-benzopyran-2-one, 2-[(4-methyl-2-oxo-2H-1-benzopyran-7-yl)oxy]-N-phenylacetamide, 7-(diethylamino)-4-methyl-2H-1-benzopyran-2-one, 3-benzyl-4-methyl-2-oxo-2H-1-benzopyran-7-yl methanesulfonate, and N-(4,7-dimethyl-2-oxo-2H-1-benzopyran-6-yl)-2-methylpropanamide; inhibition of the aldehyde dehydrogenase 1/2 family by psoralen and coumarin derivatives, structure-function relationships, overview. Poor or no inhibition by 7-(diethylamino)-4-methyl-2H-1-benzopyran-2-one and 6-bromo-3-[(1E)-N-hydroxyethanimidoyl]-2H-1-benzopyran-2-one
-
additional information
inhibition of the aldehyde dehydrogenase 1/2 family by psoralen and coumarin derivatives, structure-function relationships, overview. Poor or no inhibition by 4-methyl-7-(2-oxopropoxy)-2H-1-benzopyran-2-one, 2-[(4-methyl-2-oxo-2H-1-benzopyran-7-yl)oxy]propanoic acid, 2H-furo[2,3-h][1]benzopyran-2-one, 4-methyl-7-(2-oxo-2-phenylethoxy)-2H-1-benzopyran-2-one, 2-[(4-methyl-2-oxo-2H-1-benzopyran-7-yl)oxy]-N-phenylacetamide, 7-(diethylamino)-4-methyl-2H-1-benzopyran-2-one, 3-benzyl-4-methyl-2-oxo-2H-1-benzopyran-7-yl methanesulfonate, and N-(4,7-dimethyl-2-oxo-2H-1-benzopyran-6-yl)-2-methylpropanamide; inhibition of the aldehyde dehydrogenase 1/2 family by psoralen and coumarin derivatives, structure-function relationships, overview. Poor or no inhibition by 7-(diethylamino)-4-methyl-2H-1-benzopyran-2-one and 6-bromo-3-[(1E)-N-hydroxyethanimidoyl]-2H-1-benzopyran-2-one
-
additional information
-
substrate inhibition by aromatic aldehydes
-
additional information
-
not inhibited by rotenone
-
additional information
-
Durio zibethinus Murray fruit extract
-
additional information
-
at low coenzyme concentrations, below 0.005 mM, and high aldehyde concentrations substrate inhibition of oxidation rates is observed
-
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0.023
(3,4-dihydroxyphenyl)(hydroxy)acetaldehyde
-
membrane-bound isoenzyme ALDH
0.001
(R)-trans-4-hydroxy-2-nonenal
ALDH2, in 40 mM sodium phosphate buffer (pH 7.4), at 37°C
0.0007
(S)-trans-4-hydroxy-2-nonenal
ALDH2, in 40 mM sodium phosphate buffer (pH 7.4), at 37°C
0.0358
1,N6-ethenoadenine dinucleotide
-
isoenzyme E3
0.00015 - 0.0016
1-formyl-6-methylpyrene
0.000027 - 0.004
1-formyl-8-methylpyrene
0.0009 - 0.004
1-formylpyrene
0.0000032
2,4-dinitrobenzaldehyde
-
enzyme ALDH-2
0.00038 - 0.011
2-formylpyrene
0.000008 - 0.00046
2-naphthaldehyde
0.00024
2-naphthalene carboxylate
-
apparent Km value, diphosphate buffer, pH 8.1, cofactor NADH
0.0053
2-nonenal
-
pH and temperature not specified in the publication
0.0005 - 0.017
3,4-dihydroxyphenyl acetaldehyde
0.0004 - 0.0042
3,4-dihydroxyphenylacetaldehyde
0.00033
3,4-dimethoxybenzaldehyde
-
enzyme ALDH-2
0.022
3-acetylpyridine-NAD+
-
-
0.29 - 0.49
3-hydroxypropionaldehyde
0.12
3-hydroxypropionic acid
-
with NADH as cofactor, in 50 mM potassium phosphate buffer (pH 8.0), at 37°C
3.3
3-oxopropyl phosphonate
wild type enzyme, at pH 7.5 and 30°C
0.00196
3-Pyridinecarboxaldehyde
-
enzyme ALDH-2
0.0001 - 0.0003
4-(dimethylamino)cinnamaldehyde
0.005 - 0.014
4-aminobutyrate
0.014
4-cyanobenzaldehyde
-
-
0.0042
4-Dimethylaminobenzaldehyde
-
recombinant ALDH3A1
0.00004 - 0.00078
4-formylpyrene
3.383
4-hydroxy-2-nonenal
-
at 25°C, pH not specified in the publication
0.155
4-hydroxy-3-methoxybenzaldehyde
-
recombinant ALDH3A1
0.0021 - 0.0403
4-hydroxynonenal
0.000065
4-methoxy-1-naphthaldehyde
-
enzyme ALDH-2
0.019
4-methoxybenzaldehyde
-
recombinant ALDH3A1
0.0002
4-methyoxy-1-naphthaldehyde
-
enzyme ALDH-1
0.0043
4-nitrophenyl acetate
-
-
0.0000063
5-(dimethylamino)-2-naphthaldehyde
-
enzyme ALDH-1
0.0000004 - 0.0000025
5-bromo-1-naphthaldehyde
0.026
5-hydroxyindol acetaldehyde
-
membrane-bound isoenzyme ALDH
0.0189
5-methoxyindole-3-carboxaldehyde
-
enzyme ALDH-2
0.0000004 - 0.000011
5-nitro-1-naphthaldehyde
0.00069
6,7-dimethoxycoumarin-3-carboxaldehyde
-
enzyme ALDH-2
0.0000023
6-(dimethylamino)-2-naphthaldehyde
-
enzyme ALDH-2
0.0017 - 0.02
6-dimethylamino-2-naphthaldehyde
0.00016 - 0.0002
6-methoxy-2-naphthaldehyde
0.0054
6-methoxy-2-quinolinone-4-carboxaldehyde
-
enzyme ALDH-2
0.00213
7-(dimethylamino)-2-quinolinone-4-carboxaldehyde
-
enzyme ALDH-2
0.000062
7-(dimethylamino)-coumarin-3-carboxaldehyde
-
enzyme ALDH-2
0.00006
7-acetoxycoumarin-3-carboxaldehyde
-
enzyme ALDH-2
0.15
7-hydroxycoumarin-3-carboxaldehyde
-
enzyme ALDH-2
0.05
7-methoxy-2-quinolinone-4-carboxaldehyde
-
enzyme ALDH-2
0.00028
7-methoxycoumarin-3-carboxaldehyde
-
enzyme ALDH-2
0.00005 - 80
acetaldehyde
0.017
acetylaldehyde
-
at substrate concentrations 0-0.07 mM
0.009
acrolein
-
wild type isoform ALDH1A1, in 100 mM sodium diphosphate (pH 9.5), at 25°C
0.0093
all-trans-retinal
-
at pH 8.0 and 25°C
0.064 - 0.63
alpha-aminoadipate semialdehyde
0.00093
alpha-phenylpropanal
-
enzyme ALDH-2
0.000018 - 50
benzaldehyde
0.0411 - 0.26
Betaine aldehyde
0.0234
betaNAD+
-
isoenzyme E3
0.26 - 1.74
Butyraldehyde
0.00055
cinnamaldehyde
-
-
0.006
cinnamic aldehyde
-
recombinant ALDH3A1
1.136
D-glyceraldehyde
-
-
8.51
DL-glyceraldehyde
-
in 50 mM Tris/HCl, at pH 8.0 and 80°C
6.12
DL-glyceraldehyde 3-phosphate
-
in 50 mM Tris/HCl, at pH 8.0 and 80°C
0.000054
fluorene-2-carboxaldehyde
-
enzyme ALDH-1
0.0009 - 0.56
Glutaraldehyde
0.183
glutathione-4-oxonon-2-enal
-
-
0.17 - 7.374
glyceraldehyde
0.097 - 0.372
glyceraldehyde 3-phosphate
0.046
glycoaldehyde
-
isoenzyme 2, pH 7.4
0.005 - 0.69
glycolaldehyde
0.000018 - 0.035
Heptanal
2.9
hexanaldehyde
at pH 8.0 and 21°C
0.0005
hydrocinnamaldehyde
-
enzyme ALDH-2
0.0007 - 0.001
indole 3-acetaldehyde
0.00015 - 0.002
Indole-3-acetaldehyde
0.01 - 0.02
Indole-3-aldehyde
-
enzyme ALDH-2
0.21 - 0.68
Isovaleraldehyde
0.00009
m-methoxybenzaldehyde
-
enzyme ALDH-2
0.000018
m-methylbenzaldehyde
-
enzyme ALDH-2
0.0043 - 0.466
malondialdehyde
0.0086 - 1.876
methylglyoxal
0.043
Monochloroacetaldehyde
-
-
0.11
N-acetyl-4-aminobutyrate
-
enzyme from liver
0.944
N-guanine dinucleotide
-
isoenzyme E3
0.0008 - 0.0285
n-nonanal
0.088
NADH
-
at pH 7.0 and 55°C
0.0008
o-methoxybenzaldehyde
-
enzyme ALDH-2
1.3
o-methylbenzaldehyde
-
enzyme ALDH-2
0.0000063
o-nitrobenzaldehyde
-
enzyme ALDH-2
0.172
oxidized nicotinamide hypoxanthine dinucleotide
-
isoenzyme E3
0.00002
p-(dimethylamino)-benzaldehyde
-
enzyme ALDH-2
0.00006
p-(dimethylamino)benzaldehyde
-
enzyme ALDH-1
0.000005 - 0.00142
p-(dimethylamino)cinnamaldehyde
0.024
p-Carboxybenzaldehyde
-
-
0.000018 - 0.0004
p-Methoxybenzaldehyde
0.000017
p-methylbenzaldehyde
-
enzyme ALDH-2
0.000007 - 2
p-nitrobenzaldehyde
0.0000007
p-nitrocinnamaldehyde
-
enzyme ALDH-2
0.000034 - 0.006
pentanal
2.2
pentanaldehyde
at pH 8.0 and 21°C
0.000004
phenanthrene-9-carboxaldehyde
-
enzyme ALDH-2
0.000029 - 0.027
phenylacetaldehyde
0.0032 - 0.5
phosphonoacetaldehyde
0.0028 - 12
propionaldehyde
0.013
Pyruvic aldehyde
-
-
0.00033
quinoline-3-carboxaldehyde
-
enzyme ALDH-2
0.0028
quinoline-4-carboxaldehyde
-
enzyme ALDH-2
0.69 - 3.54
Succinic semialdehyde
0.18 - 0.199
trans-2-hexenal
0.003 - 0.0322
trans-2-nonenal
0.000035 - 0.0004
trans-cinnamaldehyde
0.14 - 0.24
Valeraldehyde
additional information
additional information
-
0.00015
1-formyl-6-methylpyrene
ALDH2, at pH 7.5 and 37°C
0.0016
1-formyl-6-methylpyrene
in 0.1 M sodium diphosphate buffer (pH 8.5), at ambient temperature
0.000027
1-formyl-8-methylpyrene
ALDH2, at pH 7.5 and 37°C
0.004
1-formyl-8-methylpyrene
in 0.1 M sodium diphosphate buffer (pH 8.5), at ambient temperature
0.0009
