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Information on EC 1.2.1.3 - aldehyde dehydrogenase (NAD+) and Organism(s) Homo sapiens and UniProt Accession P49419

for references in articles please use BRENDA:EC1.2.1.3
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EC Tree
IUBMB Comments
Wide specificity, including oxidation of D-glucuronolactone to D-glucarate.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Homo sapiens
UNIPROT: P49419
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Synonyms
aldh2, aldh1, aldh1a1, aldehyde dehydrogenase 2, aldh1a3, aldh3a1, aldehyde dehydrogenase 1, aldh1a2, mitochondrial aldehyde dehydrogenase, aldehyde dehydrogenase-2, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
aldehyde dehydrogenase 7A1
-
AHD-M1
-
-
-
-
ALD1A1
-
isoform
ALDDH
-
-
-
-
aldehyde dehydrogenase
aldehyde dehydrogenase 1
-
-
aldehyde dehydrogenase 16
-
aldehyde dehydrogenase 1A1
-
isoform
aldehyde dehydrogenase 1A3
-
-
aldehyde dehydrogenase 1B1
-
isoform
aldehyde dehydrogenase 2
-
-
aldehyde dehydrogenase 7A1
-
-
aldehyde dehydrogenase class 1
-
-
aldehyde dehydrogenase type 2
-
-
Aldehyde dehydrogenase [NAD+]
-
-
-
-
Aldehyde dehydrogenase, cytosolic
-
-
-
-
Aldehyde dehydrogenase, microsomal
-
-
-
-
aldehyde dehydrogenase-2
aldehyde:NAD+ oxidoreductase
-
-
-
-
ALDH 2
-
-
ALDH I
-
-
ALDH II
-
-
ALDH-2
ALDH-E1
-
-
-
-
ALDH-E2
-
-
-
-
ALDH1
ALDH1-NL
-
-
-
-
ALDH1A1
Aldh1a3
Aldh1b1
ALDH2
ALDH2(2)
-
mutant enzyme
ALDH3A1
ALDH3A2
-
isozyme
Aldh3b1
-
isozyme
Aldh7a1
ALDHI
-
-
-
-
ALDHX
-
-
-
-
ALHDII
-
-
-
-
Allergen Alt a 10
-
-
-
-
benzaldehyde dehydrogenase
-
-
Brassica turgor-responsive/drought-induced gene 26 protein
-
-
-
-
Btg-26
-
-
-
-
class 1 aldehyde dehydrogenase
class 2 aldehyde dehydrogenase
-
CoA-independent aldehyde dehydrogenase
-
-
-
-
ETA-crystallin
-
-
-
-
gamma-aminobutyraldehyde dehydrogenase
-
-
-
-
hALDH2
-
-
HsALDH16A1
-
K(+)-ACDH
-
-
-
-
K(+)-activated acetaldehyde dehydrogenase
-
-
-
-
m-methylbenzaldehyde dehydrogenase
-
-
-
-
Matured fruit 60 kDa protein
-
-
-
-
MF-60
-
-
-
-
Mg(2+)-ACDH
-
-
-
-
Mg(2+)-activated acetaldehyde dehydrogenase
-
-
-
-
mitochondrial aldehyde dehydrogenase
-
-
NAD+-linked aldehyde dehydrogenase
-
-
-
-
NAD-aldehyde dehydrogenase
-
-
-
-
NAD-dependent 4-hydroxynonenal dehydrogenase
-
-
-
-
NAD-dependent aldehyde dehydrogenase
-
-
-
-
NAD-linked aldehyde dehydrogenase
-
-
-
-
Non-lens ALDH1
-
-
-
-
P51
-
-
-
-
PM-ALDH9
-
-
-
-
propionaldehyde dehydrogenase
-
-
-
-
R-aminobutyraldehyde dehydrogenase
-
-
-
-
RALDH
-
-
-
-
RALDH(II)
-
-
-
-
RalDH1
Retinal dehydrogenase
-
-
-
-
retinal dehydrogenase type I
-
-
sALDH
-
-
salvery aldehyde dehydrogenase
-
-
Turgor-responsive protein 26G
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
an aldehyde + NAD+ + H2O = a carboxylate + NADH + H+
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
-
oxidation
reduction
SYSTEMATIC NAME
IUBMB Comments
aldehyde:NAD+ oxidoreductase
Wide specificity, including oxidation of D-glucuronolactone to D-glucarate.
CAS REGISTRY NUMBER
COMMENTARY hide
9028-86-8
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
alpha-aminoadipate semialdehyde + NAD+ + H2O
alpha-aminoadipate + NADH + H+
show the reaction diagram
-
-
-
?
(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
?
show the reaction diagram
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
-
?
1-formyl-6-methylpyrene + NAD+
6-methylpyrene 1-carboxylate + NADH + H+
show the reaction diagram
-
-
-
?
1-formyl-6-methylpyrene + NAD+ + H2O
6-methylpyrene-1-carboxylic acid + NADH + H+
show the reaction diagram
-
-
-
?
1-formyl-8-methylpyrene + NAD+ + H2O
8-methylpyrene-1-carboxylic acid + NADH + H+
show the reaction diagram
-
-
-
?
1-formyl-8-methylpyrene + NADP+
8-methylpyrene 1-carboxylate + NADPH + H+
show the reaction diagram
-
-
-
?
1-formylpyrene + NAD+
pyrene 1-carboxylate + NADH + H+
show the reaction diagram
-
-
-
?
1-formylpyrene + NAD+ + H2O
pyrene-1-carboxylic acid + NADH + H+
show the reaction diagram
-
-
-
?
1-naphthaldehyde + NAD+ + H2O
1-naphthoic acid + NADH + H+
show the reaction diagram
-
-
-
-
?
2,4-dinitrobenzaldehyde + NAD+ + H2O
2,4-dinitrobenzoate + NADH
show the reaction diagram
-
-
-
-
?
2-formylpyrene + NAD+
pyrene 2-carboxylate + NADH + H+
show the reaction diagram
-
-
-
?
2-formylpyrene + NAD+ + H2O
pyrene-2-carboxylic acid + NADH + H+
show the reaction diagram
-
-
-
?
2-hydroxy-3-nitrobenzaldehyde + NAD+ + H2O
2-hydroxy-3-nitrobenzoic acid + NADH + H+
show the reaction diagram
2-naphthaldehyde + NAD+ + H2O
2-naphthalene carboxylate + NADH + H+
show the reaction diagram
-
-
-
-
?
2-naphthaldehyde + NAD+ + H2O
2-naphthoate + NADH
show the reaction diagram
-
-
-
-
?
2-naphthaldehyde + NAD+ + H2O
2-naphthoic acid + NADH + H+
show the reaction diagram
-
-
-
-
?
2-nonenal + NAD+ + H2O
(E)-non-2-enoate + NADH + H+
show the reaction diagram
-
-
-
-
?
2-quinolinone-4-carboxaldehyde + NAD+ + H2O
2-quinolinone-4-carboxylate + NADH
show the reaction diagram
-
-
-
-
?
3,4-dihydroxyphenylacetaldehyde + NAD+ + H2O
3,4-dihydroxyphenylacetate + NADH + H+
show the reaction diagram
3,4-dihydroxyphenylglycolaldehyde + NAD+ + H2O
3,4-dihydroxyphenylglycolate + NADH + H+
show the reaction diagram
-
-
-
?
3,4-dimethoxybenzaldehyde + NAD+ + H2O
3,4-dimethoxybenzoate + NADH
show the reaction diagram
-
-
-
-
?
3-pyridinecarboxaldehyde + NAD+ + H2O
3-pyridinecarboxylate + NADH
show the reaction diagram
-
-
-
-
?
4-aminobutyraldehyde + NAD+ + H2O
4-aminobutyrate + NADH
show the reaction diagram
-
-
-
-
?
4-dimethylamino-1-naphthaldehyde + NAD+ + H2O
4-dimethylamino-1-naphthoic acid + NADH + H+
show the reaction diagram
-
-
-
-
?
4-dimethylaminobenzaldehyde + NAD+ + H2O
4-dimethylaminobenzoate + NADH + H+
show the reaction diagram
-
-
-
-
?
4-formylpyrene + NAD+
pyrene 4-carboxylate + NADH + H+
show the reaction diagram
-
-
-
?
4-formylpyrene + NAD+ + H2O
pyrene-4-carboxylic acid + NADH + H+
show the reaction diagram
-
-
-
?
4-hydroxy-2-nonenal + NAD+ + H2O
4-hydroxy-2-nonenoate + NADH + H+
show the reaction diagram
-
low affinity for substrate binding and poor catalytic efficiency
-
-
?
4-hydroxy-3-methoxybenzaldehyde + NAD+ + H2O
4-hydroxy-3-methoxybenzoate + NADH + H+
show the reaction diagram
-
-
-
-
?
4-hydroxynon-2-enal + NAD+
4-hydroxynon-2-enoic acid + NADH
show the reaction diagram
-
-
-
-
?
4-hydroxynonenal + NAD+ + H2O
4-hydroxynonanoate + NADH + H+
show the reaction diagram
-
-
-
-
?
4-methoxy-1-naphthaldehyde + NAD+ + H2O
4-methoxy-1-naphthoate + NADH
show the reaction diagram
-
-
-
-
?
