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Information on EC 1.2.1.36 - retinal dehydrogenase and Organism(s) Homo sapiens and UniProt Accession O94788
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1.2.1.36 retinal dehydrogenaseIUBMB Comments
A metalloflavoprotein (FAD). Acts on both the 11-trans- and 13-cis-forms of retinal.
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Word Map
- 1.2.1.36
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retinoic
- raldhs
- mesoderm
- dendritic
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all-trans
- aldh1a2
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ventral
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ra-synthesizing
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all-trans-retinoic
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cyp26s
- hindbrain
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retinol-binding
- somite
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anterior-posterior
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gut-homing
-
otic
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crabps
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ra-dependent
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ra-responsive
- molecular biology
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somitogenesis
- all-trans-retinal
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rhombomere
- synthesis
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acid-synthesizing
- diagnostics
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dorsoventral
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epicardium
- degradation
- citral
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anteroposterior
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paraxial
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ra-mediated
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rarbeta
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retinyl
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retinoid-dependent
- medicine
-
foxp3+
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raralpha
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
raldh2, retinaldehyde dehydrogenase, raldh3, retinal dehydrogenase, retinaldehyde dehydrogenase 2, retinaldehyde dehydrogenases, rdh13, retinal dehydrogenase 1, xctbp, retinaldehyde dehydrogenase-2, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
RALDH2
aldehyde dehydrogenase 1A1
ALDH1A1
Aldh1a3
cytosolic retinal dehydrogenase
-
-
-
-
dehydrogenase, retinal
-
-
-
-
NAD-dependent retinal dehydrogenases
RalDH1
RALDH3
retinaldehyde dehydrogenase 1
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
-
-
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oxidation
-
-
-
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reduction
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SYSTEMATIC NAME
IUBMB Comments
retinal:NAD+ oxidoreductase
A metalloflavoprotein (FAD). Acts on both the 11-trans- and 13-cis-forms of retinal.
CAS REGISTRY NUMBER
COMMENTARY
37250-99-0
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
10'-apo-beta-carotenal + NAD+ + H2O
10'-apo-beta-carotenoic acid + NADH + 2 H+
i.e. (2E,4E,6E,8E,10E,12E,14E)-4,9,13-trimethyl-15-(2,6,6-trimethylcyclohex-1-en-1-yl)pentadeca-2,4,6,8,10,12,14-heptaenal
-
-
?
12'-apo-beta-carotenal + NAD+ + H2O
12'-apo-beta-carotenoic acid + NADH + 2 H+
i.e. (2E,4E,6E,8E,10E,12E)-2,7,11-trimethyl-13-(2,6,6-trimethylcyclohex-1-en-1-yl)trideca-2,4,6,8,10,12-hexaenal
-
-
?
14'-apo-beta-carotenal + NAD+ + H2O
14'-apo-beta-carotenoic acid + NADH + 2 H+
i.e. (2E,4E,6E,8E,10E)-5,9-dimethyl-11-(2,6,6trimethylcyclohex-1-en-1-yl)undeca-2,4,6,8,10-pentaenal
-
-
?
all-trans retinal + NAD+ + H2O
all-trans retinoate + NADH + 2 H+
-
-
-
?
10'-apo-beta-carotenal + NAD+ + H2O
10'-apo-beta-carotenoic acid + NADH + 2 H+
i.e. (2E,4E,6E,8E,10E,12E,14E)-4,9,13-trimethyl-15-(2,6,6-trimethylcyclohex-1-en-1-yl)pentadeca-2,4,6,8,10,12,14-heptaenal
-
-
?
12'-apo-beta-carotenal + NAD+ + H2O
12'-apo-beta-carotenoic acid + NADH + 2 H+
i.e. (2E,4E,6E,8E,10E,12E)-2,7,11-trimethyl-13-(2,6,6-trimethylcyclohex-1-en-1-yl)trideca-2,4,6,8,10,12-hexaenal
-
-
?
14'-apo-beta-carotenal + NAD+ + H2O
14'-apo-beta-carotenoic acid + NADH + 2 H+
i.e. (2E,4E,6E,8E,10E)-5,9-dimethyl-11-(2,6,6trimethylcyclohex-1-en-1-yl)undeca-2,4,6,8,10-pentaenal
-
-
?
all-trans retinal + NAD+ + H2O
all-trans retinoate + NADH + 2 H+
-
-
-
?
citral + NAD+ + H2O
(2E)-3,7-dimethylocta-2,6-dienoic acid + NADH + H+
-
-
-
-
?
all-trans-retinal + H2O + NAD+
all-trans-retinoate + NADH + 2 H+
-
-
-
?
all-trans-retinal + H2O + NAD+
all-trans-retinoate + NADH + 2 H+
-
-
-
?
all-trans-retinal + H2O + NAD+
all-trans-retinoate + NADH + 2 H+
-
-
-
?
all-trans-retinal + H2O + NAD+
all-trans-retinoate + NADH + 2 H+
-
-
-
?
all-trans-retinal + H2O + NAD+
all-trans-retinoate + NADH + 2 H+
-
-
-
?
all-trans-retinal + H2O + NAD+
all-trans-retinoate + NADH + 2 H+
-
-
-
?
additional information
?
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also active with medium-chain saturated aliphatic aldehydes
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-
?
additional information
?
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no significant conversion of 17beta-, 3alpha- and 11beta-hydroxysteroids, and corresponding ketosteroids
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-
?
additional information
?
-
molecular basis of retinal recognition, comparison of enzyme from Rattus and human, overview. In contrast to long chain unsaturated substrates, the rate-limiting step of retinal oxidation by RALDHs is associated with acylation. Retinal recognition occurs in two steps: binding into the substrate access channel, and a slower structural reorganization with a rate constant of the same magnitude. The conformational transition of the RALDH-retinal complex significantly contributes to the rate-limiting step that controls the kinetics of retinal oxidation, as a prerequisite for the formation of a catalytically competent Michaelis complex. The conclusion is consistent with the general notion that structural flexibility within the active site of ALDH enzymes has been shown to be an integral component of catalysis. No activity with 2,4-decadienal, citral, and hexanal
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-
?
additional information
?
-
-
molecular basis of retinal recognition, comparison of enzyme from Rattus and human, overview. In contrast to long chain unsaturated substrates, the rate-limiting step of retinal oxidation by RALDHs is associated with acylation. Retinal recognition occurs in two steps: binding into the substrate access channel, and a slower structural reorganization with a rate constant of the same magnitude. The conformational transition of the RALDH-retinal complex significantly contributes to the rate-limiting step that controls the kinetics of retinal oxidation, as a prerequisite for the formation of a catalytically competent Michaelis complex. The conclusion is consistent with the general notion that structural flexibility within the active site of ALDH enzymes has been shown to be an integral component of catalysis. No activity with 2,4-decadienal, citral, and hexanal
-
-
?
additional information
?