1-formylpyrene
ALDH2, at pH 7.5 and 37°C
0.004
1-formylpyrene
in 0.1 M sodium diphosphate buffer (pH 8.5), at ambient temperature
0.00038
2-formylpyrene
ALDH2, at pH 7.5 and 37°C
0.011
2-formylpyrene
in 0.1 M sodium diphosphate buffer (pH 8.5), at ambient temperature
0.000008
2-naphthaldehyde
-
enzyme ALDH-2
0.0004
2-naphthaldehyde
-
recombinant ALDH3A1
0.00046
2-naphthaldehyde
-
salivary ALDH
0.0005
3,4-dihydroxyphenyl acetaldehyde
-
isoenzyme II
0.001
3,4-dihydroxyphenyl acetaldehyde
-
pH 7.1, isoenzyme 2
0.003
3,4-dihydroxyphenyl acetaldehyde
-
isoenzyme III
0.017
3,4-dihydroxyphenyl acetaldehyde
-
membrane-bound isoenzyme ALDH
0.0004
3,4-dihydroxyphenylacetaldehyde
isozyme ALDH1A1 from liver
0.001
3,4-dihydroxyphenylacetaldehyde
isozyme ALDH2 from liver
0.0042
3,4-dihydroxyphenylacetaldehyde
isozyme ALDH1A1 from brain
0.29
3-hydroxypropionaldehyde
-
with NADP+ as cofactor, in 50 mM potassium phosphate buffer (pH 8.0), at 37°C
0.48
3-hydroxypropionaldehyde
-
recombinant enzyme, in 50 mM potassium phosphate buffer, at pH 8.0 and 45°C
0.49
3-hydroxypropionaldehyde
-
with NAD+ as cofactor, in 50 mM potassium phosphate buffer (pH 8.0), at 37°C
0.0001
4-(dimethylamino)cinnamaldehyde
-
native enzyme
0.0003
4-(dimethylamino)cinnamaldehyde
-
mutant enzyme S74A
0.005
4-aminobutyrate
-
enzyme from liver
0.007
4-aminobutyrate
-
enzyme from brain
0.008
4-aminobutyrate
-
minor component of enzyme E3, pH 7.4
0.014
4-aminobutyrate
-
major component of enzyme E3, pH 7.4
0.00004
4-formylpyrene
ALDH2, at pH 7.5 and 37°C
0.00078
4-formylpyrene
in 0.1 M sodium diphosphate buffer (pH 8.5), at ambient temperature
0.0021
4-hydroxynonenal
-
pH 8.0, 25°C
0.0179
4-hydroxynonenal
-
pH 8.0, 25°C
0.0403
4-hydroxynonenal
-
in 100 mM sodium diphosphate, at pH 8.0 and 22°C
0.0000004
5-bromo-1-naphthaldehyde
-
enzyme ALDH-2
0.0000025
5-bromo-1-naphthaldehyde
-
enzyme ALDH-1
0.0000004
5-nitro-1-naphthaldehyde
-
enzyme ALDH-2
0.000011
5-nitro-1-naphthaldehyde
-
enzyme ALDH-1
0.0017
6-dimethylamino-2-naphthaldehyde
-
apparent Km value, pyrophosphate buffer, pH 8.1, cofactor NAD+
0.0072
6-dimethylamino-2-naphthaldehyde
-
salivary ALDH
0.0079
6-dimethylamino-2-naphthaldehyde
-
apparent Km value, phosphate buffer, pH 7.3, cofactor NAD+
0.0086
6-dimethylamino-2-naphthaldehyde
-
apparent Km value, phosphate buffer, pH 6.2, cofactor NAD+
0.0114
6-dimethylamino-2-naphthaldehyde
-
apparent Km value, phosphate buffer, pH 8.0, cofactor NAD+
0.02
6-dimethylamino-2-naphthaldehyde
-
recombinant ALDH3A1
0.00016
6-methoxy-2-naphthaldehyde
-
recombinant ALDH3A1
0.0002
6-methoxy-2-naphthaldehyde
-
salivary ALDH
0.00005
acetaldehyde
-
major component of enzyme E3
0.0001
acetaldehyde
-
isoenzyme 1
0.0002
acetaldehyde
-
isoenzyme F2
0.00031
acetaldehyde
-
pH 9.5
0.00036
acetaldehyde
-
pH 7.5
0.0004
acetaldehyde
-
native enzyme
0.0004
acetaldehyde
ALDH2, in 40 mM sodium phosphate buffer (pH 7.4), at 37°C
0.00048
acetaldehyde
ALDH2, at pH 7.5 and 37°C
0.00065
acetaldehyde
-
pH 8.0, 25°C, wild-type enzyme
0.002
acetaldehyde
-
pH 9.0, isoenzyme E2
0.002 - 0.003
acetaldehyde
-
isoenzyme 2
0.0024
acetaldehyde
-
isoenzyme 2, pH 9.5
0.0027
acetaldehyde
-
mutant enzyme S74A
0.003
acetaldehyde
-
isoenzyme 2, pH 7.0
0.003
acetaldehyde
-
isoenzyme E2
0.003
acetaldehyde
-
pH 7.4, isoenzyme E2
0.0032
acetaldehyde
0.1 M sodium diphosphate pH 8.0, 1 mM NAD+, 50 mM 2-mercaptoethanol, 1 mM pyrazole, 30 min, 25°C
0.0035
acetaldehyde
-
isoenzyme ALDH2 from normal liver
0.005
acetaldehyde
-
isoenzyme ALDH-II
0.0066
acetaldehyde
-
in 50 mM KH2PO4-K2HPO4 buffer (pH 8.0), at 60°C
0.00879
acetaldehyde
-
pH 8.0, 25°C, heteromeric enzyme obtained by coexpression of ALDH2 and ALDH2(2) in Escherichia coli
0.009
acetaldehyde
-
pH 9.5
0.01
acetaldehyde
-
100 mM Na2HPO4, pH 7.4, 100 mM NaCl, 1 mM NAD+, 25°C
0.0115
acetaldehyde
-
0.1 M sodium diphosphate pH 8.0, 1 mM NAD+, 50 mM 2-mercaptoethanol, 1 mM pyrazole, 30 min, 25°C
0.022
acetaldehyde
-
isoenzyme ALDH1 from normal liver
0.02573
acetaldehyde
-
pH 8.0, 25°C, mutant enzyme ALDH2(2)
0.03
acetaldehyde
-
isoenzyme E1
0.04
acetaldehyde
-
enzyme from brain
0.048
acetaldehyde
-
isoenzyme III
0.05
acetaldehyde
-
enzyme from liver
0.055
acetaldehyde
-
at 25°C, pH not specified in the publication
0.07
acetaldehyde
-
isoenzyme F1
0.12
acetaldehyde
-
isoenzyme 1, pH 9.5
0.18
acetaldehyde
-
enzyme form ALDH-1, pH 9.5
0.18
acetaldehyde
-
enzyme ALDH-1, pH 7.5
0.2
acetaldehyde
-
enzyme ALDH-2, pH 9.5
0.22
acetaldehyde
-
isoenzyme ALDH-I
0.83
acetaldehyde
-
at substrate concentrations 0.8-20 mM
1
acetaldehyde
-
with NAD+ as cofactor, in 50 mM potassium phosphate buffer (pH 8.0), at 37°C
1.6
acetaldehyde
-
at pH 7.0 and 55°C
2.4
acetaldehyde
-
enzyme I from microsome
2.4
acetaldehyde
-
at pH 8.0 and 25°C
2.5
acetaldehyde
-
isoenzyme 1, pH 7.0
5.16
acetaldehyde
at pH 8.0 and 21°C
5.8
acetaldehyde
ALDH5A, in 40 mM sodium phosphate buffer (pH 7.4), at 37°C
6.38
acetaldehyde
-
in 50 mM Tris/HCl, at pH 8.0 and 80°C
10
acetaldehyde
-
membrane-bound isoenzyme ALDH
80
acetaldehyde
in 0.1 M sodium diphosphate buffer (pH 8.5), at ambient temperature
0.064
alpha-aminoadipate semialdehyde
-
pH 8.0, 26°C, recombinant wild-type enzyme
0.169
alpha-aminoadipate semialdehyde
-
pH and temperature not specified in the publication
0.63
alpha-aminoadipate semialdehyde
-
pH 8.0, 26°C, recombinant mutant A505P
0.000018
benzaldehyde
-
enzyme ALDH-2
0.00006
benzaldehyde
-
pH 9.5
0.0001
benzaldehyde
-
native enzyme
0.0002
benzaldehyde
-
mutant enzyme S74A
0.0399
benzaldehyde
-
at 25°C and pH 8.5, with NADP+ as the electron acceptor
0.05
benzaldehyde
-
at 25°C, pH not specified in the publication
0.0634
benzaldehyde
-
at 25°C and pH 8.5, with NAD+ as the electron acceptor
0.148
benzaldehyde
-
recombinant ALDH3A1
0.15
benzaldehyde
-
100 mM Na2HPO4, pH 7.4, 100 mM NaCl, 1 mM NAD+, 25°C
0.16
benzaldehyde
-
salivary ALDH
0.23
benzaldehyde
in 0.1 M sodium diphosphate buffer (pH 8.5), at ambient temperature
0.5302
benzaldehyde
-
pH and temperature not specified in the publication
1.3
benzaldehyde
-
phenobarbital-inducible enzyme
1.6
benzaldehyde
-
enzyme I from mitochondria
3
benzaldehyde
-
enzyme II from microsomes
5.37
benzaldehyde
-
with NADP+ as cofactor, in 50 mM potassium phosphate buffer (pH 8.0), at 37°C
5.9
benzaldehyde
-
enzyme I from microsomes
50
benzaldehyde
-
enzyme II from mitochondria
0.0411
Betaine aldehyde
-
pH and temperature not specified in the publication
0.09
Betaine aldehyde
-
minor component of enzyme E3, pH 7.4
0.14
Betaine aldehyde
-
enzyme from brain
0.26
Betaine aldehyde
-
enzyme from liver
0.26
Betaine aldehyde
-
major component of enzyme form E3, pH 7.4
0.00019
Butanal
-
-
0.0007
Butanal
-
native enzyme
0.002
Butanal
-
mutant enzyme S74A
0.0038
Butanal
1 mM NAD+, 0,05 mM substrate, 250 mM sodium bicarbonate-NaOH buffer pH 10.0, 37°C
0.26
Butyraldehyde
-
recombinant enzyme, in 50 mM potassium phosphate buffer, at pH 8.0 and 45°C
0.97
Butyraldehyde
-
with NAD+ as cofactor, in 50 mM potassium phosphate buffer (pH 8.0), at 37°C
1.74
Butyraldehyde
at pH 8.0 and 21°C
0.0000029
decanal
-
enzyme form ALDH-1, pH 9.5
0.000022
decanal
-
enzyme form ALDH-2, pH 9.5
0.005
dodecanal
-
in 100 mM sodium diphosphate, at pH 8.0 and 22°C
0.02
dodecanal
-
microsomal enzyme
0.031
formaldehyde
-
-
0.178
formaldehyde
-
native enzyme
0.32
formaldehyde
-
enzyme ALDH-2
0.333
formaldehyde
1 mM NAD+, 0,05 mM substrate, 250 mM sodium bicarbonate-NaOH buffer pH 10.0, 37°C