4-methoxy-1-naphthaldehyde + NAD+ + H2O
4-methoxy-1-naphthoic acid + NADH + H+
show the reaction diagram
-
-
-
-
?
4-methoxybenzaldehyde + NAD+ + H2O
4-methoxybenzoate + NADH + H+
show the reaction diagram
-
-
-
-
?
4-nitro-1-naphthaldehyde + NAD+ + H2O
4-nitro-1-naphthoate + NADH
show the reaction diagram
-
-
-
-
?
4-oxonon-2-enal + NAD+ + H2O
4-oxonon-2-enoic acid + NADH
show the reaction diagram
-
-
-
-
?
5-(dimethylamino)-2-naphthaldehyde + NAD+ + H2O
5-(dimethylamino)-2-naphthoate + NADH + H+
show the reaction diagram
-
-
-
-
r
5-bromo-1-naphthaldehyde + NAD+ + H2O
5-bromo-1-naphthoate + NADH
show the reaction diagram
-
-
-
-
?
5-methoxyindole-3-carboxaldehyde + NAD+ + H2O
5-methoxyindole-3-carboxylate + NADH
show the reaction diagram
-
-
-
-
?
5-nitro-1-naphthaldehyde + NAD+ + H2O
5-nitro-1-naphthoate + NADH + H+
show the reaction diagram
-
-
-
-
r
6,7-dimethoxycoumarin-3-carboxaldehyde + NAD+ + H2O
6,7-dimethoxycoumarin-3-carboxylate + NADH + H+
show the reaction diagram
-
-
-
-
r
6,7-dimethoxycoumarin-4-carboxaldehyde + NAD+ + H2O
6,7-dimethoxycoumarin-4-carboxylate + NADH
show the reaction diagram
-
-
-
-
?
6-(dimethylamino)-2-naphthaldehyde + NAD+ + H2O
6-(dimethylamino)-2-naphthoate + NADH
show the reaction diagram
-
-
-
-
?
6-dimethylamino-2-naphthaldehyde + NAD+ + H2O
6-dimethylamino-2-naphthalene carboxylate + NADH + H+
show the reaction diagram
-
activity assay
-
-
?
6-dimethylamino-2-naphthaldehyde + NAD+ + H2O
6-dimethylamino-2-naphthoic acid + NADH + H+
show the reaction diagram
-
-
-
-
?
6-methoxy-2-naphthaldehyde + NAD+ + H2O
6-methoxy-2-naphthalene carboxylate + NADH + H+
show the reaction diagram
-
activity assay
-
-
?
6-methoxy-2-naphthaldehyde + NAD+ + H2O
6-methoxy-2-naphthoate + NADH + H+
show the reaction diagram
6-methoxy-2-naphthaldehyde + NAD+ + H2O
6-methoxy-2-naphthoic acid + NADH + H+
show the reaction diagram
-
-
-
-
?
6-methoxy-2-quinolinone-4-carboxaldehyde + NAD+ + H2O
6-methoxy-2-quinolinone-4-carboxylate + NADH
show the reaction diagram
-
-
-
-
?
7-(dimethylamino)-2-quinolinone-4-carboxaldehyde + NAD+ + H2O
7-(dimethylamino)-2-quinolinone-4-carboxylate + NADH
show the reaction diagram
-
-
-
-
?
7-(dimethylamino)-coumarin-3-carboxaldehyde + NAD+ + H2O
7-(dimethylamino)-coumarin-3-carboxylate + NADH + H+
show the reaction diagram
-
-
-
-
r
7-(dimethylamino)coumarin-4-carboxaldehyde + NAD+ + H2O
7-(dimethylamino)coumarin-4-carboxylate + NADH
show the reaction diagram
-
-
-
-
?
7-acetoxycoumarin-3-carboxaldehyde + NAD+ + H2O
7-acetoxycoumarin-3-carboxylate + NADH + H+
show the reaction diagram
-
-
-
-
r
7-acetoxycoumarin-4-carboxaldehyde + NAD+ + H2O
7-acetoxycoumarin-4-carboxylate + NADH
show the reaction diagram
-
-
-
-
?
7-hydroxycoumarin-3-carboxaldehyde + NAD+ + H2O
7-hydroxycoumarin-3-carboxylate + NADH + H+
show the reaction diagram
-
-
-
-
r
7-hydroxycoumarin-4-carboxaldehyde + NAD+ + H2O
7-hydroxycoumarin-4-carboxylate + NADH
show the reaction diagram
-
-
-
-
?
7-methoxy-1-naphthaldehyde + NAD+ + H2O
7-methoxy-1-naphthoic acid + NADH + H+
show the reaction diagram
-
-
-
-
?
7-methoxy-2-quinolinone-4-carboxaldehyde + NAD+ + H2O
7-methoxy-2-quinolinone-4-carboxylate + NADH
show the reaction diagram
-
-
-
-
?
7-methoxycoumarin-3-carboxaldehyde + NAD+ + H2O
7-methoxycoumarin-3-carboxylate + NADH + H+
show the reaction diagram
-
-
-
-
r
7-methoxycoumarin-4-carboxaldehyde + NAD+ + H2O
7-methoxycoumarin-4-carboxylate + NADH
show the reaction diagram
-
-
-
-
?
9-cis retinal + NAD+ + H2O
9-cis retinoic acid + NADH
show the reaction diagram
-
-
-
-
?
9-cis-retinal + NAD+ + H2O
9-cis-retinoic acid + NADH + H+
show the reaction diagram
-
-
-
-
?
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
show the reaction diagram
acrolein + NAD+ + H2O
? + NADH + H+
show the reaction diagram
-
-
-
-
?
aldophosphamide + NAD+ + H2O
? + NADH + H+
show the reaction diagram
-
-
-
-
?
all-trans retinal + NAD+ + H2O
all-trans retinoic acid + NADH
show the reaction diagram
-
-
-
-
?
all-trans-retinal + NAD+ + H2O
all-trans-retinoic acid + NADH + H+
show the reaction diagram
-
-
-
-
?
alpha-aminoadipate semialdehyde + NAD+ + H2O
alpha-aminoadipate + NADH + H+
show the reaction diagram
-
-
-
-
?
alpha-aminoadipate semialdehyde + NAD+ + H2O
alpha-aminoadipic acid + NADH + H+
show the reaction diagram
-
-
-
-
?
alpha-phenylpropanal + NAD+ + H2O
alpha-phenylpropionate + NADH
show the reaction diagram
-
-
-
-
?
an aldehyde + NAD+ + H2O
an acid + NADH + H+
show the reaction diagram
-
-
-
-
?
benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
show the reaction diagram
betaine aldehyde + NAD+ + H2O
betaine + NADH
show the reaction diagram
-
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + H+
show the reaction diagram
-
-
-
-
?
chloroacetaldehyde + NAD+ + H2O
chloroacetate + NADH + H+
show the reaction diagram
cinnamic aldehyde + NAD+ + H2O
cinnamic acid + NADH + H+
show the reaction diagram
-
-
-
-
?
dansyl-aminoacetaldehyde + ?
dansylglycine + ?
show the reaction diagram
-
the fluorescent substrate is used to monitor aldehyde dehydrogenase activity in fluorescence-activated cell sorting
-
-
?
decanal + NAD+ + H2O
decanoate + NADH
show the reaction diagram
-
-
-
-
?
fluorene-2-carboxaldehyde + NAD+ + H2O
fluorene-2-carboxylate + NADH
show the reaction diagram
-
-
-
-
?
formaldehyde + NAD+
formate + NADH + H+
show the reaction diagram
-
-
-
?
formaldehyde + NAD+ + H2O
formate + NADH
show the reaction diagram
-
activity with enzyme ALDH-2, no activity with enzyme ALDH-1
-
-
?
formaldehyde + NAD+ + H2O
formate + NADH + H+
show the reaction diagram
glutathione-4-oxonon-2-enal + NAD+ + H2O
glutathione-4-oxonon-2-enoic acid + NADH
show the reaction diagram
-
-
-
-
?
glyceraldehyde + NAD+ + H2O
glycerate + NADH
show the reaction diagram
-
-
-
-
?
glyceraldehyde + NAD+ + H2O
glycerate + NADH + H+
show the reaction diagram
-
-
-
-
?
glyceryl trinitrate + NADH + H+
1,2-glyceryl dinitrate + nitrite + NAD+
show the reaction diagram
-
-
-
-
?
glyceryl trinitrate + NADH + H+
1,3-glyceryl dinitrate + nitrite + NAD+
show the reaction diagram
-
-
-
-
?
glycolaldehyde + NAD+ + H2O
glycolate + NADH
show the reaction diagram
-
-
-
-
?
heptanal + NAD+ + H2O
heptanoate + NADH
show the reaction diagram
-
-
-
-
?
hexanal + NAD+ + H2O
hexanoate + NADH + H+
show the reaction diagram
hydrocinnamaldehyde + NAD+ + H2O
hydrocinnamate + NADH
show the reaction diagram
-
-
-
-
?
indole-3-acetaldehyde + NAD+ + H2O
indole-3-acetate + NADH + H+
show the reaction diagram
-
-
-
-
?
indole-3-aldehyde + NAD+ + H2O
indole-3-carboxylate + NADH
show the reaction diagram
-
-
-
-
?
m-hydroxybenzaldehyde + NAD+ + H2O
m-hydroxybenzoate + NADH + H+
show the reaction diagram
-
-
-
-
?
m-methoxybenzaldehyde + NAD+ + H2O
m-methoxybenzoate + NADH + H+
show the reaction diagram
-
-
-
-
?
m-methylbenzaldehyde + NAD+ + H2O
m-methylbenzoate + NADH
show the reaction diagram
-
-
-
-
?
malondialdehyde + NAD+ + H2O
?
show the reaction diagram
-
low affinity for substrate binding and poor catalytic efficiency
-
-
?
malondialdehyde + NAD+ + H2O
? + NADH
show the reaction diagram
-
-
-
-
?
malondialdehyde + NAD+ + H2O
? + NADH + H+
show the reaction diagram
-
-
-
-
?
methylglyoxal + NAD+ + H2O
methylglyoxalate + NADH
show the reaction diagram
-
-
-
-
?