-
the dissociation of NADH from the enzyme is the rate-limiting step for ALDH1A1-mediated aldehyde oxidation. ALDH1A1 can also use glutathione (GSH) and dihydrolipoic acid (DHLA) as electron donors to reduce NAD+ to NADH, product identification by thin layer chromatography (TLC). Even though they share the same NAD+-binding sites and the same active sites, the enzymatic mechanism of the GSH/DHLA-dependent NAD+-reduction activity of ALDH1A1 is distinct from its aldehyde-dehydrogenase activity
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
all-trans retinal + NAD+ + H2O
all-trans retinoate + NADH + 2 H+
-
-
-
?
all-trans retinal + NAD+ + H2O
all-trans retinoate + NADH + 2 H+
-
-
-
?
all-trans-retinal + H2O + NAD+
all-trans-retinoate + NADH + 2 H+
-
-
-
?
all-trans-retinal + H2O + NAD+
all-trans-retinoate + NADH + 2 H+
-
-
-
?
all-trans-retinal + H2O + NAD+
all-trans-retinoate + NADH + 2 H+
-
-
-
?
all-trans-retinal + H2O + NAD+
all-trans-retinoate + NADH + 2 H+
-
-
-
?
all-trans-retinal + H2O + NAD+
all-trans-retinoate + NADH + 2 H+
-
-
-
?
all-trans-retinal + H2O + NAD+
all-trans-retinoate + NADH + 2 H+
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
MgCl2
promotes the GSH/DHLA-dependent NAD+-reduction activity in a dose-dependent manner. Mg2+ exerts separate effects on the GSH/DHLA-dependent NAD+-reduction activity and the aldehyde-dehydrogenase activity of ALDH1A1
Mg2+
the presence of 1 mM magnesium ions significantly increases the activity for the natural substrate retinal of isoform RALDH3
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
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-
2,3-dimethyl-5-propyl-7H-furo[3,2-g][1]benzopyran-7-one
-
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3,5-dimethyl-6-propyl-7H-furo[3,2-g][1]benzopyran-7-one
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3-benzyl-4-methyl-2-oxo-2H-1-benzopyran-7-yl methanesulfonate
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4-dimethylamino-4-methyl-pent-2-ynthioic acid S-methyl ester
-
-
8,9-dimethyl-2,3-dihydrocyclopenta[c]furo[3,2-g][1]benzopyran-4(1H)-one
-
-
9,10-dimethyl-1,2,3,4-tetrahydro-5H-6,8-dioxacyclopenta[b]phenanthren-5-one
-
-
dichloro-all-trans-retinone
irreversible inhibitor that effectively inhibits isoform RALDH2 in the nanomolar range. I.e. (3E,5E,7E,9E)-1,1-dichloro-4,8-dimethyl-10-(2,6,6-trimethylcyclohex-1-en-1-yl)deca-3,5,7,9-tetraen-2-one
-
Mg2+
at 30 mM Mg2+, significant inhibition of activity is shown for isoform RALDH2
N,N'-(octane-1,8-diyl)bis(2,2-dichloroacetamide)
WIN 18,446, strong irreversible inhibition
-
[3-benzyl-5-(4-chlorophenyl)-1-oxopyrimido[4,5-c]quinolin-2(1H)-yl]acetic acid
a 1-oxopyrimido[4,5-c]quinoline-2-acetic acid derivative
-
1-(6-fluoro-3-(4-(methylsulfonyl)piperazine-1-carbonyl)-quinolin-4-yl)-4-phenylpiperidine-4-carbonitrile
i.e. NCT-505
-
2,3,5,6,9-pentamethyl-7H-furo[3,2-g][1]benzopyran-7-one
21.6% inhibition at 0.01 mM
-
2-(4-(4-ethylbenzoyl)piperazin-1-yl)-N-(1,3-dimethyl-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)-N-(3-methylbut-2-en-1-yl)acetamide
16.79% inhibition at 0.01 mM at pH 7.5, 25°C
-
2-(4-(4-isopropylbenzoyl)piperazin-1-yl)-N-(1,3-dimethyl-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)-N-(3-methylbut-2-en-1-yl)acetamide
14.47% inhibition at 0.01 mM at pH 7.5, 25°C
-
2-(4-(4-methoxybenzoyl)piperazin-1-yl)-N-(1,3-dimethyl-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)-N-(3-methylbut-2-en-1-yl)acetamide
29.37% inhibition at 0.01 mM at pH 7.5, 25°C
-
2-(4-(4-methylbenzoyl)piperazin-1-yl)-N-(1,3-dimethyl-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)-N-(3-methylbut-2-en-1-yl)acetamide
8.5% inhibition at 0.01 mM at pH 7.5, 25°C
-
2-[(4-methyl-2-oxo-2H-1-benzopyran-7-yl)oxy]-N-phenylacetamide
50.4% inhibition at 0.01 mM
-
2-[(4-methyl-2-oxo-2H-1-benzopyran-7-yl)oxy]acetamide
71.5% inhibition at 0.01 mM
-
2H-furo[2,3-h][1]benzopyran-2-one
39.0% inhibition at 0.01 mM
-
3,4,10-trimethyl-2H,6H-benzo[1,2-b:5,4-b']dipyran-2,6-dione
32.6% inhibition at 0.01 mM
-
3,4,8,9-tetramethyl-7H-furo[2,3-f][1]benzopyran-7-one
38.5% inhibition at 0.01 mM
-
3,4-dimethyl-6,7,8,9-tetrahydro-2H-[1]benzofuro[3,2-g][1]benzopyran-2-one
35.7% inhibition at 0.01 mM
-
3-(4-(4-(trifluoromethyl)benzoyl)piperazin-1-yl)-N-(1,3-dimethyl-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)-N-(3-methylbut-2-en-1-yl)propanamide
3.86 % inhibition at 0.01 mM at pH 7.5, 25°C
-
3-(4-(4-bromobenzoyl)piperazin-1-yl)-N-(1,3-dimethyl-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)-N-(3-methylbut-2-en-1-yl)propanamide
24.42% inhibition at 0.01 mM at pH 7.5, 25°C
-
3-(4-(4-chlorobenzoyl)piperazin-1-yl)-N-(1,3-dimethyl-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)-N-(3-methylbut-2-en-1-yl)propanamide
37.43% inhibition at 0.01 mM at pH 7.5, 25°C
-
3-(4-(4-cyanobenzoyl)piperazin-1-yl)-N-(1,3-dimethyl-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)-N-(3-methylbut-2-en-1-yl)propanamide
24.52% inhibition at 0.01 mM at pH 7.5, 25°C
-
3-(4-(4-ethylbenzoyl)piperazin-1-yl)-N-(1,3-dimethyl-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)-N-(3-methylbut-2-en-1-yl)propanamide
68.27% inhibition at 0.01 mM at pH 7.5, 25°C
-
3-(4-(4-fluorobenzoyl)piperazin-1-yl)-N-(1,3-dimethyl-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)-N-(3-methylbut-2-en-1-yl)propanamide
31.19% inhibition at 0.01 mM at pH 7.5, 25°C
-
3-(4-(4-isopropylbenzoyl)piperazin-1-yl)-N-(1,3-dimethyl-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)-N-(3-methylbut-2-en-1-yl)propanamide
77.15% inhibition at 0.01 mM at pH 7.5, 25°C
-
3-(4-(4-methoxybenzoyl)piperazin-1-yl)-N-(1,3-dimethyl-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)-N-(3-methylbut-2-en-1-yl)propanamide
60.51% inhibition at 0.01 mM at pH 7.5, 25°C
-
3-(4-(4-methylbenzoyl)piperazin-1-yl)-N-(1,3-dimethyl-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)-N-(3-methylbut-2-en-1-yl)propanamide
47.31% inhibition at 0.01 mM at pH 7.5, 25°C
-
3-(4-(4-nitrobenzoyl)piperazin-1-yl)-N-(1,3-dimethyl-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)-N-(3-methylbut-2-en-1-yl)propanamide
28.33% inhibition at 0.01 mM at pH 7.5, 25°C
-
3-(4-(cyclopropanecarbonyl)piperazin-1-yl)-N-(1,3-dimethyl-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)-N-(3-methylbut-2-en-1-yl)propanamide
0.05% inhibition at 0.01 mM at pH 7.5, 25°C
-