0.42
formaldehyde
ALDH2, at pH 7.5 and 37°C
0.7
formaldehyde
-
mutant enzyme S74A
0.0009
Glutaraldehyde
-
native enzyme
0.003
Glutaraldehyde
-
mutant enzyme S74A
0.0062
Glutaraldehyde
-
isoenzyme ALDH-II
0.05
Glutaraldehyde
-
isoenzyme ALDH-I
0.56
Glutaraldehyde
-
membrane-bound isoenzyme ALDH
0.17
glyceraldehyde
-
D-glyceraldehyde, L-glyceraldehyde, DL-glyceraldehyde
0.595
glyceraldehyde
-
wild type isoform ALDH1A1, in 100 mM sodium diphosphate (pH 9.5), at 25°C
7.374
glyceraldehyde
-
pH and temperature not specified in the publication
0.097
glyceraldehyde 3-phosphate
wild type enzyme, at pH 7.5 and 30°C
0.372
glyceraldehyde 3-phosphate
-
-
0.005
glycolaldehyde
-
isoenzyme I
0.021
glycolaldehyde
-
isoenzyme II
0.038
glycolaldehyde
-
native enzyme
0.077
glycolaldehyde
-
mutant enzyme S74A
0.11
glycolaldehyde
-
isoenzyme III
0.2
glycolaldehyde
-
enzyme from brain
0.24
glycolaldehyde
-
enzyme from liver
0.000018
Heptanal
-
enzyme form ALDH-1, pH 9.5
0.000027
Heptanal
-
enzyme form ALDH-2, pH 9.5
0.035
Heptanal
-
microsomal enzyme
0.00003
hexanal
-
enzyme form ALDH-2, pH 9.5
0.000041
hexanal
-
enzyme form ALDH-1, pH 9.5
0.0004
hexanal
-
at 25°C, pH not specified in the publication
0.0008
hexanal
-
native enzyme
0.0018
hexanal
1 mM NAD+, 0,05 mM substrate, 250 mM sodium bicarbonate-NaOH buffer pH 10.0, 37°C
0.0024
hexanal
-
mutant enzyme S74A
0.0035
hexanal
-
pH 8.0, 25°C
0.0134
hexanal
-
pH 8.0, 25°C
0.0213
hexanal
-
pH 8.0, 22°C, recombinant wild-type enzyme
0.0391
hexanal
-
pH and temperature not specified in the publication
0.071
hexanal
wild type enzyme, at pH 8.0 and 25°C
0.071
hexanal
-
in 100 mM sodium diphosphate, at pH 8.0 and 22°C
0.072
hexanal
mutant enzyme E149T/V178R/I200V, at pH 8.0 and 25°C
0.0007
indole 3-acetaldehyde
-
isoenzyme I
0.001
indole 3-acetaldehyde
-
isoenzyme III
0.00015
Indole-3-acetaldehyde
-
enzyme ALDH-2
0.00031
Indole-3-acetaldehyde
-
enzyme ALDH-1
0.002
Indole-3-acetaldehyde
-
-
0.03
Isobutanal
-
-
0.21
Isovaleraldehyde
-
recombinant enzyme, in 50 mM potassium phosphate buffer, at pH 8.0 and 45°C
0.68
Isovaleraldehyde
-
with NAD+ as cofactor, in 50 mM potassium phosphate buffer (pH 8.0), at 37°C
0.0043
malondialdehyde
-
wild type isoform ALDH1A1, in 100 mM sodium diphosphate (pH 9.5), at 25°C
0.014
malondialdehyde
-
pH 8.0, 25°C
0.1144
malondialdehyde
-
pH 8.0, 25°C
0.466
malondialdehyde
-
at 25°C, pH not specified in the publication
0.0086
methylglyoxal
-
pH 7.4, isoenzyme E2
0.021
methylglyoxal
-
pH 9.0, isoenzyme E2
0.552
methylglyoxal
-
minor component of enzyme form E3, pH 7.4
0.586
methylglyoxal
-
major component of enzyme form E3, pH 7.4
0.958
methylglyoxal
-
minor component of enzyme form E3, pH 9.0
1.876
methylglyoxal
-
major component of enzyme form E3, pH 9.0
0.0008
n-nonanal
-
at 25°C, pH not specified in the publication
0.0285
n-nonanal
-
pH and temperature not specified in the publication
0.0003
NAD+
50 mM sodium phosphate buffer, pH 7.4, 0.2 mM Mg2+,0.14 mM propanal, 25°C
0.0012
NAD+
-
apparent Km value
0.0017
NAD+
-
pH 7.5, 25°C, mutant enzyme S82A
0.0019
NAD+
-
reaction with propanal
0.0023
NAD+
-
enzyme from promotion phase of hepatocarcinogenesis
0.0026
NAD+
-
reaction with butanal
0.003
NAD+
-
reaction with propanal
0.003
NAD+
-
isoenzyme F1
0.0035
NAD+
-
pH 7.5, 25°C, mutant enzyme D80G
0.0036
NAD+
50 mM sodium phosphate buffer, pH 7.4, 0.25 mM Mg2+,0.14 mM propanal, 25°C
0.0036
NAD+
-
at 25°C, pH not specified in the publication
0.004
NAD+
-
brain enzyme
0.004
NAD+
-
native enzyme, pH 7.4
0.004
NAD+
-
pH 7.5, 25°C, mutant enzyme R84Q
0.005
NAD+
-
isoenzyme ALDH1
0.0062
NAD+
50 mM sodium phosphate buffer, pH 7.4, 0.14 mM propanal, 25°C
0.0077
NAD+
-
phenobarbital-inducible enzyme
0.008
NAD+
-
isoenzyme 1, pH 9.5
0.008
NAD+
-
pH 7.5, 25°C, mutant enzyme ALDH1-5AA
0.01
NAD+
-
native enzyme, reaction with propanal
0.011
NAD+
-
pH 7.5, 25°C, wild-type enzyme
0.011
NAD+
-
wild type isoform ALDH1A1, in 100 mM sodium diphosphate (pH 9.5), at 25°C
0.0125
NAD+
-
cytoplasmic isoenzyme
0.014
NAD+
-
enzyme from liver
0.014 - 0.015
NAD+
-
reaction with 4-aminobutyraldehyde
0.0145
NAD+
50 mM sodium phosphate buffer, pH 7.4, 0.14 mM propanal, 25°C
0.016
NAD+
-
isoenzyme ALDH2
0.018
NAD+
mutant enzyme R108A, with NAD+ in 50 mM HEPES, pH 7.5 supplemented with 10 mM MgSO4 for 5 min at 30°C
0.018
NAD+
mutant enzyme R108A, with phosphonoacetaldehyde as cosubstrate, at pH 7.5 and 30°C
0.022
NAD+
-
reaction with propanal, enzyme II from mitochondria
0.022
NAD+
-
pH 7.5, 25°C, mutant enzyme ALDH1-H3tail
0.03
NAD+
-
isoenzyme ALDH-II
0.03
NAD+
-
in the presence of 0.01 mM Alda-1, at pH 7.4 and 25°C
0.036
NAD+
-
reaction with acetaldehyde
0.036
NAD+
-
reaction with propanal, enzyme I from mitochondria
0.0367
NAD+
-
reaction with acetaldehyde, at pH 9.5
0.037
NAD+
-
native enzyme
0.038
NAD+
-
reaction with butanal
0.038
NAD+
-
isoenzyme ALDH-I
0.0383
NAD+
-
reaction with acetaldehyde, at pH 7.5
0.04
NAD+
-
isoenzyme 1, pH 7.0
0.04
NAD+
mutant enzyme N158A, with NAD+ in 50 mM HEPES, pH 7.5 supplemented with 10 mM MgSO4 for 5 min at 30°C
0.04
NAD+
mutant enzyme N158A, with phosphonoacetaldehyde as cosubstrate, at pH 7.5 and 30°C
0.041
NAD+
-
enzyme from phenotype Aldh2(1)/Aldh2(3)
0.041
NAD+
-
enzyme from phenotype Aldh2(3)/Aldh2(3)
0.041
NAD+
50 mM sodium phosphate buffer, pH 7.4, 0.014 mM propanal, 25°C
0.043
NAD+
-
enzyme from phenotype Aldh2(1)/Aldh2(1)
0.044
NAD+
-
reaction with butanal
0.047
NAD+
-
100 mM Na2HPO4, pH 7.4, 100 mM NaCl, 1 mM NAD+, 25°C
0.054
NAD+
mutant enzyme R447A, with NAD+ in 50 mM HEPES, pH 7.5 supplemented with 10 mM MgSO4 for 5 min at 30°C
0.054
NAD+
mutant enzyme R447A, with phosphonoacetaldehyde as cosubstrate, at pH 7.5 and 30°C
0.058
NAD+
wild type enzyme, with NAD+ in 50 mM HEPES, pH 7.5 supplemented with 10 mM MgSO4 for 5 min at 30°C
0.058
NAD+
wild type enzyme, with phosphonoacetaldehyde as cosubstrate, at pH 7.5 and 30°C
0.06
NAD+
-
mutant enzyme R264Q
0.07
NAD+
-
native enzyme, pH 7.4
0.07
NAD+
-
isoenzyme 2, pH 7.0 and pH 9.5
0.073
NAD+
-
in the absence of Alda-1, at pH 7.4 and 25°C
0.074
NAD+
-
native enzyme, pH 9.0
0.075
NAD+
mutant enzyme R290A, with NAD+ in 50 mM HEPES, pH 7.5 supplemented with 10 mM MgSO4 for 5 min at 30°C
0.075
NAD+
mutant enzyme R290A, with phosphonoacetaldehyde as cosubstrate, at pH 7.5 and 30°C
0.077
NAD+
-
mitochondrial isoenzyme
0.09
NAD+
-
mutant enzyme E487Q
0.09
NAD+
0,05 mM propanal, 250 mM sodium bicarbonate-NaOH buffer pH 10.0, 37°C
0.09
NAD+
-
recombinant enzyme, in 50 mM potassium phosphate buffer, at pH 8.0 and 45°C
0.095
NAD+
-
reaction with propanal, enzyme II from microsomes
0.097
NAD+
-
reaction with propanal, enzyme I from microsomes
0.119
NAD+
-
wild type enzyme, with nonanal as cosubstrate, in 100 mM sodium diphosphate, at pH 8.0 and 22°C
0.12
NAD+
50 mM sodium phosphate buffer, pH 7.4, 0.2 mM Mg2+,0.014 mM propanal, 25°C
0.132
NAD+
-
enzyme from phenotype Aldh2(2)/Aldh2(2)
0.136
NAD+
-
mutant S82A/D80G of isoform ALDH1A1, in 100 mM sodium diphosphate (pH 9.5), at 25°C
0.2
NAD+
-
reaction with decanal
0.37
NAD+
mutant enzyme E385A, with NAD+ in 50 mM HEPES, pH 7.5 supplemented with 10 mM MgSO4 for 5 min at 30°C
0.37
NAD+
mutant enzyme E385A, with phosphonoacetaldehyde as cosubstrate, at pH 7.5 and 30°C
0.389
NAD+
-
in 50 mM KH2PO4-K2HPO4 buffer (pH 8.0), at 60°C
0.4
NAD+
-
pH 9.5, reaction with acetaldehyde
0.421
NAD+
-
wild type enzyme, with hexanal as cosubstrate, in 100 mM sodium diphosphate, at pH 8.0 and 22°C