N-acetyl-4-aminobutyraldehyde + NAD+ + H2O
N-acetyl-4-aminobutyrate + NADH
show the reaction diagram
-
-
-
-
?
n-nonanal + NAD+ + H2O
n-nonanoate + NADH + H+
show the reaction diagram
nitroglycerin + NAD+ + H2O
1,2-glyceryl dinitrate + NO + NADH + H+
show the reaction diagram
-
-
-
-
?
o-hydroxybenzaldehyde + NAD+ + H2O
o-hydroxybenzoate + NADH + H+
show the reaction diagram
-
-
-
-
?
o-methoxybenzaldehyde + NAD+ + H2O
o-methoxybenzoate + NADH + H+
show the reaction diagram
-
-
-
-
?
o-methylbenzaldehyde + NAD+ + H2O
o-methylbenzoate + NADH
show the reaction diagram
-
-
-
-
?
o-nitrobenzaldehyde + NAD+ + H2O
o-nitrobenzoate + NADH
show the reaction diagram
-
-
-
-
?
octanal + NAD+ + H2O
octanoate + NADH
show the reaction diagram
-
-
-
-
?
octanal + NAD+ + H2O
octanoate + NADH + H+
show the reaction diagram
-
high specificity
-
-
?
p-(dimethylamino)-benzaldehyde + NAD+ + H2O
p-(dimethylamino)benzoate + NADH
show the reaction diagram
-
-
-
-
?
p-(dimethylamino)cinnamaldehyde + NAD+ + H2O
p-(dimethylamino)cinnamate + NADH
show the reaction diagram
-
-
-
-
?
p-methoxybenzaldehyde + NAD+ + H2O
p-methoxybenzoate + NADH + H+
show the reaction diagram
-
-
-
-
?
p-methylbenzaldehyde + NAD+ + H2O
p-methylbenzoate + NADH
show the reaction diagram
-
-
-
-
?
p-nitrobenzaldehyde + NAD+ + H2O
p-nitrobenzoate + NADH
show the reaction diagram
-
-
-
-
?
p-nitrocinnamaldehyde + NAD+ + H2O
p-nitrocinnamate + NADH
show the reaction diagram
-
-
-
-
?
pentanal + NAD+ + H2O
pentanoate + NADH
show the reaction diagram
-
-
-
-
?
phenanthrene-9-carboxaldehyde + NAD+ + H2O
phenanthrene-9-carboxylate + NADH
show the reaction diagram
-
-
-
-
?
phenylacetaldehyde + NAD+ + H2O
phenylacetate + NADH + H+
show the reaction diagram
-
-
-
-
?
propanal + 1,N6-ethenoadenine dinucleotide + H2O
propionate + ?
show the reaction diagram
-
isoenzyme E3
-
-
?
propanal + 3-acetylpyridine-adenine dinucleotide + H2O
propionate + ?
show the reaction diagram
-
isoenzyme E3
-
-
?
propanal + 3-thionicotinamide-adenine dinucleotide + H2O
propionate + ?
show the reaction diagram
-
isoenzyme E3
-
-
?
propanal + N-guanine dinucleotide + H2O
propionate + ?
show the reaction diagram
-
isoenzyme E3
-
-
?
propanal + NAD+ + H2O
propanoate + NADH + H+
show the reaction diagram
-
-
-
-
?
propanal + NAD+ + H2O
propanoic acid + NADH + H+
show the reaction diagram
-
activity assay
-
-
?
propanal + NAD+ + H2O
propionate + NADH
show the reaction diagram
propanal + NAD+ + H2O
propionate + NADH + H+
show the reaction diagram
-
-
-
-
?
propanal + oxidized nicotinamide hypoxanthine dinucleotide + H2O
propionate + reduced nicotinamide hypoxanthine dinucleotide
show the reaction diagram
-
isoenzyme E3
-
-
?
propionaldehyde + NAD+
propionate + NADH + H+
show the reaction diagram
-
-
-
?
propionaldehyde + NAD+ + H2O
propionate + NADH
show the reaction diagram
-
-
-
-
?
propionaldehyde + NAD+ + H2O
propionate + NADH + H+
show the reaction diagram
quinoline-3-carboxaldehyde + NAD+ + H2O
quinoline-3-carboxylate + NADH
show the reaction diagram
-
-
-
-
?
quinoline-4-carboxaldehyde + NAD+ + H2O
quinoline-4-carboxylate + NADH
show the reaction diagram
-
-
-
-
?
retinal + NAD+ + H2O
retinoic acid + NADH + H+
show the reaction diagram
-
-
-
?
trans-cinnamaldehyde + NAD+ + H2O
trans-cinnamate + NADH
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
alpha-aminoadipate semialdehyde + NAD+ + H2O
alpha-aminoadipate + NADH + H+
show the reaction diagram
-
-
-
?
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
show the reaction diagram
-
-
-
-
?
all-trans-retinal + NAD+ + H2O
all-trans-retinoic acid + NADH + H+
show the reaction diagram
-
-
-
-
?
alpha-aminoadipate semialdehyde + NAD+ + H2O
alpha-aminoadipate + NADH + H+
show the reaction diagram
-
-
-
-
?
an aldehyde + NAD+ + H2O
an acid + NADH + H+
show the reaction diagram
-
-
-
-
?
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADP+
-
-
additional information
-
very low activity
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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
-
2,3,5-trimethyl-6-propyl-7H-furo[3,2-g][1]benzopyran-7-one
-
2,3,5-trimethyl-6-[3-oxo-3-(piperidin-1-yl)propyl]-7H-furo[3,2-g][1]benzopyran-7-one
-
2,3-dimethyl-5-propyl-7H-furo[3,2-g][1]benzopyran-7-one
-
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
-
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-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-diethylaminobenzaldehyde
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-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-oxonon-2-enal
-
90% inhibition at 0.05 mM
4-oxonon-2-enoic acid
-
90% inhibition at 0.05 mM
5-benzyl-2,3-dimethyl-7H-furo[3,2-g][1]benzopyran-7-one
16.3% inhibition at 0.01 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
-
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
-
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
-
9,10-dimethyl-5H-6,8-dioxacyclopenta[b]phenanthren-5-one
57.8% inhibition at 0.01 mM
-
acetaldehyde
-
0.02 mM, substrate inhibition of isoenzyme I, no inhibition of isoenzyme II and III
acrolein
-
-
adenine
-
-
adenosine
-
-
adenosine 5'-monophosphate
-
competitive with NAD+ and noncompetitive with acetaldehyde
Alda-1
arsenite
-
47% residual activity at 1 mM arsenite at pH 9.5, 28% residual activity at 2 mM arsenite at pH 7.4
benomyl
Caffeine
-
-
Chloral hydrate
Chloroacetaldehyde
-
86% residual activity at 1 mM chloroacetaldehyde at pH 9.5
cyanamide
daidzin
diethylaminobenzaldehyde
0.025 mM diethylaminobenzaldehyde inhibits about 80% of the enzymatic activity
dimethyl ampal thiolester
-
78% inhibition of isozyme ALDH1 at 0.0075 mM
Disulfiram
glyceraldehyde
-
substrate inhibition
kolaflavanone
-
-
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
molinate
-
irreversible inhibition of ALDH2
molinate sulfoxide
-
i.e. S-ethyl-hexahydro-1H-azepine-1-carbothioate sulfoxide, irreversible inhibition of ALDH2
N'-methylnicotinamide
-
-
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
-
NAD+
-
pronounced inhibition occurs at above 5 mM
nitroglycerin
o-nitrobenzaldehyde
-
substrate inhibition
p-methylbenzaldehyde
-
substrate inhibition
p-nitrobenzaldehyde
-
substrate inhibition
p-nitrocinnamaldehyde
-
substrate inhibition
theophylline
-
-
thio-NAD+
-
-
[(4-methyl-2-oxo-2H-1-benzopyran-7-yl)oxy]acetonitrile
58.7% inhibition at 0.01 mM
-
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-mercaptoethanol
highest activity at 50 mM
Alda-1
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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 - 0.003
3,4-dihydroxyphenyl acetaldehyde
0.0004 - 0.0042
3,4-dihydroxyphenylacetaldehyde
0.00033
3,4-dimethoxybenzaldehyde
-
enzyme ALDH-2
0.00196
3-Pyridinecarboxaldehyde
-
enzyme ALDH-2
0.005 - 0.014
4-aminobutyrate
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
0.0179
4-hydroxynonenal
-
pH 8.0, 25°C
0.000065
4-methoxy-1-naphthaldehyde
-
enzyme ALDH-2
0.019
4-methoxybenzaldehyde
-
recombinant ALDH3A1
0.0002
4-methyoxy-1-naphthaldehyde
-
enzyme ALDH-1
0.0000063
5-(dimethylamino)-2-naphthaldehyde
-
enzyme ALDH-1
0.0000004 - 0.0000025
5-bromo-1-naphthaldehyde
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 - 0.5302
benzaldehyde
0.0411 - 0.26
Betaine aldehyde
0.0234
betaNAD+
-
isoenzyme E3
0.00055
cinnamaldehyde
-
-
0.006
cinnamic aldehyde
-
recombinant ALDH3A1
0.0000029 - 0.000022
decanal
0.000054
fluorene-2-carboxaldehyde
-
enzyme ALDH-1
0.32 - 0.42
formaldehyde
0.183
glutathione-4-oxonon-2-enal