3-(4-(furan-2-carbonyl)piperazin-1-yl)-N-(1,3-dimethyl-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)-N-(3-methylbut-2-en-1-yl)propanamide
9.44% inhibition at 0.01 mM at pH 7.5, 25°C
-
3-(4-benzoylpiperazin-1-yl)-N-(1,3-dimethyl-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)-N-(3-methylbut-2-en-1-yl)propanamide
39.23% inhibition at 0.01 mM at pH 7.5, 25°C at pH 7.5, 25°C
-
3-(4-isonicotinoylpiperazin-1-yl)-N-(1,3-dimethyl-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)-N-(3-methylbut-2-en-1-yl)propanamide
36.65% inhibition at 0.01 mM at pH 7.5, 25°C
-
3-(4-nicotinoylpiperazin-1-yl)-N-(1,3-dimethyl-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)-N-(3-methylbut-2-en-1-yl)propanamide
30.95% inhibition at 0.01 mM at pH 7.5, 25°C
-
3-(benzo[d][1,3]dioxole-5-carbonyl)piperazin-1-yl)-N-(1,3-dimethyl-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)-N-(3-methylbut-2-en-1-yl)propanamide
35.93% inhibition at 0.01 mM at pH 7.5, 25°C
-
3-tert-butyl-5,6-dimethyl-7H-furo[3,2-g][1]benzopyran-7-one
5.5% inhibition at 0.01 mM
-
3-[(3-oxobutan-2-yl)oxy]-6H-dibenzo[b,d]pyran-6-one
41.3% inhibition at 0.01 mM
-
3-[4-(furan-2-carbonyl)piperazin-1-yl]-N-(3-methylbut-2-en-1-yl)-N-(4-methyl-2-oxo-2H-1-benzopyran-7-yl)propanamide
-
-
4-(4-(4-ethylbenzoyl)piperazin-1-yl)-N-(1,3-dimethyl-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)-N-(3-methylbut-2-en-1-yl)acetamide
27.23% inhibition at 0.01 mM at pH 7.5, 25°C
-
4-(4-(4-isopropylbenzoyl)piperazin-1-yl)-N-(1,3-dimethyl-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)-N-(3-methylbut-2-en-1-yl)acetamide
33.01% inhibition at 0.01 mM at pH 7.5, 25°C
-
4-(4-(4-methoxybenzoyl)piperazin-1-yl)-N-(1,3-dimethyl-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)-N-(3-methylbut-2-en-1-yl)acetamide
13.10% inhibition at 0.01 mM at pH 7.5, 25°C
-
4-(4-(4-methylbenzoyl)piperazin-1-yl)-N-(1,3-dimethyl-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)-N-(3-methylbut-2-en-1-yl)acetamide
32.19% inhibition at 0.01 mM at pH 7.5, 25°C
-
4-dimethylamino-4-methyl-pent-2-ynthioic acid S-methyl ester
-
-
4-methyl-7-(2-oxo-2-phenylethoxy)-2H-1-benzopyran-2-one
71.0% inhibition at 0.01 mM
-
4-methyl-7-(2-oxopropoxy)-2H-1-benzopyran-2-one
47.8% inhibition at 0.01 mM
-
4-methyl-7-[(3-methylbut-2-en-1-yl)oxy]-2H-1-benzopyran-2-one
61.7% inhibition at 0.01 mM
-
4-methyl-7-[(prop-2-en-1-yl)oxy]-2H-1-benzopyran-2-one
64.5% inhibition at 0.01 mM
-
5-benzyl-2,3-dimethyl-7H-furo[3,2-g][1]benzopyran-7-one
43.0% inhibition at 0.01 mM
-
5-methyl-2-[(3-oxobutan-2-yl)oxy]-7H-furo[3,2-g][1]benzopyran-7-one
31.3% inhibition at 0.01 mM
-
6-bromo-3-[(1E)-N-hydroxyethanimidoyl]-2H-1-benzopyran-2-one
-
-
6-methyl-3,4-dihydro-2H,8H-benzo[1,2-b:5,4-b']dipyran-2,8-dione
34.8% inhibition at 0.01 mM
-
7-(2-oxopropoxy)-2H-1-benzopyran-2-one
7.6% inhibition at 0.01 mM
-
7-(diethylamino)-4-methyl-2H-1-benzopyran-2-one
85.7% inhibition at 0.01 mM
-
7-methoxy-4-methyl-2H-1-benzopyran-2-one
19.8% 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, 75.22% inhibition at 0.01 mM at pH 7.5, 25°C at pH 7.5, 25°C
-
9,10-dimethyl-1,2,3,4-tetrahydro-5H-6,8-dioxacyclopenta[b]phenanthren-5-one
43.7% inhibition at 0.01 mM
-
9,10-dimethyl-5H-6,8-dioxacyclopenta[b]phenanthren-5-one
17.6% inhibition at 0.01 mM
-
diethylaminobenzaldehyde
DEAB, an ALDH1A1 inhibitor which competitively binds to the aldehyde-binding pocket of ALDH1A1 and completely inhibits the aldehyde oxidation activity of the enzyme at 0.01 mM, but has no effect on the GSH/DHLA-dependent NAD+-reduction activity
ethyl ([4-oxo-3-[3-(pyrrolidin-1-yl)propyl]-3,4-dihydro[1]benzothieno[3,2-d]pyrimidin-2-yl]sulfanyl)acetate
i.e. CM37
-
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-(3,5-dimethylbenzyl)-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-(4,7-dimethyl-2-oxo-2H-1-benzopyran-6-yl)-2-methylpropanamide
40.2% inhibition at 0.01 mM
-
N-(4-chlorobenzyl)-N-(1,3-dimethyl-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)-3-(4-(4-isopropylbenzoyl)piperazin-1-yl)propanamide
-
-
N-(4-fluorobenzyl)-N-(1,3-dimethyl-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)-3-(4-(4-isopropylbenzoyl)piperazin-1-yl)propanamide
-
-
N-(4-methylbenzyl)-N-(1,3-dimethyl-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)-3-(4-(4-isopropylbenzoyl)piperazin-1-yl)propanamide
-
-
N-(cyclobutylmethyl)-N-(1,3-dimethyl-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)-3-(4-(4-isopropylbenzoyl)piperazin-1-yl)propanamide
-
-
N-(cyclohexylmethyl)-N-(1,3-dimethyl-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)-3-(4-(4-isopropylbenzoyl)piperazin-1-yl)propanamide
-
-
N-(cyclopentylmethyl)-N-(1,3-dimethyl-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)-3-(4-(4-isopropylbenzoyl)piperazin-1-yl)propanamide
-
-
N-(cyclopropylmethyl)-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
6.4% inhibition at 0.01 mM
-
N-benzyl-N-(1,3-dimethyl-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)-3-(4-(4-isopropylbenzoyl)piperazin-1-yl)propanamide
-
-
N-butyl-N-(1,3-dimethyl-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)-3-(4-(4-isopropylbenzoyl)piperazin-1-yl)propanamide
-
-
N-ethyl-3-[4-(furan-2-carbonyl)piperazin-1-yl]-N-(4-methyl-2-oxo-2H-1-benzopyran-7-yl)propanamide
-
-
N-ethyl-N-(1,3-dimethyl-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)-3-(4-(4-isopropylbenzoyl)piperazin-1-yl)propanamide
-
-
N-isobutyl-N-(1,3-dimethyl-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)-3-(4-(4-isopropylbenzoyl)piperazin-1-yl)propanamide
-
-
N-isopentyl-N-(1,3-dimethyl-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)-3-(4-(4-isopropylbenzoyl)piperazin-1-yl)propanamide
-
-
N-isopropyl-N-(1,3-dimethyl-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)-3-(4-(4-isopropylbenzoyl)piperazin-1-yl)propanamide
-
-
N-propyl-N-(1,3-dimethyl-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)-3-(4-(4-isopropylbenzoyl)piperazin-1-yl)propanamide
-
-
[(4-methyl-2-oxo-2H-1-benzopyran-7-yl)oxy]acetonitrile
64.3% inhibition at 0.01 mM
-
[(5E)-2,4-dioxo-5-([4-[(4-oxo-3-phenyl-3,4-dihydroquinazolin-2-yl)methoxy]phenyl]methylidene)-1,3-thiazolidin-3-yl]acetic acid
-
[3-benzyl-5-(4-chlorophenyl)-1-oxopyrimido[4,5-c]quinolin-2(1H)-yl]acetic acid
a 1-oxopyrimido[4,5-c]quinoline-2-acetic acid derivative and a non-competitive inhibitor of ALDH1A3
-
2,3,5,6-tetramethyl-7H-furo[3,2-g][1]benzopyran-7-one
9.5% inhibition at 0.01 mM
-
2,3,5-trimethyl-6-propyl-7H-furo[3,2-g][1]benzopyran-7-one