0.421
NAD+
wild type enzyme, with hexanal as cosubstrate, at pH 8.0 and 25°C
0.441
NAD+
mutant enzyme E149D, with hexanal as cosubstrate, at pH 8.0 and 25°C
0.496
NAD+
-
mutant enzyme I200V, with hexanal as cosubstrate, in 100 mM sodium diphosphate, at pH 8.0 and 22°C
0.496
NAD+
mutant enzyme I200V, with hexanal as cosubstrate, at pH 8.0 and 25°C
0.5
NAD+
-
at pH 7.7 and 25°C
0.53
NAD+
wild type enzyme, with glyceraldehyde-3-phosphate as cosubstrate, at pH 7.5 and 30°C
0.564
NAD+
mutant enzyme E149T/I200V, with trans-2-nonenal as cosubstrate, at pH 8.0 and 25°C
0.62
NAD+
-
reaction with formaldehyde
0.63
NAD+
mutant enzyme E149N, with hexanal as cosubstrate, at pH 8.0 and 25°C
0.7
NAD+
-
mutant enzyme E487K, pH 7.4
0.74
NAD+
-
mutant enzyme R274E
0.82
NAD+
-
with Dl-glyceraldehyde as cosubstrate, in 50 mM Tris/HCl, at pH 8.0 and 80°C
0.84
NAD+
-
with acetaldehyde as cosubstrate, in 50 mM Tris/HCl, at pH 8.0 and 80°C
0.85
NAD+
-
mutant enzyme R475Q
0.886
NAD+
mutant enzyme E149Q, with hexanal as cosubstrate, at pH 8.0 and 25°C
0.991
NAD+
mutant enzyme E149D/I200V, with hexanal as cosubstrate, at pH 8.0 and 25°C
0.992
NAD+
mutant enzyme E149N/I200V, with hexanal as cosubstrate, at pH 8.0 and 25°C
1
NAD+
-
at pH 7.5 and 30°C
1.068
NAD+
mutant enzyme E149T/V178R/I200V, with trans-2-nonenal as cosubstrate, at pH 8.0 and 25°C
1.092
NAD+
mutant enzyme E149T/I200V, with trans-2-hexenal as cosubstrate, at pH 8.0 and 25°C
1.1
NAD+
-
mutant enzyme E487K, pH 9.0
1.262
NAD+
mutant enzyme E149T, with hexanal as cosubstrate, at pH 8.0 and 25°C
1.3
NAD+
-
mutant enzyme R475Q/R264Q and R475E
1.622
NAD+
mutant enzyme E149T/V178R/I200V, with trans-2-hexenal as cosubstrate, at pH 8.0 and 25°C
1.648
NAD+
mutant enzyme E149T/I200V, with hexanal as cosubstrate, at pH 8.0 and 25°C
1.649
NAD+
mutant enzyme E149T/I200V, with hexanal as cosubstrate, at pH 8.0 and 25°C
1.829
NAD+
mutant enzyme E149T/I200V, with nonanal as cosubstrate, at pH 8.0 and 25°C
1.856
NAD+
mutant enzyme E149Q/I200V, with hexanal as cosubstrate, at pH 8.0 and 25°C
1.9
NAD+
-
mutant enzyme S74A, reaction with propanal
2.115
NAD+
mutant enzyme E149T/V178R/I200V, with nonanal as cosubstrate, at pH 8.0 and 25°C
2.524
NAD+
mutant enzyme E149T/V178R/I200V, with hexanal as cosubstrate, at pH 8.0 and 25°C
3.218
NAD+
-
mutant enzyme I200G, with hexanal as cosubstrate, in 100 mM sodium diphosphate, at pH 8.0 and 22°C
3.218
NAD+
mutant enzyme I200G, with hexanal as cosubstrate, at pH 8.0 and 25°C
3.418
NAD+
mutant enzyme E149T/I200G, with hexanal as cosubstrate, at pH 8.0 and 25°C
3.651
NAD+
mutant enzyme E149D/I200G, with hexanal as cosubstrate, at pH 8.0 and 25°C
4.059
NAD+
mutant enzyme E149Q/I200G, with hexanal as cosubstrate, at pH 8.0 and 25°C
4.136
NAD+
mutant enzyme E149N/I200G, with hexanal as cosubstrate, at pH 8.0 and 25°C
7.4
NAD+
-
mutant enzyme E487K
16
NAD+
-
mutant enzyme R475E/R264E
0.27
NADP+
-
reaction with benzaldehyde, enzyme II from microsomes
0.44
NADP+
-
reaction with benzaldehyde, enzyme II from mitochondria
0.44
NADP+
-
reaction with benzaldehyde, enzyme I from microsomes
0.91
NADP+
-
reaction with benzaldehyde, enzyme I from mitochondria
3.81
NADP+
-
with acetaldehyde as cosubstrate, in 50 mM Tris/HCl, at pH 8.0 and 80°C
8.47
NADP+
-
with Dl-glyceraldehyde as cosubstrate, in 50 mM Tris/HCl, at pH 8.0 and 80°C
0.008
Nonanal
wild type enzyme, at pH 8.0 and 25°C
0.008
Nonanal
-
in 100 mM sodium diphosphate, at pH 8.0 and 22°C
0.065
Nonanal
mutant enzyme E149T/V178R/I200V, at pH 8.0 and 25°C
0.000012
octanal
-
enzyme form ALDH-1, pH 9.5
0.000028
octanal
-
enzyme form ALDH-2, pH 9.5
0.000085
octanal
1 mM NAD+, 0,05 mM substrate, 250 mM sodium bicarbonate-NaOH buffer pH 10.0, 37°C
0.0175
octanal
-
pH and temperature not specified in the publication
0.029
octanal
-
in 100 mM sodium diphosphate, at pH 8.0 and 22°C
0.000005
p-(dimethylamino)cinnamaldehyde
-
enzyme ALDH-2
0.0009
p-(dimethylamino)cinnamaldehyde
-
enzyme ALDH-1
0.00142
p-(dimethylamino)cinnamaldehyde
-
enzyme ALDH-1
0.000018
p-Methoxybenzaldehyde
-
enzyme ALDH-2
0.0001
p-Methoxybenzaldehyde
-
native enzyme
0.0004
p-Methoxybenzaldehyde
-
mutant enzyme S74A
0.000007
p-nitrobenzaldehyde
-
enzyme ALDH-2
0.0001
p-nitrobenzaldehyde
-
native enzyme
0.0004
p-nitrobenzaldehyde
-
mutant enzyme S74A
0.0034
p-nitrobenzaldehyde
-
-
0.018
p-nitrobenzaldehyde
-
isoenzyme ALDH-II
0.056
p-nitrobenzaldehyde
-
membrane-bound isoenzyme ALDH
2
p-nitrobenzaldehyde
-
isoenzyme ALDH-I
0.000034
pentanal
-
enzyme form ALDH-2, pH 9.5
0.00016
pentanal
-
enzyme form ALDH-1, pH 9.5
0.000029
phenylacetaldehyde
-
enzyme ALDH-2
0.00352
phenylacetaldehyde
-
-
0.0055
phenylacetaldehyde
-
enzyme ALDH-1
0.02
phenylacetaldehyde
-
at pH 7.7 and 25°C
0.027
phenylacetaldehyde
-
-
0.0032
phosphonoacetaldehyde
wild type enzyme, at pH 7.5 and 30°C
0.0032
phosphonoacetaldehyde
wild type enzyme, with NAD+ in 50 mM HEPES, pH 7.5 supplemented with 10 mM MgSO4 for 5 min at 30°C
0.005
phosphonoacetaldehyde
mutant enzyme R290A, with NAD+ in 50 mM HEPES, pH 7.5 supplemented with 10 mM MgSO4 for 5 min at 30°C
0.0051
phosphonoacetaldehyde
mutant enzyme R290A, at pH 7.5 and 30°C
0.009
phosphonoacetaldehyde
mutant enzyme R108A, with NAD+ in 50 mM HEPES, pH 7.5 supplemented with 10 mM MgSO4 for 5 min at 30°C
0.0097
phosphonoacetaldehyde
mutant enzyme R108A, at pH 7.5 and 30°C
0.019
phosphonoacetaldehyde
mutant enzyme E385A, with NAD+ in 50 mM HEPES, pH 7.5 supplemented with 10 mM MgSO4 for 5 min at 30°C
0.019
phosphonoacetaldehyde
mutant enzyme E385A, at pH 7.5 and 30°C
0.029
phosphonoacetaldehyde
mutant enzyme N158A, with NAD+ in 50 mM HEPES, pH 7.5 supplemented with 10 mM MgSO4 for 5 min at 30°C
0.029
phosphonoacetaldehyde
mutant enzyme N158A, at pH 7.5 and 30°C
0.15
phosphonoacetaldehyde
mutant enzyme R447A, with NAD+ in 50 mM HEPES, pH 7.5 supplemented with 10 mM MgSO4 for 5 min at 30°C
0.15
phosphonoacetaldehyde
mutant enzyme R447A, at pH 7.5 and 30°C
0.5
phosphonoacetaldehyde
-
at pH 7.5 and 30°C
0.000008
propanal
-
major component of enzyme E3
0.00001
propanal
-
minor component of enzyme E3
0.00004
propanal
-
minor component of enzyme E3
0.00008
propanal
-
native enzyme, pH 7.4
0.000095
propanal
-
enzyme form ALDH-2, pH 9.5
0.0001
propanal
-
native enzyme, pH 9.0
0.00011
propanal
-
pH 7.5
0.0002
propanal
-
mutant enzyme E487Q, pH 7.4
0.0002
propanal
50 mM sodium phosphate buffer, pH 7.4, 0.2 mM Mg2+,1 mM NAD+, 25°C
0.0002
propanal
50 mM sodium phosphate buffer, pH 7.4, 1 mM NAD+, 25°C
0.00035
propanal
-
pH 9.5
0.0006
propanal
-
mutant enzyme E487K, pH 7.4
0.0007
propanal
-
native enzyme
0.0007
propanal
-
enzyme form ALDH-1, pH 9.5
0.0007
propanal
-
native enzyme, pH 7.4
0.0007
propanal
-
isoenzyme 2, pH 7.0
0.0007
propanal
-
in the absence of Alda-1, at pH 7.4 and 25°C
0.0008
propanal
-
native enzyme and mutant enzyme S74A
0.0009
propanal
-
mutant enzyme S74A
0.0012
propanal
-
isoenzyme 2, pH 9.5
0.0012
propanal
50 mM sodium phosphate buffer, pH 7.4, 0.2 mM Mg2+,1 mM NAD+, 25°C
0.0014
propanal
-
mutant enzyme E487K, pH 7.4
0.0017
propanal
-
mutant enzyme E487K, pH 9.0
0.0024
propanal
0.1 M sodium diphosphate pH 8.0, 1 mM NAD+, 50 mM 2-mercaptoethanol, 1 mM pyrazole, 30 min, 25°C
0.0033
propanal
-
isoenzyme ALDH-II
0.0034
propanal
50 mM sodium phosphate buffer, pH 7.4, 0.25 mM Mg2+,1 mM NAD+, 25°C
0.004
propanal
-
isoenzyme III
0.0045
propanal
-
enzyme form ALDH-1, pH 9.5
0.0052
propanal