-
-
0.205 - 7.374
glyceraldehyde
0.046
glycoaldehyde
-
isoenzyme 2, pH 7.4
0.005 - 0.24
glycolaldehyde
0.000018 - 0.000027
Heptanal
0.00003 - 0.0391
hexanal
0.0005
hydrocinnamaldehyde
-
enzyme ALDH-2
0.0007 - 0.001
indole 3-acetaldehyde
0.00015 - 0.00031
Indole-3-acetaldehyde
0.01 - 0.02
Indole-3-aldehyde
-
enzyme ALDH-2
0.00009
m-methoxybenzaldehyde
-
enzyme ALDH-2
0.000018
m-methylbenzaldehyde
-
enzyme ALDH-2
0.0043 - 0.466
malondialdehyde
0.0086 - 1.876
methylglyoxal
0.11
N-acetyl-4-aminobutyrate
-
enzyme from liver
0.944
N-guanine dinucleotide
-
isoenzyme E3
0.0008 - 0.0285
n-nonanal
0.0003 - 16
NAD+
0.0008
o-methoxybenzaldehyde
-
enzyme ALDH-2
1.3
o-methylbenzaldehyde
-
enzyme ALDH-2
0.0000063
o-nitrobenzaldehyde
-
enzyme ALDH-2
0.000012 - 0.0175
octanal
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
0.000018
p-Methoxybenzaldehyde
-
enzyme ALDH-2
0.000017
p-methylbenzaldehyde
-
enzyme ALDH-2
0.000007
p-nitrobenzaldehyde
-
enzyme ALDH-2
0.0000007
p-nitrocinnamaldehyde
-
enzyme ALDH-2
0.000034 - 0.00016
pentanal
0.000004
phenanthrene-9-carboxaldehyde
-
enzyme ALDH-2
0.000029 - 0.0055
phenylacetaldehyde
0.000008 - 1
propanal
0.0028 - 12
propionaldehyde
0.00033
quinoline-3-carboxaldehyde
-
enzyme ALDH-2
0.0028
quinoline-4-carboxaldehyde
-
enzyme ALDH-2
0.000035 - 0.0004
trans-cinnamaldehyde
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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
27.7
3-Pyridinecarboxaldehyde
-
enzyme ALDH-2
4.42
4-methoxy-1-naphthaldehyde
-
enzyme ALDH-1
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
13.2 - 19.7
acetaldehyde
0.3 - 1
alpha-aminoadipate semialdehyde
15.2
alpha-phenylpropanal
-
enzyme ALDH-2
5.83
benzaldehyde
-
enzyme ALDH-2
3.83 - 11.7
decanal
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
4.33 - 22.7
Heptanal
4.17 - 28.5
hexanal
12.3
hydrocinnamaldehyde
-
enzyme ALDH-2
9.33 - 11.3
Indole-3-acetaldehyde
1
m-hydroxybenzaldehyde
-
enzyme ALDH-2
5.83
m-methoxybenzaldehyde
-
enzyme ALDH-2
4.5
m-methylbenzaldehyde
-
enzyme ALDH-2
0.0667 - 3.5
NAD+
0.367
o-methoxybenzaldehyde
-
enzyme ALDH-2
2.75
o-methylbenzaldehyde
-
enzyme ALDH-2
1.23
o-nitrobenzaldehyde
-
enzyme ALDH-2
4.17 - 15
octanal
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
7.17
p-nitrobenzaldehyde
-
enzyme ALDH-2
0.45
p-nitrocinnamaldehyde
-
enzyme ALDH-2
8.17 - 22.8
pentanal
0.3
phenanthrene-9-carboxaldehyde
-
enzyme ALDH-2
30 - 50
phenylacetaldehyde
0.42 - 19.7
propanal
11.2
quinoline-3-carboxaldehyde
-
enzyme ALDH-2
4.67
quinoline-4-carboxaldehyde
-
enzyme ALDH-2
2.5 - 7.83
trans-cinnamaldehyde
additional information
additional information
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.6 - 4.7
alpha-aminoadipate semialdehyde
0.027 - 0.117
NAD+
0.517 - 3.13
propanal
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0074
2,6-Dichloro-4-nitrophenol
-
isoform ALDH2, in 0.1 M sodium diphosphate buffer (pH 9.5), at 21-23°C
3.5
Caffeine
-
apparent Ki value
0.17
Chloral hydrate
-
-
0.0002
Disulfiram
-
isoenzyme 1
2 - 12
methylglyoxal
0.053 - 0.133
NADH
7.3
theophylline
-
apparent Ki value
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0068 - 0.0083
1-(4-chlorophenyl)-3-(1-piperidinyl)-1-propanone
0.00019 - 0.00031
2,3,5,6-tetramethyl-7H-furo[3,2-g][1]benzopyran-7-one
-
0.00011 - 0.00036
2,3,5-trimethyl-6-propyl-7H-furo[3,2-g][1]benzopyran-7-one
-
0.002 - 0.0026
2,3,5-trimethyl-6-[3-oxo-3-(piperidin-1-yl)propyl]-7H-furo[3,2-g][1]benzopyran-7-one
-
0.000086 - 0.00036
2,3-dimethyl-5-propyl-7H-furo[3,2-g][1]benzopyran-7-one
-
0.00015
3,4,8,9-tetramethyl-7H-furo[2,3-f][1]benzopyran-7-one
Homo sapiens
pH 7.5, 25°C
-
0.00034 - 0.00088
3,5-dimethyl-6-propyl-7H-furo[3,2-g][1]benzopyran-7-one
-
0.0022 - 0.0086
3-(1-azepanyl)-1-phenyl-1-propanone
0.0025 - 0.0064
3-(dimethylamino)-1-(3-fluoro-4-methoxyphenyl)-1-propanone
0.0054 - 0.0079
3-(dimethylamino)-1-(4-ethylphenyl)-1-propanone
0.013
3-benzyl-4-methyl-2-oxo-2H-1-benzopyran-7-yl methanesulfonate
Homo sapiens
pH 7.5, 25°C
-
0.0046
6-bromo-3-[(1E)-N-hydroxyethanimidoyl]-2H-1-benzopyran-2-one
Homo sapiens
pH 7.5, 25°C
-
0.00047
6-methyl-3,4-dihydro-2H,8H-benzo[1,2-b:5,4-b']dipyran-2,8-dione
Homo sapiens
pH 7.5, 25°C
-
0.000067 - 0.00016
8,9-dimethyl-2,3-dihydrocyclopenta[c]furo[3,2-g][1]benzopyran-4(1H)-one
-
0.000067 - 0.000095
9,10-dimethyl-1,2,3,4-tetrahydro-5H-6,8-dioxacyclopenta[b]phenanthren-5-one
-
0.00015
9,10-dimethyl-5H-6,8-dioxacyclopenta[b]phenanthren-5-one
Homo sapiens
pH 7.5, 25°C
-
2.5
Caffeine
Homo sapiens
-
-
0.0035 - 0.0051
daidzin
0.0015
methyl 2-[(4-methyl-2-oxo-2H-1-benzopyran-7-yl)oxy]propanoate
Homo sapiens
pH 7.5, 25°C
-
3.5
theophylline
Homo sapiens
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.000047
-
tested group, n = 32, squamous cell cancer, mean
0.000048
-
tested group, n = 59, healthy tissue, mean
0.000049
-
tested group, n = 59, esophageal cancer, mean
0.00005
-
non-drinkers, n = 24, healthy tissue, mean
0.000051
0.000052
0.000053
-
tested group, n = 32, squamous cell cancer, median
0.000054
0.000055
-
tested group, n = 59, esophageal cancer, median
0.000058
-
drinkers, n = 35, esophageal cancer, median
0.000059
-
tested group, n = 27, adenocarcinoma, median
0.000119
-
total group, n = 44, healthy tissue, mean
0.00012
-
non-drinkers, n = 25, healthy tissue, mean
0.000123
0.000125
-
total group, n = 44, healthy tissue, median
0.000128
-
drinkers, n = 19, healthy tissue, median
0.000179
-
metastatic tumor, mean
0.00018
-
conversion of glycerol trinitrate to 1,3-glycerol dinitrate
0.000185
-
primary tumor, mean
0.000186
-
metastatic tumor, median
0.000188
-
non-drinkers, n = 25, cancer tissue, mean
0.00019
0.000192
-
primary tumor, median
0.000193
-
total group, n = 44, cancer tissue, median
0.000194
-
drinkers, n = 19, cancer tissue, mean
0.000198
-
drinkers, n = 19, cancer tissue, median
0.00066
-
conversion of glycerol trinitrate to 1,3-glycerol dinitrate
0.00088
-
-
0.003
-
conversion of glycerol trinitrate to 1,2-glycerol dinitrate
0.009
-
conversion of glycerol trinitrate to 1,2-glycerol dinitrate
0.137
-
-
0.2341
-
substrate: propionaldehyde, pH 8.0, 25°C
0.29
-
isoenzyme I
0.375
-
recombinant enzyme, using propionaldehyde as the substrate, in 50 mM sodium phosphate buffer, pH 7.4, at 37°C
0.445
-
isoenzyme III
0.462
-
-
0.5
-
isoenzyme ALDH1 from atypical liver
0.51
-
ALDH1 from usual human liver
0.54
-
isoenzyme E1
0.58
-
isoenzyme 1
0.79
-
ALDH2 from usual human liver
1.01
-
isoenzyme E2
1.3
-
isoenzyme E2
3
-
isoenzyme II
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.8
-
activity assay
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 9
-
pH 7.0: about 66% of maximal activity, pH 9.0: about 85% of maximal activity, isoenzyme 1
8 - 9.5
-
pH 8.0: about 35% of maximal activity, above pH 9.0: optimum, isoenzyme 2
8.5 - 10.5
-
pH 8.5: about 40% of the activity of isoenzyme ALDH1 and 2, pH 10.5: about 50% of the activity of isoenzyme ALDH2, about 65% of the activity of isoenzyme ALDH1
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
26
-
assay at
37
-
incubation of ALDH with 14C-labeled nitroglycerin
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.9
-
about
6.3
-
isoelectric focusing
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
aneurysm wall
Manually annotated by BRENDA team
-
increased activity in colorectal cancer cells
Manually annotated by BRENDA team
recombinant enzyme
Manually annotated by BRENDA team
-
tissue with highest content