-
-
2,3,5-trimethyl-6-propyl-7H-furo[3,2-g][1]benzopyran-7-one
63.7% 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
-
-
2,3,5-trimethyl-6-[3-oxo-3-(piperidin-1-yl)propyl]-7H-furo[3,2-g][1]benzopyran-7-one
91.3% inhibition at 0.01 mM
-
2,3-dimethyl-5-propyl-7H-furo[3,2-g][1]benzopyran-7-one
-
-
2,3-dimethyl-5-propyl-7H-furo[3,2-g][1]benzopyran-7-one
25.9% inhibition at 0.01 mM
-
3,5-dimethyl-6-propyl-7H-furo[3,2-g][1]benzopyran-7-one
-
-
3,5-dimethyl-6-propyl-7H-furo[3,2-g][1]benzopyran-7-one
51.4% inhibition at 0.01 mM
-
3-benzyl-4-methyl-2-oxo-2H-1-benzopyran-7-yl methanesulfonate
-
-
3-benzyl-4-methyl-2-oxo-2H-1-benzopyran-7-yl methanesulfonate
75.4% inhibition at 0.01 mM
-
6-benzyl-3,5-dimethyl-7H-furo[3,2-g][1]benzopyran-7-one
41.5% inhibition at 0.01 mM
-
6-benzyl-3,5-dimethyl-7H-furo[3,2-g][1]benzopyran-7-one
12.6% inhibition at 0.01 mM
-
8,9-dimethyl-2,3-dihydrocyclopenta[c]furo[3,2-g][1]benzopyran-4(1H)-one
-
-
8,9-dimethyl-2,3-dihydrocyclopenta[c]furo[3,2-g][1]benzopyran-4(1H)-one
49.2% inhibition at 0.01 mM
-
Mg2+
at 30 mM Mg2+, significant inhibition of activity is shown for isoform RALDH1
Mg2+
inhibits the aldehyde dehydrogenase activity of ALDH1A1 by inhibiting the dissociation of NADH from the enzyme
N,N'-(octane-1,8-diyl)bis(2,2-dichloroacetamide)
WIN 18,446
-
N,N'-(octane-1,8-diyl)bis(2,2-dichloroacetamide)
WIN 18,446, weak inhibition
-
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-(trifluoromethyl)benzyl)-N-(1,3-dimethyl-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)-3-(4-(4-isopropylbenzoyl)piperazin-1-yl)propanamide
6.25% inhibition at 0.01 mM at pH 7.5, 25°C
-
[(5E)-2,4-dioxo-5-([4-[(4-oxo-3-phenyl-3,4-dihydroquinazolin-2-yl)methoxy]phenyl]methylidene)-1,3-thiazolidin-3-yl]acetic acid
-
-
[(5E)-2,4-dioxo-5-([4-[(4-oxo-3-phenyl-3,4-dihydroquinazolin-2-yl)methoxy]phenyl]methylidene)-1,3-thiazolidin-3-yl]acetic acid
a 2,4-thiazolidinedione-3-acetic acid derivative
-
additional information
design and 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. All tested compounds exhibit almost no inhibition against isozyme ALDH1A2 and show excellent selectivity toward isozyme ALDH1A1
-
additional information
design and 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. All tested compounds exhibit almost no inhibition against isozyme ALDH1A2 and show excellent selectivity toward isozyme ALDH1A1
-
additional information
design and 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. All tested compounds exhibit almost no inhibition against isozyme ALDH1A2 and show excellent selectivity toward isozyme ALDH1A1
-
additional information
inhibition of the aldehyde dehydrogenase 1/2 family by psoralen and coumarin derivatives, structure-function relationships, overview. Poor or no inhibition by methyl 2-[(4-methyl-2-oxo-2H-1-benzopyran-7-yl)oxy]propanoate, 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 methyl 2-[(4-methyl-2-oxo-2H-1-benzopyran-7-yl)oxy]propanoate, 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 methyl 2-[(4-methyl-2-oxo-2H-1-benzopyran-7-yl)oxy]propanoate, 7-(diethylamino)-4-methyl-2H-1-benzopyran-2-one, and 6-bromo-3-[(1E)-N-hydroxyethanimidoyl]-2H-1-benzopyran-2-one
-
additional information
[(5E)-2,4-dioxo-5-([4-[(4-oxo-3-phenyl-3,4-dihydroquinazolin-2-yl)methoxy]phenyl]methylidene)-1,3-thiazolidin-3-yl]acetic acid, a 2,4-thiazolidinedione-3-acetic acid derivative, is inactive as inhibitor
-
additional information
[(5E)-2,4-dioxo-5-([4-[(4-oxo-3-phenyl-3,4-dihydroquinazolin-2-yl)methoxy]phenyl]methylidene)-1,3-thiazolidin-3-yl]acetic acid, a 2,4-thiazolidinedione-3-acetic acid derivative, is inactive as inhibitor
-
additional information
[(5E)-2,4-dioxo-5-([4-[(4-oxo-3-phenyl-3,4-dihydroquinazolin-2-yl)methoxy]phenyl]methylidene)-1,3-thiazolidin-3-yl]acetic acid, a 2,4-thiazolidinedione-3-acetic acid derivative, is inactive as inhibitor
-
additional information
-
if dithiothreitol is omitted from the elution buffer during RDH13-His6 purification, the purified enzyme has a very low activity, but can be reactivated by the addition of dithiothreitol. Becomes partially inactivated after 20 min of incubation at 37°C. Not inhibited at 0.05 mM by nonanal, 6-cis-nonenal and 2-trans-nonenal, glyceraldehyde and acetoacetyl-coenzyme A, taurocholic acid, 25-hydroxycholesterol and 25-nor-5-cholesten-3-ol-25b-one
-
additional information
design and synthesis of 1,3-dimethylpyrimidine-2,4-diones as potent and selective aldehyde dehydrogenase 1A1 (ALDH1A1) inhibitors with glucose consumption improving activity. 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 effectively improves glucose consumption in Hep-G2 cells compared to compound 1 (CM026). Cell viability assays with compounds 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-(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-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-(trifluoromethyl)benzyl)-N-(1,3-dimethyl-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)-3-(4-(4-isopropylbenzoyl)piperazin-1-yl)propanamide, and 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 in Hep-G2 cells. Comparison of inhibitory activities on different ALDH isozymes, overview
-
additional information
design and synthesis of 1,3-dimethylpyrimidine-2,4-diones as potent and selective aldehyde dehydrogenase 1A1 (ALDH1A1) inhibitors with glucose consumption improving activity. 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 effectively improves glucose consumption in Hep-G2 cells compared to compound 1 (CM026). Cell viability assays with compounds 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-(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-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-(trifluoromethyl)benzyl)-N-(1,3-dimethyl-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)-3-(4-(4-isopropylbenzoyl)piperazin-1-yl)propanamide, and 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 in Hep-G2 cells. Comparison of inhibitory activities on different ALDH isozymes, overview
-
additional information