50 mM sodium phosphate buffer, pH 7.4, 1 mM NAD+, 25°C
0.0053
propanal
-
100 mM Na2HPO4, pH 7.4, 100 mM NaCl, 1 mM NAD+, 25°C
0.0058
propanal
50 mM sodium phosphate buffer, pH 7.4, 1 mM NAD+, 25°C
0.006
propanal
-
in the presence of 0.01 mM Alda-1, at pH 7.4 and 25°C
0.0061
propanal
-
0.1 M sodium diphosphate pH 8.0, 1 mM NAD+, 50 mM 2-mercaptoethanol, 1 mM pyrazole, 30 min, 25°C
0.0091
propanal
1 mM NAD+, 0,05 mM substrate, 250 mM sodium bicarbonate-NaOH buffer pH 10.0, 37°C
0.011
propanal
-
isoenzyme 2, pH 9.5
0.15
propanal
-
enzyme I and II from mitochondria
0.294
propanal
-
microsomal enzyme
0.5
propanal
-
isoenzyme ALDH-I
0.6474
propanal
-
pH and temperature not specified in the publication
0.765
propanal
-
at substrate concentrations 0.8-20 mM
1
propanal
-
isoenzyme 1, pH 7.0
1.3
propanal
-
enzyme from promotion phase of hepatocarcinogenesis
1.4
propanal
-
phenobarbital-inducible enzyme
1.7
propanal
-
enzyme II from microsome
2
propanal
-
membrane-bound isoenzyme ALDH
2.76
propanal
pH 8.0, 50°C, recombinant wild-type enzyme
0.0028
propionaldehyde
-
pH 7.5, 25°C, mutant enzyme D80G
0.0044
propionaldehyde
-
pH 7.5, 25°C, mutant enzyme S82A
0.008
propionaldehyde
-
pH 7.5, 25°C, mutant enzyme ALDH1-5AA
0.012
propionaldehyde
-
pH 7.5, 25°C, wild-type enzyme
0.012
propionaldehyde
-
wild type isoform ALDH1A1, in 100 mM sodium diphosphate (pH 9.5), at 25°C
0.014
propionaldehyde
-
at 25°C, pH not specified in the publication
0.031
propionaldehyde
-
pH 7.5, 25°C, mutant enzyme ALDH1-H3tail
0.0662
propionaldehyde
-
pH 8.0, 25°C
0.07
propionaldehyde
-
pH 7.5, 25°C, mutant enzyme R84Q
0.1372
propionaldehyde
-
pH 8.0, 25°C
0.189
propionaldehyde
-
mutant S82A/D80G of isoform ALDH1A1, in 100 mM sodium diphosphate (pH 9.5), at 25°C
0.51
propionaldehyde
-
in 100 mM sodium diphosphate, at pH 8.0 and 22°C
0.82
propionaldehyde
at pH 8.0 and 21°C
1.21
propionaldehyde
-
with NAD+ as cofactor, in 50 mM potassium phosphate buffer (pH 8.0), at 37°C
12
propionaldehyde
in 0.1 M sodium diphosphate buffer (pH 8.5), at ambient temperature
0.69
Succinic semialdehyde
+/- 0.22
3.54
Succinic semialdehyde
-
-
0.18
trans-2-hexenal
wild type enzyme, at pH 8.0 and 25°C
0.18
trans-2-hexenal
-
in 100 mM sodium diphosphate, at pH 8.0 and 22°C
0.199
trans-2-hexenal
mutant enzyme E149T/V178R/I200V, at pH 8.0 and 25°C
0.003
trans-2-nonenal
wild type enzyme, at pH 8.0 and 25°C
0.003
trans-2-nonenal
-
in 100 mM sodium diphosphate, at pH 8.0 and 22°C
0.0322
trans-2-nonenal
mutant enzyme E149T/V178R/I200V, at pH 8.0 and 25°C
0.000035
trans-cinnamaldehyde
-
enzyme ALDH-2
0.0004
trans-cinnamaldehyde
-
enzyme ALDH-1
0.14
Valeraldehyde
-
recombinant enzyme, in 50 mM potassium phosphate buffer, at pH 8.0 and 45°C
0.24
Valeraldehyde
-
with NAD+ as cofactor, in 50 mM potassium phosphate buffer (pH 8.0), at 37°C
additional information
additional information
-
influence of pH-value and buffer on Km-value for hexanal
-
additional information
additional information
-
Km-values of the 475 and 264 arginine mutants of Oriental variant E847K
-
additional information
additional information
-
Michaelis-Menten steady-state kinetics of wild-type and mutant enzymes
-
additional information
additional information
-
Michaelis-Menten kinetics and modeling
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.039
(R)-trans-4-hydroxy-2-nonenal
ALDH2, in 40 mM sodium phosphate buffer (pH 7.4), at 37°C
0.04
(S)-trans-4-hydroxy-2-nonenal
ALDH2, in 40 mM sodium phosphate buffer (pH 7.4), at 37°C
0.667
2,4-dinitrobenzaldehyde
-
enzyme ALDH-2
4
2-naphthaldehyde
-
enzyme ALDH-2
1.57
2-quinolinone-4-carboxaldehyde
-
enzyme ALDH-2
1.42
3,4-dimethoxybenzaldehyde
-
enzyme ALDH-2
4.91 - 28.54
3-hydroxypropionaldehyde
0.26
3-hydroxypropionic acid
-
with NADH as cofactor, in 50 mM potassium phosphate buffer (pH 8.0), at 37°C
1.5
3-oxopropyl phosphonate
wild type enzyme, at pH 7.5 and 30°C
27.7
3-Pyridinecarboxaldehyde
-
enzyme ALDH-2
4.42
4-methoxy-1-naphthaldehyde
-
enzyme ALDH-1
0.26
4-nitrophenyl acetate
-
-
2.67
5-(dimethylamino)-2-naphthaldehyde
-
enzyme ALDH-1
0.158 - 0.25
5-bromo-1-naphthaldehyde
0.55 - 0.833
5-nitro-1-naphthaldehyde
0.983
6,7-dimethoxycoumarin-3-carboxaldehyde
-
enzyme ALDH-2
0.617
6-(dimethylamino)-2-naphthaldehyde
-
enzyme ALDH-2
0.983
6-methoxy-2-quinolinone-4-carboxaldehyde
-
enzyme ALDH-2
2.17
7-(dimethylamino)-2-quinolinone-4-carboxaldehyde
-
enzyme ALDH-2
1.3
7-(dimethylamino)-coumarin-3-carboxaldehyde
-
enzyme ALDH-2
7.9
7-(dimethylamino)coumarin-4-carboxaldehyde
-
enzyme ALDH-2
1.08
7-acetoxycoumarin-3-carboxaldehyde
-
enzyme ALDH-2
8.33
7-hydroxycoumarin-3-carboxaldehyde
-
enzyme ALDH-2
5.33
7-methoxy-2-quinolinone-4-carboxaldehyde
-
enzyme ALDH-2
3.17
7-methoxycoumarin-3-carboxaldehyde
-
enzyme ALDH-2
0.3 - 1
alpha-aminoadipate semialdehyde
15.2
alpha-phenylpropanal
-
enzyme ALDH-2
0.0425 - 17.37
benzaldehyde
3.44 - 26.95
Butyraldehyde
0.92
DL-glyceraldehyde
-
in 50 mM Tris/HCl, at pH 8.0 and 80°C
0.83
DL-glyceraldehyde 3-phosphate
-
in 50 mM Tris/HCl, at pH 8.0 and 80°C
2.83 - 6
fluorene-2-carboxaldehyde
67.5
formaldehyde
-
enzyme ALDH-2
0.04
glutathione-4-oxonon-2-enal
-
50 mM sodium phosphate buffer pH 7.4, 1 mM NAD+, 37°C
0.098 - 0.28
glyceraldehyde 3-phosphate
5.61
hexanaldehyde
at pH 8.0 and 21°C
12.3
hydrocinnamaldehyde
-
enzyme ALDH-2
9.33 - 11.3
Indole-3-acetaldehyde
27.31
Isovaleraldehyde
-
with NAD+ as cofactor, in 50 mM potassium phosphate buffer (pH 8.0), at 37°C
1
m-hydroxybenzaldehyde
-
enzyme ALDH-2
5.83
m-methoxybenzaldehyde
-
enzyme ALDH-2
4.5
m-methylbenzaldehyde
-
enzyme ALDH-2
240
NADH
-
at pH 7.0 and 55°C
0.367
o-methoxybenzaldehyde
-
enzyme ALDH-2
2.75
o-methylbenzaldehyde
-
enzyme ALDH-2
1.23
o-nitrobenzaldehyde
-
enzyme ALDH-2
2.33
p-(dimethylamino)-benzaldehyde
-
enzyme ALDH-2
2.13
p-(dimethylamino)benzaldehyde
-
enzyme ALDH-1
1.5 - 8.17
p-(dimethylamino)cinnamaldehyde
2.5
p-Methoxybenzaldehyde
-
enzyme ALDH-2
3
p-methylbenzaldehyde
-
enzyme ALDH-2
0.23 - 7.17
p-nitrobenzaldehyde
0.45
p-nitrocinnamaldehyde
-
enzyme ALDH-2
5.44
pentanaldehyde
at pH 8.0 and 21°C
0.3
phenanthrene-9-carboxaldehyde
-
enzyme ALDH-2
1.39 - 50
phenylacetaldehyde
0.01 - 2.2
phosphonoacetaldehyde
3.45 - 24.35
propionaldehyde
11.2
quinoline-3-carboxaldehyde
-
enzyme ALDH-2
4.67
quinoline-4-carboxaldehyde
-
enzyme ALDH-2
0.76
Succinic semialdehyde
-
-
1.1 - 2.2
trans-2-hexenal
2.7 - 3.8
trans-2-nonenal
2.5 - 7.83
trans-cinnamaldehyde
26.24
Valeraldehyde
-
with NAD+ as cofactor, in 50 mM potassium phosphate buffer (pH 8.0), at 37°C
additional information
additional information
-
4.91
3-hydroxypropionaldehyde
-
with NADP+ as cofactor, in 50 mM potassium phosphate buffer (pH 8.0), at 37°C
28.54
3-hydroxypropionaldehyde
-
with NAD+ as cofactor, in 50 mM potassium phosphate buffer (pH 8.0), at 37°C
0.158
5-bromo-1-naphthaldehyde
-
enzyme ALDH-1
0.25
5-bromo-1-naphthaldehyde
-
enzyme ALDH-2
0.55
5-nitro-1-naphthaldehyde
-
enzyme ALDH-1
0.833
5-nitro-1-naphthaldehyde
-
enzyme ALDH-2
0.26
acetaldehyde
ALDH2, in 40 mM sodium phosphate buffer (pH 7.4), at 37°C
1.14
acetaldehyde
-
in 50 mM Tris/HCl, at pH 8.0 and 80°C
1.62
acetaldehyde
at pH 8.0 and 21°C
3.5
acetaldehyde
ALDH5A, in 40 mM sodium phosphate buffer (pH 7.4), at 37°C
11.03
acetaldehyde
-
with NAD+ as cofactor, in 50 mM potassium phosphate buffer (pH 8.0), at 37°C
13.2
acetaldehyde
-
enzyme form ALDH-1, pH 9.5
19.7
acetaldehyde
-
enzyme form ALDH-2, pH 9.5
240
acetaldehyde
-
at pH 7.0 and 55°C
0.3