Manually annotated by BRENDA team
-
ALDH1A1 is preferentially expressed in the CD133+ subpopulation
Manually annotated by BRENDA team
-
aldehyde dehydrogenase activity correlates with the viability of cells taken from peripheral blood stem cell grafts
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
the enzyme belongs to the aldehyde dehydrogenase (ALDH) superfamily. Enzyme ALDH16 has an extra C-terminal domain of unknown function and shows absence of the essential catalytic cysteine residue in certain non-bacterial ALDH16 sequences
malfunction
physiological function
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
AL7A1_HUMAN
539
0
58487
Swiss-Prot
Mitochondrion (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
157600
-
sedimentation equilibrium analysis, and analytical ultracentifugation
170000
-
GFP-tagged enzyme, gel filtration
208000 - 210000
-
isoenzyme I, non-denaturing PAGE
210000
-
gel filtration
216000
220000
-
isoenzyme III, gel filtration
224000
-
gel filtration
225000
230000
-
isoenzyme E2
236000
-
isoenzyme III, non-denaturing PAGE
245000
50000
50390
calculated from sequence of cDNA
51500
-
4 * 51500, SDS-PAGE
52000
-
determined by SDS-PAGE
52600
53000
-
x * 53000, enzyme form ALDH-2, SDS-PAGE
54000
54200
-
4 * 54200, isoenzyme 2, SDS-PAGE
54400
-
4 * 54400
54800
-
4 * 54800, isoenzyme 1, SDS-PAGE
55000
55450
-
MALDI-TOF mass spectrometry
56000
56108
-
-
57000
-
determined by SDS-PAGE and Western Blot analysis
58000
-
x * 58000, enzyme form ALDH-1, SDS-PAGE
85000
-
2 * 85000, GFP-tagged enzyme, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
2 * 85395, mass spectrometry
homodimer
homotetramer
tetramer
additional information
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
apoenzyme and in complex with L-2-aminoadipate or NAD+, sitting drop vapor diffusion method, using 0.1 M MgCl2, 0.1 M sodium acetate trihydrate, 0.1 M Tris-HCl (pH 8.0) and 20% (w/v) PEG 4000, or 0.1 M HEPES (pH 7.5), 0.1 M MgCl2 and 20% (w/v) PEG 3350, or 0.2 M ammonium sulfate, 20% (w/v) polyethylene glycol (PEG) 3350 and 0.1 mM Bis-Tris (pH 6.5)
complexed with NAD+ and retinoic acid, hanging drop vapor diffusion method
-
in silico modeling studies, substrate (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 is capable of binding in the active site with the amide bond near the molybdenum cofactor, orientated in such a way to enable potential nucleophilic attack on the carbonyl of the amide bond by the hydroxyl of the molybdenum cofactor
isoform ALDH2, using 100 mM Na-ACES buffer, pH 6.4-6.6, 100 mM guanidine-HCl, 10 mM MgCl2, and 4 mM dithiothreitol and 16-17% (w/v) PEG 6000
-
purified enzyme in complex with inhibitor 2, X-ray diffraction structure determination and analysis at 2.4 A resolution
sitting drop vapor diffusion method, using 20% (w/v) polyethylene glycol 3350, 10% (v/v) ethylene glycol, 0.2 M NaBr, 0.1 M Bis-Tris propane (pH 6.6)
-
sitting drop vapour diffusion method with 100 mM ACES, pH 6.6-6.8, 5-10 mM MgCl2, 100 mM guanidine HCl, 15% (w/v) PEG 6000, and 4-8 mM dithiothreitol
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
C302S
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
D80G/S82A
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
E487K
K487E
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
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
additional information
-
construction of a C-terminal truncation mutant DELTA504-511 lacking the last eight residues
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40
-
1 min, mutant enzyme R475Q loses 50% of its activity
50
-
2 min, complete loss of activity of mutant enzyme R475Q, native enzyme loses 10% of itst activity
55
-
1 min, 50% loss of activity of native enzyme
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
freezing and thawing causes loss of activity
-
half-life of wild-type enzyme and mutant enzyme R84Q in 7 M urea is 10 min, the half-life of the double-mutant enzyme S82A is less than 2 min. At 2 M urea all of the proteins are present as a mixture of native and altered state
-
urea concentrations higher than 4.5 M almost completely denature wild type isoform ALDH1A1
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 20% glycerol, less than 15% loss of activity per months
-
-70°C, liquid nitrogen, 6 months, the enzyme remains stable
-
-70°C, pH 6.0, 30 mM potassium phosphate, 1 mM EDTA, 1 nN dithiothreitol, 2 mM benzamidine, 70 mM MES, after half a year of storage with repeated freezing and thawing the activity of both ALDH-1 and ALDH-2 decrease 2fold to 3fold
-
4°C, 10 mM phosphate buffer, pH 6.8, 1 mM EDTA, 0.1% v/v 2-mercaptoethanol, stable for a week
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
5'-AMP-Sepharose 4B affinity column chromatography, gel filtration
-
5'-AMP-Sepharose 4B affinity column, 95% purity
ammonium sulfate precipitation, column chromatography, and gel filtration
-
by p-hydroxyacetophenone affinity chromatography
-
by p-hydroxyacetophenone affinity chromatography and gel filtration
-
DEAE MacroPrep column chromatography
DEAE-Sepharose chromatography
enzyme I and II
-
isoenzyme ALDH1 and ALDH2 from normal livers, ALDH1 from the atypical phenotype
-
isoenzyme E3
-
Ni-NTA chromatography and Sephacryl S200 gel filtration
-
Ni2+-Sepharose column chromatography and Superdex S200 gel filtration
-
nickel chelating Sepharose column chromatography
-
nickel column chromatography
-
p-hydroxyacetophenone Sepharose affinity column
-
recombinant ALDH3A1 is isolated with Ni-NTA Fast Start Kit
-
recombinant wild-type and mutant enzymes from Escherichia coli by nickel affinity chromatography, tag cleavage by TEV protease, dialysis, and gel filtration
-
two chromatography steps, homogeneous on SDS-PAGE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21 (DE3) cells
expressed in Escherichia coli BL21 cells
-
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli K-562 and H-1299 cells
expressed in Escherichia coli XL-1 cells
expressed in HeLa, Hep-G2 and JTC-12 cells
-
expressed in in Sf9 insect cells and in Mus musculus (highest human ALDH1B1 mRNA expression is detected in liver and part of the small intestine, moderate levels in the testis, distal colon, lung, heart, and duodenum and the lowest levels are found in the kidney and stomach)
-
expressed in Mus musculus
-
expressed in PCI-13 and SCCHN cell lines
-
expressed in Salmonella typhimurium strain TA100
-
expressed in Sf9 insect cells, in CHO cells, in human renal proximal tubular epithelial (HK-2) cells, and in Escherichia coli BL21(DE3) cells
-
expression by a baculovirus system
-
expression in Escherichia coli
expression in Escherichia coli. Chaperonin GroESL mediates the protein folding of human liver mitochondrial aldehyde dehydrogenase in Escherichia coli
-
expression in Spodoptera frugiperda cells
into the vector pET28a for expression in Escherichia coli BL21DE3 cells
-
into the vector pT7.7 for expression in Escherichia coli BL21DE3 cells
-
mutant enzymes expressed in Escherichia coli
-
recombinant expression of wild-type and mutant enzymes in Escherichia coli
-
the GFP-tagged enzyme is expressed in Escherichia coli BL21(DE3) pLysS cells
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
protein and mRNA expression of all ALDH isozymes is elevated in the mucinous and endometrioid ovarian epithelial tumors than in serous and clear cell tumors
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Inoue, K.; Nishimukai, H.; Yamasawa, K.