design and synthesis of 1,3-dimethylpyrimidine-2,4-diones as potent and selective aldehyde dehydrogenase 1A1 (ALDH1A1) inhibitors with glucose consumption improving activity. 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 effectively improves glucose consumption in Hep-G2 cells compared to compound 1 (CM026). Cell viability assays with compounds 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-(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-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-(trifluoromethyl)benzyl)-N-(1,3-dimethyl-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)-3-(4-(4-isopropylbenzoyl)piperazin-1-yl)propanamide, and 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 in Hep-G2 cells. Comparison of inhibitory activities on different ALDH isozymes, overview
-
additional information
design and 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. Almost all tested compounds exhibit almost no inhibition against isozyme ALDH1A2 and show excellent selectivity toward isozyme ALDH1A1
-
additional information
design and 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. Almost all tested compounds exhibit almost no inhibition against isozyme ALDH1A2 and show excellent selectivity toward isozyme ALDH1A1
-
additional information
design and 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. Almost all tested compounds exhibit almost no inhibition against isozyme ALDH1A2 and show excellent selectivity toward isozyme ALDH1A1
-
additional information
inhibition of the aldehyde dehydrogenase 1/2 family by psoralen and coumarin derivatives, structure-function relationships, overview. Poor or no inhibition by daidzin, methyl 2-[(4-methyl-2-oxo-2H-1-benzopyran-7-yl)oxy]propanoate, 2-[(4-methyl-2-oxo-2H-1-benzopyran-7-yl)oxy]propanoic acid, 3-(7-hydroxy-4-methyl-2-oxo-2H-1-benzopyran-3-yl)propanoic acid, 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 daidzin, methyl 2-[(4-methyl-2-oxo-2H-1-benzopyran-7-yl)oxy]propanoate, 2-[(4-methyl-2-oxo-2H-1-benzopyran-7-yl)oxy]propanoic acid, 3-(7-hydroxy-4-methyl-2-oxo-2H-1-benzopyran-3-yl)propanoic acid, 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 daidzin, methyl 2-[(4-methyl-2-oxo-2H-1-benzopyran-7-yl)oxy]propanoate, 2-[(4-methyl-2-oxo-2H-1-benzopyran-7-yl)oxy]propanoic acid, 3-(7-hydroxy-4-methyl-2-oxo-2H-1-benzopyran-3-yl)propanoic acid, 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 daidzin, methyl 2-[(4-methyl-2-oxo-2H-1-benzopyran-7-yl)oxy]propanoate, 9,10-dimethyl-1,2,3,4-tetrahydro-5H-6,8-dioxacyclopenta[b]phenanthren-5-one, and 7-(diethylamino)-4-methyl-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 daidzin, methyl 2-[(4-methyl-2-oxo-2H-1-benzopyran-7-yl)oxy]propanoate, 9,10-dimethyl-1,2,3,4-tetrahydro-5H-6,8-dioxacyclopenta[b]phenanthren-5-one, and 7-(diethylamino)-4-methyl-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 daidzin, methyl 2-[(4-methyl-2-oxo-2H-1-benzopyran-7-yl)oxy]propanoate, 9,10-dimethyl-1,2,3,4-tetrahydro-5H-6,8-dioxacyclopenta[b]phenanthren-5-one, and 7-(diethylamino)-4-methyl-2H-1-benzopyran-2-one
-
additional information
no inhibition of ALDH1A1 by [3-benzyl-5-(4-chlorophenyl)-1-oxopyrimido[4,5-c]quinolin-2(1H)-yl]acetic acid
-
additional information
no inhibition of ALDH1A1 by [3-benzyl-5-(4-chlorophenyl)-1-oxopyrimido[4,5-c]quinolin-2(1H)-yl]acetic acid
-
additional information
no inhibition of ALDH1A1 by [3-benzyl-5-(4-chlorophenyl)-1-oxopyrimido[4,5-c]quinolin-2(1H)-yl]acetic acid
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
7-(2-oxopropoxy)-2H-1-benzopyran-2-one
activates by 6% at 0.01 mM
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0018
12'-apo-beta-carotenal
isoform ALDH1A2, at pH 8.0 and 37°C
-
0.005
14'-apo-beta-carotenal
isoform ALDH1A2, at pH 8.0 and 37°C
0.003
12'-apo-beta-carotenal
isoform ALDH1A3, at pH 8.0 and 37°C
-
0.012
14'-apo-beta-carotenal
isoform ALDH1A1, at pH 8.0 and 37°C
0.095
3-deoxyglucosone
-
partially purified recombinant ALDH1A1 at pH 7.1 and in the presence of 1 mM NAD
0.085
NAD+
-
partially purified recombinant ALDH1A1 at pH 7.1 and in the presence of 0.1 mM 3-deoxyglucosone
0.0081
all-trans-retinal
pH 8.5, 25°C, recombinant wild-type ALDH1A1 enzyme
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics and pre-steady-state kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics and pre-steady-state kinetics
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.142
12'-apo-beta-carotenal
isoform ALDH1A2, at pH 8.0 and 37°C
-
0.078
14'-apo-beta-carotenal
isoform ALDH1A2, at pH 8.0 and 37°C
0.022
12'-apo-beta-carotenal
isoform ALDH1A3, at pH 8.0 and 37°C
-
0.052
14'-apo-beta-carotenal
isoform ALDH1A1, at pH 8.0 and 37°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
80
12'-apo-beta-carotenal
isoform ALDH1A2, at pH 8.0 and 37°C
-
15.5
14'-apo-beta-carotenal
isoform ALDH1A2, at pH 8.0 and 37°C
0.733
12'-apo-beta-carotenal
isoform ALDH1A1, at pH 8.0 and 37°C
-
7.5
12'-apo-beta-carotenal
isoform ALDH1A3, at pH 8.0 and 37°C
-
4.28
14'-apo-beta-carotenal
isoform ALDH1A1, at pH 8.0 and 37°C
5.05
14'-apo-beta-carotenal
isoform ALDH1A3, at pH 8.0 and 37°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00006435
dichloro-all-trans-retinone
isoform RALDH2, at pH 8.2 and 25°C
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00033
2,3,5,6-tetramethyl-7H-furo[3,2-g][1]benzopyran-7-one
Homo sapiens
pH 7.5, 25°C
-
0.0003
2,3,5-trimethyl-6-propyl-7H-furo[3,2-g][1]benzopyran-7-one
Homo sapiens
pH 7.5, 25°C
-
0.0016
2,3,5-trimethyl-6-[3-oxo-3-(piperidin-1-yl)propyl]-7H-furo[3,2-g][1]benzopyran-7-one
Homo sapiens
pH 7.5, 25°C
-
0.000069
2,3-dimethyl-5-propyl-7H-furo[3,2-g][1]benzopyran-7-one
Homo sapiens
pH 7.5, 25°C
-
0.00076
3,5-dimethyl-6-propyl-7H-furo[3,2-g][1]benzopyran-7-one
Homo sapiens
pH 7.5, 25°C
-
0.011
3-benzyl-4-methyl-2-oxo-2H-1-benzopyran-7-yl methanesulfonate
Homo sapiens
pH 7.5, 25°C
-
0.00013
8,9-dimethyl-2,3-dihydrocyclopenta[c]furo[3,2-g][1]benzopyran-4(1H)-one
Homo sapiens
pH 7.5, 25°C
-
0.000065
9,10-dimethyl-1,2,3,4-tetrahydro-5H-6,8-dioxacyclopenta[b]phenanthren-5-one
Homo sapiens
pH 7.5, 25°C
-
0.00019132
dichloro-all-trans-retinone
Homo sapiens
isoform RALDH2, at pH 8.2 and 25°C
-
0.00007
N,N'-(octane-1,8-diyl)bis(2,2-dichloroacetamide)
Homo sapiens
pH 8.0, 25°C, recombinant enzyme
-
0.0095
N,N-diethylaminobenzaldehyde
Homo sapiens
pH 8.0, 25°C, recombinant enzyme
-
0.0035
[3-benzyl-5-(4-chlorophenyl)-1-oxopyrimido[4,5-c]quinolin-2(1H)-yl]acetic acid
Homo sapiens
pH 8.0, 25°C, recombinant enzyme
-
0.00027
2,3,5,6-tetramethyl-7H-furo[3,2-g][1]benzopyran-7-one
Homo sapiens
pH 7.5, 25°C
-
0.0004
2,3,5-trimethyl-6-propyl-7H-furo[3,2-g][1]benzopyran-7-one
Homo sapiens
pH 7.5, 25°C
-
0.00013 - 0.014
2,3,5-trimethyl-6-[3-oxo-3-(piperidin-1-yl)propyl]-7H-furo[3,2-g][1]benzopyran-7-one