alpha-aminoadipate semialdehyde
-
pH 8.0, 26°C, recombinant wild-type enzyme
1
alpha-aminoadipate semialdehyde
-
pH 8.0, 26°C, recombinant mutant A505P
0.0425
benzaldehyde
-
at 25°C and pH 8.5, with NADP+ as the electron acceptor
0.137
benzaldehyde
-
at 25°C and pH 8.5, with NAD+ as the electron acceptor
5.83
benzaldehyde
-
enzyme ALDH-2
17.37
benzaldehyde
-
with NADP+ as cofactor, in 50 mM potassium phosphate buffer (pH 8.0), at 37°C
3.44
Butyraldehyde
at pH 8.0 and 21°C
26.95
Butyraldehyde
-
with NAD+ as cofactor, in 50 mM potassium phosphate buffer (pH 8.0), at 37°C
3.83
decanal
-
enzyme form ALDH-1, pH 9.5
11.7
decanal
-
enzyme form ALDH-2, pH 9.5
2.83
fluorene-2-carboxaldehyde
-
enzyme ALDH-2
6
fluorene-2-carboxaldehyde
-
enzyme ALDH-1
0.098
glyceraldehyde 3-phosphate
wild type enzyme, at pH 7.5 and 30°C
0.28
glyceraldehyde 3-phosphate
-
-
4.33
Heptanal
-
enzyme form ALDH-1, pH 9.5
22.7
Heptanal
-
enzyme form ALDH-2, pH 9.5
3.3
hexanal
-
pH 8.0, 22°C, recombinant wild-type enzyme
4.17
hexanal
-
enzyme form ALDH-1, pH 9.5
8.2
hexanal
mutant enzyme E149T/V178R/I200V, at pH 8.0 and 25°C
11.2
hexanal
wild type enzyme, at pH 8.0 and 25°C
28.5
hexanal
-
enzyme form ALDH-2, pH 9.5
9.33
Indole-3-acetaldehyde
-
enzyme ALDH-2
11.3
Indole-3-acetaldehyde
-
enzyme ALDH-1
0.0667
NAD+
-
mutant enzyme R475E/R264E
0.2
NAD+
-
mutant enzyme R264E
0.3
NAD+
-
mutant enzyme R475E
0.6
NAD+
-
with DL-glyceraldehyde as cosubstrate, in 50 mM Tris/HCl, at pH 8.0 and 80°C
1.8
NAD+
mutant enzyme E149T/V178R/I200V, with trans-2-hexenal as cosubstrate, at pH 8.0 and 25°C
1.9
NAD+
-
in the absence of Alda-1, at pH 7.4 and 25°C
2
NAD+
-
mutant enzyme R475Q
2.05
NAD+
-
with acetaldehyde as cosubstrate, in 50 mM Tris/HCl, at pH 8.0 and 80°C
2.08
NAD+
-
mutant enzyme R264Q
2.2
NAD+
mutant enzyme E149T/I200V, with trans-2-nonenal as cosubstrate, at pH 8.0 and 25°C
3.05
NAD+
-
in the presence of 0.01 mM Alda-1, at pH 7.4 and 25°C
3.1
NAD+
mutant enzyme E149T/I200V, with trans-2-hexenal as cosubstrate, at pH 8.0 and 25°C
4
NAD+
mutant enzyme E149T/V178R/I200V, with trans-2-nonenal as cosubstrate, at pH 8.0 and 25°C
10.2
NAD+
mutant enzyme E149T, with hexanal as cosubstrate, at pH 8.0 and 25°C
10.7
NAD+
mutant enzyme E149D, with hexanal as cosubstrate, at pH 8.0 and 25°C
11.4
NAD+
mutant enzyme E149Q/I200V, with hexanal as cosubstrate, at pH 8.0 and 25°C
12.2
NAD+
mutant enzyme E149T/V178R/I200V, with hexanal as cosubstrate, at pH 8.0 and 25°C
12.4
NAD+
mutant enzyme E149D/I200V, with hexanal as cosubstrate, at pH 8.0 and 25°C
12.7
NAD+
mutant enzyme E149Q, with hexanal as cosubstrate, at pH 8.0 and 25°C
12.7
NAD+
mutant enzyme E149T/V178R/I200V, with nonanal as cosubstrate, at pH 8.0 and 25°C
13.1
NAD+
mutant enzyme E149N/I200V, with hexanal as cosubstrate, at pH 8.0 and 25°C
15.7
NAD+
mutant enzyme E149T/I200V, with hexanal as cosubstrate, at pH 8.0 and 25°C
16.3
NAD+
mutant enzyme I200G, with hexanal as cosubstrate, at pH 8.0 and 25°C
16.6
NAD+
mutant enzyme E149N, with hexanal as cosubstrate, at pH 8.0 and 25°C
17.2
NAD+
wild type enzyme, with hexanal as cosubstrate, at pH 8.0 and 25°C
18
NAD+
mutant enzyme E149T/I200V, with nonanal as cosubstrate, at pH 8.0 and 25°C
18.5
NAD+
mutant enzyme I200V, with hexanal as cosubstrate, at pH 8.0 and 25°C
20.1
NAD+
mutant enzyme E149Q/I200G, with hexanal as cosubstrate, at pH 8.0 and 25°C
23.2
NAD+
mutant enzyme E149D/I200G, with hexanal as cosubstrate, at pH 8.0 and 25°C
26.9
NAD+
mutant enzyme E149N/I200G, with hexanal as cosubstrate, at pH 8.0 and 25°C
33.9
NAD+
mutant enzyme E149T/I200G, with hexanal as cosubstrate, at pH 8.0 and 25°C
1.63
NADP+
-
with DL-glyceraldehyde as cosubstrate, in 50 mM Tris/HCl, at pH 8.0 and 80°C
3.71
NADP+
-
with acetaldehyde as cosubstrate, in 50 mM Tris/HCl, at pH 8.0 and 80°C
13
Nonanal
mutant enzyme E149T/V178R/I200V, at pH 8.0 and 25°C
17.9
Nonanal
wild type enzyme, at pH 8.0 and 25°C
4.17
octanal
-
enzyme form ALDH-2, pH 9.5
15
octanal
-
enzyme form ALDH-2, pH 9.5
1.5
p-(dimethylamino)cinnamaldehyde
-
enzyme ALDH-2
8.17
p-(dimethylamino)cinnamaldehyde
-
enzyme ALDH-1
0.23
p-nitrobenzaldehyde
-
-
7.17
p-nitrobenzaldehyde
-
enzyme ALDH-2
8.17
pentanal
-
enzyme form ALDH-1, pH 9.5
22.8
pentanal
-
enzyme form ALDH-2, pH 9.5
1.39
phenylacetaldehyde
-
-
30
phenylacetaldehyde
-
enzyme ALDH-2
50
phenylacetaldehyde
-
enzyme ALDH-1
0.01
phosphonoacetaldehyde
mutant enzyme N158A, with NAD+ in 50 mM HEPES, pH 7.5 supplemented with 10 mM MgSO4 for 5 min at 30°C
0.01
phosphonoacetaldehyde
mutant enzyme N158A, at pH 7.5 and 30°C
0.051
phosphonoacetaldehyde
mutant enzyme R108A, with NAD+ in 50 mM HEPES, pH 7.5 supplemented with 10 mM MgSO4 for 5 min at 30°C
0.051
phosphonoacetaldehyde
mutant enzyme R108A, at pH 7.5 and 30°C
0.076
phosphonoacetaldehyde
mutant enzyme R447A, with NAD+ in 50 mM HEPES, pH 7.5 supplemented with 10 mM MgSO4 for 5 min at 30°C
0.076
phosphonoacetaldehyde
mutant enzyme R447A, at pH 7.5 and 30°C
0.12
phosphonoacetaldehyde
mutant enzyme R290A, with NAD+ in 50 mM HEPES, pH 7.5 supplemented with 10 mM MgSO4 for 5 min at 30°C
0.12
phosphonoacetaldehyde
mutant enzyme R290A, at pH 7.5 and 30°C
0.19
phosphonoacetaldehyde
mutant enzyme E385A, with NAD+ in 50 mM HEPES, pH 7.5 supplemented with 10 mM MgSO4 for 5 min at 30°C
0.19
phosphonoacetaldehyde
mutant enzyme E385A, at pH 7.5 and 30°C
2.2
phosphonoacetaldehyde
wild type enzyme, at pH 7.5 and 30°C
2.2
phosphonoacetaldehyde
wild type enzyme, with NAD+ in 50 mM HEPES, pH 7.5 supplemented with 10 mM MgSO4 for 5 min at 30°C
0.42
propanal
50 mM sodium phosphate buffer, pH 7.4, 0.25 mM Mg2+,1 mM NAD+, 25°C
0.65
propanal
50 mM sodium phosphate buffer, pH 7.4, 0.2 mM Mg2+,1 mM NAD+, 25°C
1.33
propanal
50 mM sodium phosphate buffer, pH 7.4, 1 mM NAD+, 25°C
1.48
propanal
50 mM sodium phosphate buffer, pH 7.4, 1 mM NAD+, 25°C
1.9
propanal
-
in the absence of Alda-1, at pH 7.4 and 25°C
3.05
propanal
-
in the presence of 0.01 mM Alda-1, at pH 7.4 and 25°C
3.16
propanal
50 mM sodium phosphate buffer, pH 7.4, 1 mM NAD+, 25°C
6.16
propanal
50 mM sodium phosphate buffer, pH 7.4, 0.2 mM Mg2+,1 mM NAD+, 25°C
19.7
propanal
-
enzyme form ALDH-2
3.45
propionaldehyde
at pH 8.0 and 21°C
24.35
propionaldehyde
-
with NAD+ as cofactor, in 50 mM potassium phosphate buffer (pH 8.0), at 37°C
1.1
trans-2-hexenal
mutant enzyme E149T/V178R/I200V, at pH 8.0 and 25°C
2.2
trans-2-hexenal
wild type enzyme, at pH 8.0 and 25°C
2.7
trans-2-nonenal
wild type enzyme, at pH 8.0 and 25°C
3.8
trans-2-nonenal
mutant enzyme E149T/V178R/I200V, at pH 8.0 and 25°C
2.5
trans-cinnamaldehyde
-
enzyme ALDH-2
7.83
trans-cinnamaldehyde
-
enzyme ALDH-1
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
turnover numbers of the 475 and 264 arginine mutants of Oriental variant E847K
-
additional information
propanal
50 mM sodium phosphate buffer, pH 7.4, 0.2 mM Mg2+,1 mM NAD+, 25°C
additional information
propanal
-
50 mM sodium phosphate buffer, pH 7.4, 0.2 mM Mg2+,1 mM NAD+, 25°C
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C247S
-
the mutant shows slightly reduced activity compared to the wild type enzyme
C253S
-
the mutation abolishes enzymatic activity
C45S
-
the mutant shows stongly reduced activity compared to the wild type enzyme
E149D
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
E149D/I200G
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
E149D/I200V
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
E149N
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