Purification and partial characterization of aldehyde dehydrogenase from human erythrocytes
Biochim. Biophys. Acta
569
117-123
1979
Homo sapiens
Manually annotated by BRENDA team
Wei, B.; Ni, L.; Hurley, T.D.; Weiner, H.
Cooperativity in Nicotinamide Adenine Dinucleotide Binding Induced by Mutations of Arginine 475 Located at the Subunit Interface in the Human Liver Mitochondrial Class 2 Aldehyde Dehydrogenase
Biochemistry
39
5295-5302
2000
Homo sapiens
Manually annotated by BRENDA team
Rashkovetsky, L.G.; Maret, W.; Klyosov, A.A.
Human liver aldehyde dehydrogenases: new method of purification of the major mitochondrial and cytosolic enzymes and re-evaluation of their kinetic properties
Biochim. Biophys. Acta
1205
301-307
1994
Homo sapiens
Manually annotated by BRENDA team
Farres, J.; Wang, X.; Takahashi, K.; Cunningham, S.J.; Wang, T.T.; Weiner, H.
Effects of changing glutamate 487 to lysine in rat and human liver mitochondrial aldehyde dehydrogenase. A model to study human (Oriental type) class 2 aldehyde dehydrogenase
J. Biol. Chem.
269
13854-13860
1994
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Kikonyogo, A.; Pietruszko, R.
Aldehyde dehydrogenase from adult human brain that dehydrogenates gamma-aminobutyraldehyde: purification, characterization, cloning and distribution
Biochem. J.
316
317-324
1996
Homo sapiens
Manually annotated by BRENDA team
Izaguirre, G.; Kikonyogo, A.; Pietruszko, R.
Methylglyoxal as substrate and inhibitor of human aldehyde dehydrogenase: comparison of kinetic properties among the three isoenzymes
Comp. Biochem. Physiol. B
119
747-754
1998
Homo sapiens
Manually annotated by BRENDA team
Klyosov, A.A.
Kinetics and specificity of human liver aldehyde dehydrogenases toward aliphatic, aromatic, and fused polycyclic aldehydes
Biochemistry
35
4457-4467
1996
Homo sapiens
Manually annotated by BRENDA team
Izaguirre, G.; Pietruszko, R.; Cho, S.; MacKerell, A.D., Jr.
Human aldehyde dehydrogenase catalytic activity and structural interactions with coenzyme analogs
J. Biomol. Struct. Dyn.
19
429-447
2001
Homo sapiens
Manually annotated by BRENDA team
Kurys, G.; Ambroziak, W.; Pietruszko, R.
Human aldehyde dehydrogenase. Purification and characterization of a third isozyme with low Km for gamma-aminobutyraldehyde
J. Biol. Chem.
264
4715-4721
1989
Homo sapiens
Manually annotated by BRENDA team
Ryzlak, M.T.; Pietruszko, R.
Purification and characterization of aldehyde dehydrogenase from human brain
Arch. Biochem. Biophys.
255
409-418
1987
Homo sapiens
Manually annotated by BRENDA team
Ikawa, M.; Impraim, C.C.; Wang, G.; Yoshida, A.
Isolation and characterization of aldehyde dehydrogenase isozymes from usual and atypical human livers
J. Biol. Chem.
258
6282-6287
1983
Homo sapiens
Manually annotated by BRENDA team
Pietruszko, R.; Yonetani, T.
Aldehyde dehydrogenases from liver
Methods Enzymol.
71
772-781
1981
Equus caballus, Ovis aries, Homo sapiens
Manually annotated by BRENDA team
Vallari, R.C.; Pietruszko, R.
Kinetic mechanism of the human cytoplasmic aldehyde dehydrogenase E1
Arch. Biochem. Biophys.
212
9-19
1981
Homo sapiens
Manually annotated by BRENDA team
Greenfield, N.J.; Pietruszko, R.
Two aldehyde dehydrogenases from human liver. Isolation via affinity chromatography and characterization of the isozymes
Biochim. Biophys. Acta
483
35-45
1977
Homo sapiens
Manually annotated by BRENDA team
Sidhu, R.S.; Blair, A.H.
Human liver aldehyde dehydrogenase. Kinetics of aldehyde oxidation
J. Biol. Chem.
250
7899-7904
1975
Homo sapiens
Manually annotated by BRENDA team
Lee, K.H.; Kim, H.S.; Jeong, H.S.; Lee, Y.S.
Chaperonin GroESL mediates the protein folding of human liver mitochondrial aldehyde dehydrogenase in Escherichia coli
Biochem. Biophys. Res. Commun.
298
216-224
2002
Homo sapiens
Manually annotated by BRENDA team
Rodriguez-Zavala, J.S.; Weiner, H.
Structural aspects of aldehyde dehydrogenase that influence dimer-tetramer formation
Biochemistry
41
8229-8237
2002
Homo sapiens
Manually annotated by BRENDA team
Manzer, R.; Qamar, L.; Estey, T.; Pappa, A.; Petersen, D.R.; Vasiliou, V.
Molecular cloning and baculovirus expression of the rabbit corneal aldehyde dehydrogenase (ALDH1A1) cDNA
DNA Cell Biol.
22
329-338
2003
Oryctolagus cuniculus, Homo sapiens
Manually annotated by BRENDA team
Sladek, N.E.
Human aldehyde dehydrogenases: Potential pathological, pharmacological, and toxicological impact
J. Biochem. Mol. Toxicol.
17
7-23
2003
Homo sapiens
Manually annotated by BRENDA team
Ho, K.K.; Allali-Hassani, A.; Hurley, T.D.; Weiner, H.
Differential effects of Mg2+ ions on the individual kinetic steps of human cytosolic and mitochondrial aldehyde dehydrogenases
Biochemistry
44
8022-8029
2005
Homo sapiens (P05091), Homo sapiens
Manually annotated by BRENDA team
Ho, K.K.; Hurley, T.D.; Weiner, H.
Selective alteration of the rate-limiting step in cytosolic aldehyde dehydrogenase through random mutagenesis
Biochemistry
45
9445-9453
2006
Homo sapiens (P05091), Homo sapiens
Manually annotated by BRENDA team
Hess, D.A.; Wirthlin, L.; Craft, T.P.; Herrbrich, P.E.; Hohm, S.A.; Lahey, R.; Eades, W.C.; Creer, M.H.; Nolta, J.A.
Selection based on CD133 and high aldehyde dehydrogenase activity isolates long-term reconstituting human hematopoietic stem cells
Blood
107
2162-2169
2006
Homo sapiens
Manually annotated by BRENDA team
Lioznov, M.V.; Freiberger, P.; Kroeger, N.; Zander, A.R.; Fehse, B.
Aldehyde dehydrogenase activity as a marker for the quality of hematopoietic stem cell transplants
Bone Marrow Transplant.
35
909-914
2005
Homo sapiens
Manually annotated by BRENDA team
Doorn, J.A.; Hurley, T.D.; Petersen, D.R.
Inhibition of human mitochondrial aldehyde dehydrogenase by 4-hydroxynon-2-enal and 4-oxonon-2-enal
Chem. Res. Toxicol.
19
102-110
2006
Homo sapiens
Manually annotated by BRENDA team
Lassen, N.; Estey, T.; Tanguay, R.L.; Pappa, A.; Reimers, M.J.; Vasiliou, V.
Molecular cloning, baculovirus expression, and tissue distribution of the zebrafish aldehyde dehydrogenase 2
Drug Metab. Dispos.
33
649-656
2005
Danio rerio, Homo sapiens (P05091), Homo sapiens
Manually annotated by BRENDA team
Glatt, H.; Rost, K.; Frank, H.; Seidel, A.; Kollock, R.
Detoxification of promutagenic aldehydes derived from methylpyrenes by human aldehyde dehydrogenases ALDH2 and ALDH3A1
Arch. Biochem. Biophys.
477
196-205
2008
Homo sapiens, Homo sapiens (P05091)
Manually annotated by BRENDA team
Jelski, W.; Zalewski, B.; Szmitkowski, M.
The activity of class I, II, III, and IV alcohol dehydrogenase (ADH) isoenzymes and aldehyde dehydrogenase (ALDH) in liver cancer
Digest. Dis. Sci.
53
2550-2555
2008
Homo sapiens
Manually annotated by BRENDA team
Quash, G.; Fournet, G.; Courvoisier, C.; Martinez, R.M.; Chantepie, J.; Paret, M.J.; Pharaboz, J.; Joly-Pharaboz, M.O.; Gore, J.; Andre, J.; Reichert, U.