-
0.0011
3,5-dimethyl-6-propyl-7H-furo[3,2-g][1]benzopyran-7-one
Homo sapiens
pH 7.5, 25°C
-
0.01
3-benzyl-4-methyl-2-oxo-2H-1-benzopyran-7-yl methanesulfonate
Homo sapiens
pH 7.5, 25°C
-
0.00017
8,9-dimethyl-2,3-dihydrocyclopenta[c]furo[3,2-g][1]benzopyran-4(1H)-one
Homo sapiens
pH 7.5, 25°C
-
0.00121
8-[[4-(3-furoyl)-1-piperazinyl]methyl]-1,3-dimethyl-7-(3-methylbutyl)-3,7-dihydro-1H-purine-2,6-dione
Homo sapiens
pH 7.5, 25°C
-
0.00013
9,10-dimethyl-1,2,3,4-tetrahydro-5H-6,8-dioxacyclopenta[b]phenanthren-5-one
Homo sapiens
pH 7.5, 25°C
-
0.000059
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
Homo sapiens
pH 7.5, 25°C
-
0.000126
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
Homo sapiens
pH 7.5, 25°C
-
0.000429
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
Homo sapiens
pH 7.5, 25°C
-
0.000872
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
Homo sapiens
pH 7.5, 25°C
-
0.000149
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
Homo sapiens
pH 7.5, 25°C
-
0.000379
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
Homo sapiens
pH 7.5, 25°C
-
0.000385
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
Homo sapiens
pH 7.5, 25°C
-
0.001075
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
Homo sapiens
pH 7.5, 25°C
-
0.000966
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
Homo sapiens
pH 7.5, 25°C
-
0.000715
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
Homo sapiens
pH 7.5, 25°C
-
0.001144
N-(4-methylbenzyl)-N-(1,3-dimethyl-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)-3-(4-(4-isopropylbenzoyl)piperazin-1-yl)propanamide
Homo sapiens
pH 7.5, 25°C
-
0.001135
N-benzyl-N-(1,3-dimethyl-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)-3-(4-(4-isopropylbenzoyl)piperazin-1-yl)propanamide
Homo sapiens
pH 7.5, 25°C
-
0.0054 - 0.023
[(5E)-2,4-dioxo-5-([4-[(4-oxo-3-phenyl-3,4-dihydroquinazolin-2-yl)methoxy]phenyl]methylidene)-1,3-thiazolidin-3-yl]acetic acid
-
0.0012
[3-benzyl-5-(4-chlorophenyl)-1-oxopyrimido[4,5-c]quinolin-2(1H)-yl]acetic acid
Homo sapiens
pH 8.0, 25°C, recombinant enzyme
-
0.00013
2,3,5-trimethyl-6-[3-oxo-3-(piperidin-1-yl)propyl]-7H-furo[3,2-g][1]benzopyran-7-one
Homo sapiens
pH 7.5, 25°C
-
0.014
2,3,5-trimethyl-6-[3-oxo-3-(piperidin-1-yl)propyl]-7H-furo[3,2-g][1]benzopyran-7-one
Homo sapiens
pH 7.5, 25°C
-
0.031
N,N'-(octane-1,8-diyl)bis(2,2-dichloroacetamide)
Homo sapiens
pH 8.0, 25°C, recombinant enzyme
-
0.056
N,N'-(octane-1,8-diyl)bis(2,2-dichloroacetamide)
Homo sapiens
pH 8.0, 25°C, recombinant enzyme
-
0.00018
N,N-diethylaminobenzaldehyde
Homo sapiens
pH 8.0, 25°C, recombinant enzyme
-
0.047
N,N-diethylaminobenzaldehyde
Homo sapiens
pH 8.0, 25°C, recombinant enzyme
-
0.0054
[(5E)-2,4-dioxo-5-([4-[(4-oxo-3-phenyl-3,4-dihydroquinazolin-2-yl)methoxy]phenyl]methylidene)-1,3-thiazolidin-3-yl]acetic acid
Homo sapiens
pH 8.0, 25°C, recombinant enzyme
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
7.5
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
25
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
additional information
ALDH1A1 is highly expressed in lung carcinoma cell line A549 and EKVX, as well as in the large cell carcinoma cell line H460. Isozyme ALDH3A1 (EC 1.2.1.5) shows a similar expression pattern like ALDH1A1. Other members of the aldehyde dehydrogenase family are not expressed in the lung cancer cell lines examined
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
the enzyme plays a role in the physiological metabolism of apocarotenoids
physiological function
the cytosolic isozymes ALDH1A1, ALDH1A2, and ALDH1A3 play important roles in cell signaling via oxidation of retinaldehyde to retinoic acid. In the cell, retinoic acid produced in the cytoplasm binds to cellular retinoic acid binding protein type II, and is transferred to the nucleus where it binds to heterodimers of retinoic acid receptor (RAR) and retinoid X receptor (RXR). Once activated, these receptor complexes bind to retinoic acid response elements (RAREs), which are regulatory sequences that induce gene transcription and modulate a wide range of biological processes, including cell proliferation, differentiation, cell cycle arrest and apoptosis
evolution
aldehyde dehydrogenase 1A1 (ALDH1A1) is a member of the aldehyde dehydrogenase superfamily that oxidizes aldehydes to their corresponding acids, reactions that are coupled to the reduction of NAD+ to NADH
malfunction
H-1299 cells expressing C302A, E107G, and I304K mutant forms of ALDH1A1 lacked aldehyde-dehydrogenase activity
metabolism
physiological function
metabolism
ALDH1A1 and ALDH3A1 have the same GSH/DHLA-dependent NAD+-reduction activity
metabolism
the enzyme plays a role in the physiological metabolism of apocarotenoids
physiological function
aldehyde dehydrogenase 1A1 increases NADH levels and promotes tumor growth via glutathione/dihydrolipoic acid-dependent NAD+ reduction. ALDH1A1 can also use glutathione (GSH) and dihydrolipoic acid (DHLA) as electron donors to reduce NAD+ to NADH. The GSH/DHLA-dependent NAD+-reduction activity of ALDH1A1 is not affected by the aldehyde dehydrogenase inhibitor or by mutation of the residues in its aldehyde-binding pocket. It is thus a distinct biochemical reaction from the classic aldehyde-dehydrogenase activity catalyzed by ALDH1A1. The GSH/DHLA-dependent NAD+-reduction activity of ALDH1A1 can decrease cellular NAD(P)+/NAD(P)H ratio and promote tumor growth. The tumor-promoting effect of ALDH1A1 is achieved, at least partially, through decreasing the cellular NAD+/ NADH ratio
physiological function
-
ALDH1A1 contributes to protection of A-549 cells against retinaldehyde toxicity. ALDH1 confers protection against retinaldehyde toxicity in cancer cells
physiological function
ALDH1A1 is a NAD+-dependent aldehyde dehydrogenase that participates in multiple metabolic pathways and has been indicated to play an important role in obesity and diabetes
physiological function
-
retinal dehydrogenase 5 is an important enzyme in the visual cycle and plays a crucial role in suppressing proliferation and metastasis in hepatocellular carcinoma
physiological function