E149N/I200G
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
E149N/I200V
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
E149Q
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
E149Q/I200G
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
E149Q/I200V
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
E149T
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
E149T/I200G
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
E149T/I200V
the mutant shows a good catalysis with NADP+ compared to the wild type enzyme
E149T/V178R/I200V
the mutant uses NADP+ with almost 7fold higher catalytic efficiency compared to NAD+
C289D
-
enzyme activity is nearly abolished in this mutant
C289P
-
enzyme activity is nearly abolished in this mutant
C289R
-
enzyme activity is nearly abolished in this mutant
E255D
-
the mutant enzyme shows severely diminished activity
E255K
-
the mutant enzyme shows severely diminished activity
A505P
-
site-directed mutagenesis, the mutant enzyme exhibits a profound kinetic defect characterized by markedly elevated Michaelis constants for alpha-aminoadipate semialdehyde, suggesting that the mutated residue is important for substrate binding. The mutant enzyme is defective in tetramer formation, and shows highly reduced activity compared to wild-type
A505P/Q506K
-
site-directed mutagenesis, the mutant enzyme exhibits a profound kinetic defect characterized by markedly elevated Michaelis constants for alpha-aminoadipate semialdehyde, suggesting that the mutated residues are important for substrate binding. The mutant enzyme is defective in tetramer formation, and shows highly reduced activity compared to wild-type. Structure analysis of the protomer of ALDH7A1 with the mutated residues Ala505 and Gln506, PDB ID 4ZUL
ALDH-H3tail
-
aldehyde dehydrogenase class 1 with the addition of the C-terminal tail of class 3, KM-value for propionaldehyde is 2.6fold higher than the KM-value of the wild-type enzyme, KM-value for NAD+ is 2fold higher than the KM-value of the wild-type enzyme
ALDH1-5AA
-
aldehyde dehydrogenase class 1 with the addition of five amino acids at the C-terminus, KM-value for propionaldehyde is 67% of the KM-value of the wild-type enzyme, KM-value for NAD+ is 73% of the KM-value of the wild-type enzyme
D80G
-
KM-value for propionaldehyde is 24% of the KM-value of the wild-type enzyme, KM-value for NAD+ is 32% of the KM-value of the wild-type enzyme
E268Q
the mutant shows 1.39% residual dehydrogenase activity at pH 9.0 and 0.88% residual dehydrogenase activity at pH 7.5 compared to the wild type enzyme. The mutant exhibits virtually unaffected rates of nitroglycerin denitration despite low dehydrogenase and esterase activities. The mutant exhibits about 50% lower rates of superoxide formation than the wild type enzyme
E399Q
mutant is not inhibited by MgCl2
Q506K
-
site-directed mutagenesis, the mutant enzyme exhibits a profound kinetic defect characterized by markedly elevated Michaelis constants for alpha-aminoadipate semialdehyde, suggesting that the mutated residue is important for substrate binding. The mutant enzyme is defective in tetramer formation, and shows highly reduced activity compared to wild-type
R264E
-
turnover-number is about 6% of that of the native enzyme, Km-value is about 20fold higher than the Km-value of the wild-type enzyme
R264Q
-
turnover-number is about 50% of that of the native enzyme, Km-value is about 1.6fold higher than the Km-value of the wild-type enzyme
R475E
-
turnover-number is about 9% of that of the native enzyme, Km-value is about 35fold higher than the Km-value of the wild-type enzyme
R475E/R264E
-
turnover-number is about 2% of that of the native enzyme, Km-value is about 430fold higher than the Km-value of the wild-type enzyme
R475Q/R264Q
-
Km-value is about 35fold higher than the KM-value of the wild-type enzyme
R84Q
-
KM-value for propionaldehyde is 5.8fold higher than the Km-value of the wild-type enzyme, KM-value for NAD+ is 36% of the KM-value of the wild-type enzyme
S31T/V63A/T244S/E479D
generated by random mutagenesis and selected for insensivity to Mg2+ inhibition
S33C/T244S/C463S
generated by random mutagenesis and selected for insensivity to Mg2+ inhibition
S82A
-
KM-value for propionaldehyde is 36% of the KM-value of the wild-type enzyme, KM-value for NAD+ is 15% of the KM-value of the wild-type enzyme
T244S
the T244S mutation is not inhibited by Mg2+. The mutant shows a decreasing Km for NAD+ binding with increasing Mg2+ concentration. chloroacetaldehyde is a better substrate for the mutant enzyme than acetaldehyde in the presence of Mg2+ which is similar to the Mg2+-dependent ALDH2
T244S/D391E
generated by random mutagenesis and selected for insensivity to Mg2+ inhibition
C295A
-
site-directed mutagenesis, inactive mutant
S74A
-
half-life of the mutant enzyme at 50°C is 1 min compared to the half-life of the native enzyme of 1 min. Mutation diminishes NAD+ binding, affecting both the on and the off rates, as well as the rate-limiting step. About 100fold higher Km-value for NAD+
S74C
-
about 70fold higher Km-value for NAD+
S74T
-
about 100fold higher Km-value for NAD+
C274A
-
the mutation leads to a drastic loss of the activity
C274S
-
the mutation leads to a drastic loss of the activity
E240A
-
the mutation leads to a drastic loss of the activity
E240S
-
the mutation leads to a drastic loss of the activity
E370Q
-
the mutation results in decreased activity (higher Km and lower kcat values toward NAD+ and acetaldehyde than the wild type enzyme)
I168A
-
the mutation results in no obvious change of kinetics properties toward acetaldehyde and a comparable increase of affinity toward NAD+
K165Q
-
the mutation results in decreased activity (higher Km and lower kcat values toward NAD+ and acetaldehyde than the wild type enzyme)
N142A
-
the mutation results in decreased activity (higher Km and lower kcat values toward NAD+ and acetaldehyde than the wild type enzyme)
C274A
-
the mutation leads to a drastic loss of the activity
-
C274S
-
the mutation leads to a drastic loss of the activity
-
E240A
-
the mutation leads to a drastic loss of the activity
-
E370Q
-
the mutation results in decreased activity (higher Km and lower kcat values toward NAD+ and acetaldehyde than the wild type enzyme)
-
K165Q
-
the mutation results in decreased activity (higher Km and lower kcat values toward NAD+ and acetaldehyde than the wild type enzyme)
-
I200G
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
I200G
-
the mutant also exhibits activity with NADP+ and shows decreased affinity for NAD+ compared to the wild type enzyme
I200V
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
I200V
-
the mutant also exhibits activity with NADP+ and shows decreased affinity for NAD+ compared to the wild type enzyme
C302S
-
no reactivity is observed for either molinate or molinate sulfone with the C302S mutant
C302S
the mutation leads to more than 90% loss of all enzyme activities (0.29% residual dehydrogenase activity at pH 9.0 and 0.32% residual dehydrogenase activity at pH 7.5 compared to the wild type enzyme)
D80G/S82A
-
the maximal velocity of the mutant enzyme is 7.5% of the activity of the wild-type enzyme
D80G/S82A
-
the unstable mutant starts to denature at urea concentrations below 0.5 M, reaching half of the denaturation at 1.2 M urea
E487K
-