Aldehyde dehydrogenase inhibitors: alpha,beta-acetylenic N-substituted aminothiolesters are reversible growth inhibitors of normal epithelial but irreversible apoptogens for cancer epithelial cells from human prostate in culture
Eur. J. Med. Chem.
43
906-916
2008
Homo sapiens
Manually annotated by BRENDA team
Jelski, W.; Chrostek, L.; Szmitkowski, M.
The activity of class I, II, III, and IV of alcohol dehydrogenase isoenzymes and aldehyde dehydrogenase in pancreatic cancer
Pancreas
35
142-146
2007
Homo sapiens
Manually annotated by BRENDA team
Marchitti, S.A.; Deitrich, R.A.; Vasiliou, V.
Neurotoxicity and metabolism of the catecholamine-derived 3,4-dihydroxyphenylacetaldehyde and 3,4-dihydroxyphenylglycolaldehyde: the role of aldehyde dehydrogenase
Pharmacol. Rev.
59
125-150
2007
Homo sapiens, Homo sapiens (P05091), Homo sapiens (P30837), Homo sapiens (Q9H2A2)
Manually annotated by BRENDA team
Wymore, T.; Deerfield, D.W.; Hempel, J.
Mechanistic implications of the cysteine-nicotinamide adduct in aldehyde dehydrogenase based on quantum mechanical/molecular mechanical simulations
Biochemistry
46
9495-9506
2007
Homo sapiens (P05091), Homo sapiens
Manually annotated by BRENDA team
Brodeur, H.; Parisotto, M.; Chagnon, S.; Mader, S.; Bhat, P.V.
Isomer-specific retinoic acid biosynthesis in HeLa cells expressing recombinant class I aldehyde dehydrogenases
Biochim. Biophys. Acta
1770
1548-1556
2007
Homo sapiens
Manually annotated by BRENDA team
Visus, C.; Ito, D.; Amoscato, A.; Maciejewska-Franczak, M.; Abdelsalem, A.; Dhir, R.; Shin, D.M.; Donnenberg, V.S.; Whiteside, T.L.; DeLeo, A.B.
Identification of human aldehyde dehydrogenase 1 family member A1 as a novel CD8+ T-cell-defined tumor antigen in squamous cell carcinoma of the head and neck
Cancer Res.
67
10538-10545
2007
Homo sapiens
Manually annotated by BRENDA team
Jelski, W.; Szmitkowski, M.
Alcohol dehydrogenase (ADH) and aldehyde dehydrogenase (ALDH) in the cancer diseases
Clin. Chim. Acta
395
1-5
2008
Homo sapiens
Manually annotated by BRENDA team
Gentry, T.; Foster, S.; Winstead, L.; Deibert, E.; Fiordalisi, M.; Balber, A.
Simultaneous isolation of human BM hematopoietic, endothelial and mesenchymal progenitor cells by flow sorting based on aldehyde dehydrogenase activity: implications for cell therapy
Cytotherapy
9
259-274
2007
Homo sapiens
Manually annotated by BRENDA team
Pearce, D.J.; Bonnet, D.
The combined use of Hoechst efflux ability and aldehyde dehydrogenase activity to identify murine and human hematopoietic stem cells
Exp. Hematol.
35
1437-1446
2007
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Christ, O.; Lucke, K.; Imren, S.; Leung, K.; Hamilton, M.; Eaves, A.; Smith, C.; Eaves, C.
Improved purification of hematopoietic stem cells based on their elevated aldehyde dehydrogenase activity
Haematologica
92
1165-1172
2007
Homo sapiens
Manually annotated by BRENDA team
Hui, P.; Nakayama, T.; Morita, A.; Sato, N.; Hishiki, M.; Saito, K.; Yoshikawa, Y.; Tamura, M.; Sato, I.; Takahashi, T.; Soma, M.; Izumi, Y.; Ozawa, Y.; Cheng, Z.
Common single nucleotide polymorphisms in Japanese patients with essential hypertension: aldehyde dehydrogenase 2 gene as a risk factor independent of alcohol consumption
Hypertens. Res.
30
585-592
2007
Homo sapiens
Manually annotated by BRENDA team
Hink, U.; Daiber, A.; Kayhan, N.; Trischler, J.; Kraatz, C.; Oelze, M.; Mollnau, H.; Wenzel, P.; Vahl, C.F.; Ho, K.K.; Weiner, H.; Munzel, T.
Oxidative inhibition of the mitochondrial aldehyde dehydrogenase promotes nitroglycerin tolerance in human blood vessels
J. Am. Coll. Cardiol.
50
2226-2232
2007
Homo sapiens (P05091), Homo sapiens
Manually annotated by BRENDA team
Povsic, T.J.; Zavodni, K.L.; Kelly, F.L.; Zhu, S.; Goldschmidt-Clermont, P.J.; Dong, C.; Peterson, E.D.
Circulating progenitor cells can be reliably identified on the basis of aldehyde dehydrogenase activity
J. Am. Coll. Cardiol.
50
2243-2248
2007
Homo sapiens
Manually annotated by BRENDA team
Larson, H.N.; Zhou, J.; Chen, Z.; Stamler, J.S.; Weiner, H.; Hurley, T.D.
Structural and functional consequences of coenzyme binding to the inactive Asian variant of mitochondrial aldehyde dehydrogenase: roles of residues 475 and 487
J. Biol. Chem.
282
12940-12950
2007
Homo sapiens (P05091)
Manually annotated by BRENDA team
Cheung, A.M.; Wan, T.S.; Leung, J.C.; Chan, L.Y.; Huang, H.; Kwong, Y.L.; Liang, R.; Leung, A.Y.
Aldehyde dehydrogenase activity in leukemic blasts defines a subgroup of acute myeloid leukemia with adverse prognosis and superior NOD/SCID engrafting potential
Leukemia
21
1423-1430
2007
Homo sapiens
Manually annotated by BRENDA team
Ma, S.; Chan, K.W.; Lee, T.K.; Tang, K.H.; Wo, J.Y.; Zheng, B.J.; Guan, X.Y.
Aldehyde dehydrogenase discriminates the CD133 liver cancer stem cell populations
Mol. Cancer Res.
6
1146-1153
2008
Homo sapiens
Manually annotated by BRENDA team
Wierzchowski, J.; Pietrzak, M.; Szelag, M.; Wroczynski, P.
Salivary aldehyde dehydrogenase-Reversible oxidation of the enzyme and its inhibition by caffeine, investigated using fluorimetric method
Arch. Oral Biol.
53
423-428
2008
Homo sapiens
Manually annotated by BRENDA team
Mirabelli, P.; Di Noto, R.; Lo Pardo, C.; Morabito, P.; Abate, G.; Gorrese, M.; Raia, M.; Pascariello, C.; Scalia, G.; Gemei, M.; Mariotti, E.; Del Vecchio, L.
Extended flow cytometry characterization of normal bone marrow progenitor cells by simultaneous detection of aldehyde dehydrogenase and early hematopoietic antigens: implication for erythroid differentiation studies
BMC Physiol.
8
13
2008
Homo sapiens
Manually annotated by BRENDA team
Morimoto, K.; Kim, S.J.; Tanei, T.; Shimazu, K.; Tanji, Y.; Taguchi, T.; Tamaki, Y.; Terada, N.; Noguchi, S.
Stem cell marker aldehyde dehydrogenase 1-positive breast cancers are characterized by negative estrogen receptor, positive human epidermal growth factor receptor type 2, and high Ki67 expression
Cancer Sci.
100
1062-1068
2009
Homo sapiens
Manually annotated by BRENDA team
Daiber, A.; Wenzel, P.; Oelze, M.; Schuhmacher, S.; Jansen, T.; Muenzel, T.
Mitochondrial aldehyde dehydrogenase (ALDH-2)--maker of and marker for nitrate tolerance in response to nitroglycerin treatment
Chem. Biol. Interact.
178
40-47
2009
Homo sapiens
Manually annotated by BRENDA team
Jelski, W.; Chrostek, L.; Zalewski, B.; Szmitkowski, M.
Alcohol dehydrogenase (ADH) isoenzymes and aldehyde dehydrogenase (ALDH) activity in the sera of patients with gastric cancer
Digest. Dis. Sci.
53
2101-2105
2008
Homo sapiens
Manually annotated by BRENDA team
Jelski, W.; Kozlowski, M.; Laudanski, J.; Niklinski, J.; Szmitkowski, M.
The activity of class I, II, III, and IV alcohol dehydrogenase (ADH) isoenzymes and aldehyde dehydrogenase (ALDH) in esophageal cancer
Digest. Dis. Sci.
54
725-730
2009
Homo sapiens
Manually annotated by BRENDA team
Jelski, W.; Orywal, K.; Panek, B.; Gacko, M.; Mroczko, B.; Szmitkowski, M.
The activity of class I, II, III and IV of alcohol dehydrogenase (ADH) isoenzymes and aldehyde dehydrogenase (ALDH) in the wall of abdominal aortic aneurysms
Exp. Mol. Pathol.
87
59-62
2009
Homo sapiens
Manually annotated by BRENDA team
Huellner, M.W.; Schrepfer, S.; Weyand, M.; Weiner, H.; Wimplinger, I.; Eschenhagen, T.; Rau, T.