the cytosolic isozymes ALDH1A1, ALDH1A2, and ALDH1A3 play important roles in cell signaling via oxidation of retinaldehyde to retinoic acid. In the cell, retinoic acid produced in the cytoplasm binds to cellular retinoic acid binding protein type II, and is transferred to the nucleus where it binds to heterodimers of retinoic acid receptor (RAR) and retinoid X receptor (RXR). Once activated, these receptor complexes bind to retinoic acid response elements (RAREs), which are regulatory sequences that induce gene transcription and modulate a wide range of biological processes, including cell proliferation, differentiation, cell cycle arrest and apoptosis
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). AL1A2_HUMAN
518
0
56724
Swiss-Prot
other Location (Reliability: 1)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
tetramer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified enzyme in complex with inhibitors 2,3,5-trimethyl-6-[3-oxo-3-(piperidin-1-yl)propyl]-7H-furo[3,2-g][1]benzopyran-7-one, 7-(diethylamino)-4-methyl-2H-1-benzopyran-2-one, and 3-benzyl-4-methyl-2-oxo-2H-1-benzopyran-7-yl methanesulfonate, X-ray diffraction structure determination and analysis at 1.70-2.05 A resolution
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C302A
site-directed mutagenesis of catalytic active center residue, the mutant ALDH1A1 loses both activities
C303A
site-directed mutagenesis of catalytic active center residue, the mutant ALDH1A1 loses both activities
C456A
site-directed mutagenesis of a cysteine residue outside the active center, the mutation has no effect on both the aldehyde-dehydrogenase activity and the GSH/DHLA-dependent NAD+-reduction activity
E107G
site-directed mutagenesis, mutation of a residue that contributes to conformational integrity, the mutant loses its aldehyde-dehydrogenase activity, yet completely retains its GSH/DHLA-dependent NAD+-reduction activity
G246A/G251A
site-directed mutagenesis of NAD+-binding sites, the mutant ALDH1A1 loses both the aldehyde-dehydrogenase activity and the GSH/DHLA-dependent NAD+-reduction activity
I304K
site-directed mutagenesis, the mutant loses its aldehyde-dehydrogenase activity
K127A
N120A
W178E/I304K
site-directed mutagenesis, mutation of aldehyde binding residues W178 and I304, the mutant loses its aldehyde-dehydrogenase activity, yet completely retains its GSH/DHLA-dependent NAD+-reduction activity
Y296A
Y296V
additional information
ectopic expression of ALDH1A1 decreases the intracellular NAD+/NADH ratio, while knockout of ALDH1A1 increases the NAD+/NADH ratio. Simultaneous knockout of ALDH1A1 and its isozyme ALDH3A1 (EC 1.2.1.5) in lung cancer cell line NCI-H460 inhibits tumor growth in a xenograft model. Moreover, the ALDH1A1 mutants that retain their GSH/DHLA-dependent NAD+ reduction activity and lose their aldehyde-dehydrogenase activity are able to decrease the NAD+/NADH ratio and to rescue the impaired growth of ALDH1A1/3A1 double knockout tumor cells. H-1299 cells expressing C302A, E107G, and I304K mutant forms of ALDH1A1 lack aldehyde-dehydrogenase activity
K127A
site-directed mutagenesis, the mutant shows reduced activity with retinoic acid compared to the wild-type enzyme
N120A
site-directed mutagenesis, the mutant shows reduced activity with retinoic acid compared to the wild-type enzyme
Y296A
site-directed mutagenesis, the mutant shows reduced activity with retinoic acid compared to the wild-type enzyme
Y296V
site-directed mutagenesis, the mutant shows reduced activity with retinoic acid compared to the wild-type enzyme
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
nickel chelating resin column chromatography and Superdex 200 gel filtration
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3)pLys by nickel affinity chromatography
by gel filtration, more than 400fold with a yield of about 1%, to near homogeneity
-
nickel chelating resin column chromatography and Superdex 200 gel filtration
purification of the enzyme(s) responsible for the GSH/DHLA-dependent NAD+ reduction activity from large-scale cell cultures, native enzyme from EKVX lung cancer cells by ultracentrifugation of crude cell extract and anion echange chromatography, hydrophobic interaction and hydroxyapatite chromatography, followed by gel filtration and another different step of anion exchange chromatography
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3)pLys by nickel affinity chromatography
recombinant N-terminally His-tagged wild-type and mutant enzymes from Escherichia coli strain C41(DE3) by nickel affinityy chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene ALDH1A1, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)pLys
cloned into the pET28a vector. Expressed in Sf9 cells as a fusion with the C-terminal His6 tag
-
gene ALDH1A1, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)pLys
gene ALDH1A1, recombinant expression of N-terminally His-tagged wild-type and mutant enzymes in Escherichia coli strain C41(DE3)
recombinant H1299 cells expressing C302A, E107G, and I304K mutant forms of ALDH1A1 lack aldehyde-dehydrogenase activity
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
mRNA expression is upregulated by p53 (44.3fold) and p63gamma (16.3fold) by binding to the retSDR1 promoter in vivo
-
retinal dehydrogenase 5 is significantly downregulated in hepatocellular carcinoma tissues
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
degradation
-
urinary excretion of 2-keto-3-deoxygluconate amounts to 16.7 micromol/g creatinine in humans, indicating that 3-deoxyglucosone may be quantitatively a more important substrate than retinaldehyde for ALDH1A1
medicine
additional information
medicine
-
retinoic acid down-regulates aldehyde dehydrogenase and increases cytotoxicity of 4-hydroperoxycyclophosphamide and acetaldehyde in lung cancer cell lines
medicine
-
low retinal dehydrogenase 5 expression is associated with metastasis and poor patient prognosis
additional information
-
RDH13 is significantly different from related RDH11, RDH12 and RDH14 in that it is targeted to the mitochondria, but at the same time, RDH13 is very similar to the members of the RDH11-14 cluster of short-chain dehydrogenases/reductases in terms of its substrate and cofactor preferences. It may function to protect mitochondria against oxidative stress associated with the highly reactive retinaldehyde produced from dietary beta-carotene
additional information
-
similar localization of Rdh12 and RDH12 proteins in mouse and human photoreceptors, respectively, which may indicate an analogous physiological role of the enzymes in both species
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Sladek, N.E.