mutant enzyme shows altered kinetic properties when compared to wild-type enzyme, The Km-value for NAD+ at pH 7.4 increases more than 150fold, the turnover-number decreases 2-10fold, many oriental people posses this variant of liver mitochondrial aldehyde dehydrogenase and have very low levels of enzyme activity
E487K
-
the East Asian variant results in very low aldehyde dehydrogenase activity and catalyzes nitroglycerin denitration with about 7fold lower maximal rates than the wild type enzyme1
E487K
-
the mutation results in disruption of the co-enzyme NAD+ binding and reduced catalytic activity of ALDH2 (1-5% of wild type ALDH activity)
E487K
-
the mutation results in poor binding affinity to cofactor NAD+ and about 90% loss of enzyme activity
K487E
reduced activity
K487E
-
there is a significant association between essential hypertension and the ALDH2 mutation K487E
R475Q
-
positive cooperativity in NAD+ binding, Km-value increases 23fold, mutant enzyme is thermally less stable than the native enzyme, the presence of NAD+ restores nativelike stability to the mutant
R475Q
the mutant is less thermally stable by 15°C and shows 2fold reduction in kcat-value compared to the wild type enzyme
E385A
the mutant shows strongly reduced activity compared to the wild type enzyme
E385A
the mutation results in 10fold reduction in kcat, with an approximately 6fold higher KM,NAD+
N158A
the mutant shows strongly reduced activity compared to the wild type enzyme
N158A
the mutation results in a 200fold decrease in kcat
R108A
the mutant shows strongly reduced activity compared to the wild type enzyme
R108A
the mutation leads to a 40fold decrease in kcat and a 3fold increase in KM,PnAA
R290A
the mutant shows strongly reduced activity compared to the wild type enzyme
R290A
the mutation results in a 20fold decrease in kcat with a slightly elevated KM,PnAA relative to wild type
R447A
the mutant shows strongly reduced activity compared to the wild type enzyme
R447A
the mutation reduces the kcat 30fold and increases the KM,PnAA 50fold
additional information
construction of a single ALDH3I1 mutant K06 line and a double T-DNA insertion mutant line K06/62 that is defective in representative members of Arabidopsis thaliana ALDH families 3 and 7, ALDH3I1 and ALDH7B4, by T-DNA insertion. The loss of function of ALDH3I1 and ALDH7B4 leads to a decrease of NAD(P)H, NAD(P)H/NAD(P) ratio, and an alteration of the glutathione pools. The aldh double mutant has higher glucose-6-phosphate dehydrogenase activity than the wild-type, indicating a high demand for reduced pyridine nucleotides. Mutant KO6 plants accumulate higher levels of reactive oxygen species (ROS) and malondialdehyde (MDA) than the wild-type. Moreover, the mutant has a reduced quantum yield of photosystem II and photosynthetic capacity at relatively high light intensities compared to the wild-type. The levels of the total glutathione (reduced + oxidized) and of the reduced to oxidized glutathione ratio (GSH/GSSG) are reduced by 20% and 33% in KO6/62 compared to wild-type, respectively. Phenotype, overview
additional information
construction of a single ALDH3I1 mutant K06 line and a double T-DNA insertion mutant line K06/62 that is defective in representative members of Arabidopsis thaliana ALDH families 3 and 7, ALDH3I1 and ALDH7B4, by T-DNA insertion. The loss of function of ALDH3I1 and ALDH7B4 leads to a decrease of NAD(P)H, NAD(P)H/NAD(P) ratio, and an alteration of the glutathione pools. The aldh double mutant has higher glucose-6-phosphate dehydrogenase activity than the wild-type, indicating a high demand for reduced pyridine nucleotides. Mutant KO6 plants accumulate higher levels of reactive oxygen species (ROS) and malondialdehyde (MDA) than the wild-type. Moreover, the mutant has a reduced quantum yield of photosystem II and photosynthetic capacity at relatively high light intensities compared to the wild-type. The levels of the total glutathione (reduced + oxidized) and of the reduced to oxidized glutathione ratio (GSH/GSSG) are reduced by 20% and 33% in KO6/62 compared to wild-type, respectively. Phenotype, overview
additional information
construction of of a single ALDH7B4 mutant K62 line and a double T-DNA insertion mutant that is defective in representative members of Arabidopsis thaliana ALDH families 3and 7, ALDH3I1 and ALDH7B4, respectively. The loss of function of ALDH3I1 and ALDH7B4 leads to a decrease of NAD(P)H, NAD(P)H/NAD(P) ratio, and an alteration of the glutathione pools. The aldh double mutant has higher glucose-6-phosphate dehydrogenase activity than the wild-type, indicating a high demand for reduced pyridine nucleotides. Mutant K62 plants accumulate higher levels of reactive oxygen species (ROS) and malondialdehyde (MDA) than the wild-type. Moreover, the mutant has a reduced quantum yield of photosystem II and photosynthetic capacity at relatively high light intensities compared to the wild-type. The levels of the total glutathione (reduced + oxidized) and of the reduced to oxidized glutathione ratio (GSH/GSSG) are reduced by 20% and 33% in KO6/62 compared to wild-type, respectively. Phenotype, overview
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construction of of a single ALDH7B4 mutant K62 line and a double T-DNA insertion mutant that is defective in representative members of Arabidopsis thaliana ALDH families 3and 7, ALDH3I1 and ALDH7B4, respectively. The loss of function of ALDH3I1 and ALDH7B4 leads to a decrease of NAD(P)H, NAD(P)H/NAD(P) ratio, and an alteration of the glutathione pools. The aldh double mutant has higher glucose-6-phosphate dehydrogenase activity than the wild-type, indicating a high demand for reduced pyridine nucleotides. Mutant K62 plants accumulate higher levels of reactive oxygen species (ROS) and malondialdehyde (MDA) than the wild-type. Moreover, the mutant has a reduced quantum yield of photosystem II and photosynthetic capacity at relatively high light intensities compared to the wild-type. The levels of the total glutathione (reduced + oxidized) and of the reduced to oxidized glutathione ratio (GSH/GSSG) are reduced by 20% and 33% in KO6/62 compared to wild-type, respectively. Phenotype, overview
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construction of a C-terminal truncation mutant DELTA504-511 lacking the last eight residues
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construction of an ALD6 dominant negative strain that is catalytically inactive, catalytic residues of the ALD6 gene are deleted
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construction of an ALD6 dominant negative strain that is catalytically inactive, catalytic residues of the ALD6 gene are deleted
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construction of an ALD6 dominant negative strain that is catalytically inactive, catalytic residues of the ALD6 gene are deleted
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the TFA T-668 mutant is obtained by insertion of a nonpolar KIXX cassette into the NaeI site of thnG, resulting in truncation of the gene beyond codon 169, the mutant shows reduced but clearly evident ALDH activity
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the TFA T-668 mutant is obtained by insertion of a nonpolar KIXX cassette into the NaeI site of thnG, resulting in truncation of the gene beyond codon 169, the mutant shows reduced but clearly evident ALDH activity
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