Inhibition of aldehyde dehydrogenase type 2 attenuates vasodilatory action of nitroglycerin in human veins
FASEB J.
22
2561-2568
2008
Homo sapiens
Manually annotated by BRENDA team
Beretta, M.; Gruber, K.; Kollau, A.; Russwurm, M.; Koesling, D.; Goessler, W.; Keung, W.M.; Schmidt, K.; Mayer, B.
Bioactivation of nitroglycerin by purified mitochondrial and cytosolic aldehyde dehydrogenases
J. Biol. Chem.
283
17873-17880
2008
Homo sapiens
Manually annotated by BRENDA team
Giebultowicz, J.; Wolinowska, R.; Sztybor, A.; Pietrzak, M.; Wroczy?ski, P.; Wierzchowski, J.
Salivary aldehyde dehydrogenase: activity towards aromatic aldehydes and comparison with recombinant ALDH3A1
Molecules
14
2363-2372
2009
Homo sapiens
Manually annotated by BRENDA team
Chiang, C.P.; Wu, C.W.; Lee, S.P.; Chung, C.C.; Wang, C.W.; Lee, S.L.; Nieh, S.; Yin, S.J.
Expression pattern, ethanol-metabolizing activities, and cellular localization of alcohol and aldehyde dehydrogenases in human pancreas: implications for pathogenesis of alcohol-induced pancreatic injury
Alcohol. Clin. Exp. Res.
33
1059-1068
2009
Homo sapiens
Manually annotated by BRENDA team
Chen, C.H.; Sun, L.; Mochly-Rosen, D.
Mitochondrial aldehyde dehydrogenase and cardiac diseases
Cardiovasc. Res.
88
51-57
2010
Homo sapiens
Manually annotated by BRENDA team
Allen, E.M.; Anderson, D.G.; Florang, V.R.; Khanna, M.; Hurley, T.D.; Doorn, J.A.
Relative inhibitory potency of molinate and metabolites with aldehyde dehydrogenase 2: implications for the mechanism of enzyme inhibition
Chem. Res. Toxicol.
23
1843-1850
2010
Homo sapiens
Manually annotated by BRENDA team
Stagos, D.; Chen, Y.; Brocker, C.; Donald, E.; Jackson, B.C.; Orlicky, D.J.; Thompson, D.C.; Vasiliou, V.
Aldehyde dehydrogenase 1B1: molecular cloning and characterization of a novel mitochondrial acetaldehyde-metabolizing enzyme
Drug Metab. Dispos.
38
1679-1687
2010
Homo sapiens
Manually annotated by BRENDA team
Wenzl, M.V.; Beretta, M.; Gorren, A.C.; Zeller, A.; Baral, P.K.; Gruber, K.; Russwurm, M.; Koesling, D.; Schmidt, K.; Mayer, B.
Role of the general base Glu-268 in nitroglycerin bioactivation and superoxide formation by aldehyde dehydrogenase-2
J. Biol. Chem.
284
19878-19886
2009
Homo sapiens (P05091)
Manually annotated by BRENDA team
Brocker, C.; Lassen, N.; Estey, T.; Pappa, A.; Cantore, M.; Orlova, V.V.; Chavakis, T.; Kavanagh, K.L.; Oppermann, U.; Vasiliou, V.
Aldehyde dehydrogenase 7A1 (ALDH7A1) is a novel enzyme involved in cellular defense against hyperosmotic stress
J. Biol. Chem.
285
18452-18463
2010
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Beretta, M.; Gorren, A.C.; Wenzl, M.V.; Weis, R.; Russwurm, M.; Koesling, D.; Schmidt, K.; Mayer, B.
Characterization of the East Asian variant of aldehyde dehydrogenase-2: bioactivation of nitroglycerin and effects of Alda-1
J. Biol. Chem.
285
943-952
2010
Homo sapiens
Manually annotated by BRENDA team
Kollock, R.; Rost, K.; Batke, M.; Glatt, H.
Effect of pentachlorophenol and 2,6-dichloro-4-nitrophenol on the activity of cDNA-expressed human alcohol and aldehyde dehydrogenases
Toxicol. Lett.
191
360-364
2009
Homo sapiens
Manually annotated by BRENDA team
Mukhopadhyay, A.; Wei, B.; Weiner, H.
Mitochondrial NAD dependent aldehyde dehydrogenase either from yeast or human replaces yeast cytoplasmic NADP dependent aldehyde dehydrogenase for the aerobic growth of yeast on ethanol
Biochim. Biophys. Acta
1830
3391-3398
2013
Saccharomyces cerevisiae, Homo sapiens
Manually annotated by BRENDA team
Saw, Y.T.; Yang, J.; Ng, S.K.; Liu, S.; Singh, S.; Singh, M.; Welch, W.R.; Tsuda, H.; Fong, W.P.; Thompson, D.; Vasiliou, V.; Berkowitz, R.S.; Ng, S.W.
Characterization of aldehyde dehydrogenase isozymes in ovarian cancer tissues and sphere cultures
BMC Cancer
12
329
2012
Homo sapiens
Manually annotated by BRENDA team
Moreb, J.S.; Ucar, D.; Han, S.; Amory, J.K.; Goldstein, A.S.; Ostmark, B.; Chang, L.J.
The enzymatic activity of human aldehyde dehydrogenases 1A2 and 2 (ALDH1A2 and ALDH2) is detected by Aldefluor, inhibited by diethylaminobenzaldehyde and has significant effects on cell proliferation and drug resistance
Chem. Biol. Interact.
195
52-60
2012
Homo sapiens (P05091), Homo sapiens
Manually annotated by BRENDA team
Khanna, M.; Chen, C.H.; Kimble-Hill, A.; Parajuli, B.; Perez-Miller, S.; Baskaran, S.; Kim, J.; Dria, K.; Vasiliou, V.; Mochly-Rosen, D.; Hurley, T.D.
Discovery of a novel class of covalent inhibitor for aldehyde dehydrogenases
J. Biol. Chem.
286
43486-43494
2011
Homo sapiens
Manually annotated by BRENDA team
Yoval-Sanchez, B.; Pardo, J.P.; Rodriguez-Zavala, J.S.
New insights into the half-of-the-sites reactivity of human aldehyde dehydrogenase 1A1
Proteins
81
1330-1339
2013
Homo sapiens
Manually annotated by BRENDA team
Luo, M.; Tanner, J.J.
Structural basis of substrate recognition by aldehyde dehydrogenase 7A1
Biochemistry
54
5513-5522
2015
Homo sapiens (P49419), Homo sapiens
Manually annotated by BRENDA team
Sodhi, J.K.; Wong, S.; Kirkpatrick, D.S.; Liu, L.; Khojasteh, S.C.; Hop, C.E.; Barr, J.T.; Jones, J.P.; Halladay, J.S.
A novel reaction mediated by human aldehyde oxidase: amide hydrolysis of GDC-0834
Drug Metab. Dispos.
43
908-915
2015
Homo sapiens (P05091)
Manually annotated by BRENDA team
Belmont-Diaz, J.A.; Yoval-Sanchez, B.; Calleja-Castaneda, L.F.; Pardo Vazquez, J.P.; Rodriguez-Zavala, J.S.
Alda-1 modulates the kinetic properties of mitochondrial aldehyde dehydrogenase (ALDH2)
FEBS J.
283
3637-3650
2016
Homo sapiens
Manually annotated by BRENDA team
Moretti, A.; Li, J.; Donini, S.; Sobol, R.W.; Rizzi, M.; Garavaglia, S.
Crystal structure of human aldehyde dehydrogenase 1A3 complexed with NAD+ and retinoic acid
Sci. Rep.
6
35710
2016
Homo sapiens
Manually annotated by BRENDA team
Korasick, D.A.; Wyatt, J.W.; Luo, M.; Laciak, A.R.; Ruddraraju, K.; Gates, K.S.; Henzl, M.T.; Tanner, J.J.
Importance of the C-terminus of aldehyde dehydrogenase 7A1 for oligomerization and catalytic activity
Biochemistry
56
5910-5919
2017
Homo sapiens
Manually annotated by BRENDA team
Ma, Z.; Jiang, L.; Li, G.; Liang, D.; Li, L.; Liu, L.; Jiang, C.
Design, synthesis of 1,3-dimethylpyrimidine-2,4-diones as potent and selective aldehyde dehydrogenase 1A1 (ALDH1A1) inhibitors with glucose consumption improving activity
Bioorg. Chem.
101
103971
2020
Homo sapiens (P05091)
Manually annotated by BRENDA team
Buchman, C.D.; Hurley, T.D.
Inhibition of the aldehyde dehydrogenase 1/2 family by psoralen and coumarin derivatives
J. Med. Chem.
60
2439-2455
2017
Homo sapiens (P05091), Homo sapiens (P30837)
Manually annotated by BRENDA team
Liu, L.K.; Tanner, J.J.
Crystal structure of aldehyde dehydrogenase 16 reveals trans-hierarchical structural similarity and a new dimer
J. Mol. Biol.
431
524-541
2019
Loktanella sp., Homo sapiens (Q8IZ83), Homo sapiens
Manually annotated by BRENDA team