Human aldehyde dehydrogenases: Potential pathological, pharmacological, and toxicological impact
J. Biochem. Mol. Toxicol.
17
7-23
2003
Homo sapiens
Moreb, J.S.; Gabr, A.; Vartikar, G.R.; Gowda, S.; Zucali, J.R.; Mohuczy, D.
Retinoic acid down-regulates aldehyde dehydrogenase and increases cytotoxicity of 4-hydroperoxycyclophosphamide and acetaldehyde
J. Pharmacol. Exp. Ther.
312
339-345
2005
Homo sapiens
Belyaeva, O.V.; Korkina, O.V.; Stetsenko, A.V.; Kedishvili, N.Y.
Human retinol dehydrogenase 13 (RDH13) is a mitochondrial short-chain dehydrogenase/reductase with a retinaldehyde reductase activity
FEBS J.
275
138-147
2008
Homo sapiens
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 (O94788)
Collard, F.; Vertommen, D.; Fortpied, J.; Duester, G.; Van Schaftingen, E.
Identification of 3-deoxyglucosone dehydrogenase as aldehyde dehydrogenase 1A1 (retinaldehyde dehydrogenase 1)
Biochimie
89
369-373
2007
Homo sapiens, Mus musculus
Kurth, I.; Thompson, D.A.; Ruether, K.; Feathers, K.L.; Chrispell, J.D.; Schroth, J.; McHenry, C.L.; Schweizer, M.; Skosyrski, S.; Gal, A.; Huebner, C.A.
Targeted disruption of the murine retinal dehydrogenase gene Rdh12 does not limit visual cycle function
Mol. Cell. Biol.
27
1370-1379
2007
Homo sapiens, Mus musculus
Kirschner, R.D.; Rother, K.; Mueller, G.A.; Engeland, K.
The retinal dehydrogenase/reductase retSDR1/DHRS3 gene is activated by p53 and p63 but not by mutants derived from tumors or EEC/ADULT malformation syndromes
Cell Cycle
9
2177-2188
2010
Homo sapiens
Bchini, R.; Vasiliou, V.; Branlant, G.; Talfournier, F.; Rahuel-Clermont, S.
Retinoic acid biosynthesis catalyzed by retinal dehydrogenases relies on a rate-limiting conformational transition associated with substrate recognition
Chem. Biol. Interact.
202
78-84
2013
Homo sapiens, Rattus norvegicus
Bchini, R.; Vasiliou, V.; Branlant, G.; Talfournier, F.; Rahuel-Clermont, S.
Retinoic acid biosynthesis catalyzed by retinal dehydrogenases relies on a rate-limiting conformational transition associated with substrate recognition
Chem. Biol. Interact.
202
78-84
2013
Homo sapiens (P00352), Homo sapiens, Rattus norvegicus (Q63639)
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 (O94788), Homo sapiens (P00352), Homo sapiens (P47895)
Harper, A.R.; Le, A.T.; Mather, T.; Burgett, A.; Berry, W.; Summers, J.A.
Design, synthesis, and ex vivo evaluation of a selective inhibitor for retinaldehyde dehydrogenase enzymes
Bioorg. Med. Chem.
26
5766-5779
2018
Gallus gallus, Gallus gallus (O93344), Gallus gallus (P27463), Homo sapiens (O94788)
Bui, T.B.C.; Nosaki, S.; Kokawa, M.; Xu, Y.; Kitamura, Y.; Tanokura, M.; Hachimura, S.; Miyakawa, T.
Evaluation of spice and herb as phyto-derived selective modulators of human retinaldehyde dehydrogenases using a simple in vitro method
Biosci. Rep.
41
BSR20210491
2021
Homo sapiens (O94788), Homo sapiens (P00352), Homo sapiens (P47895), Homo sapiens
Jimenez, R.; Pequerul, R.; Amor, A.; Lorenzo, J.; Metwally, K.; Aviles, F.X.; Pares, X.; Farres, J.
Inhibitors of aldehyde dehydrogenases of the 1A subfamily as putative anticancer agents kinetic characterization and effect on human cancer cells
Chem. Biol. Interact.
306
123-130
2019
Homo sapiens (O94788), Homo sapiens (P00352), Homo sapiens (P47895)
Hu, H.; Xu, L.; Luo, S.J.; Xiang, T.; Chen, Y.; Cao, Z.R.; Zhang, Y.J.; Mo, Z.; Wang, Y.; Meng, D.F.; Yu, L.; Lin, L.Z.; Zhang, S.J.
Retinal dehydrogenase 5 (RHD5) attenuates metastasis via regulating HIPPO/YAP signaling pathway in hepatocellular carcinoma
Int. J. Med. Sci.
17
1897-1908
2020
Homo sapiens
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 (O94788), Homo sapiens (P00352), Homo sapiens (P47895)
Wang, B.; Chen, X.; Wang, Z.; Xiong, W.; Xu, T.; Zhao, X.; Cao, Y.; Guo, Y.; Li, L.; Chen, S.; Huang, S.; Wang, X.; Fang, M.; Shen, Z.
Aldehyde dehydrogenase 1A1 increases NADH levels and promotes tumor growth via glutathione/dihydrolipoic acid-dependent NAD+ reduction
Oncotarget
8
67043-67055
2017
Homo sapiens (P00352)
Park, J.W.; Jung, K.H.; Lee, J.H.; Moon, S.H.; Cho, Y.S.; Lee, K.H.
Inhibition of aldehyde dehydrogenase 1 enhances the cytotoxic effect of retinaldehyde on A549 cancer cells
Oncotarget
8
99382-99393
2017
Homo sapiens
Dominguez, M.; Pequerul, R.; Alvarez, R.; Gimenez-Dejoz, J.; Birta, E.; Porte, S.; Ruehl, R.; Pares, X.; Farres, J.; de Lera, A.
Synthesis of apocarotenoids by acyclic cross metathesis and characterization as substrates for human retinaldehyde dehydrogenases
Tetrahedron
74
2567-2574
2018
Homo sapiens (O94788), Homo sapiens (P00352), Homo sapiens (P47895)
-
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