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1,2-Cyclohexanedione
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33% residual activity at 2.5 mM
2,3,5-trimethyl-6-propyl-7H-furo[3,2-g][1]benzopyran-7-one
13.7% inhibition at 0.01 mM
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2,3-dimethyl-5-propyl-7H-furo[3,2-g][1]benzopyran-7-one
19.6% inhibition at 0.01 mM
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2,4-Dinitro-1-fluorobenzene
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11% residual activity at 2.5 mM
2-mercaptoethanol
10% (v/v), 55% inhibition
2-[(4-methyl-2-oxo-2H-1-benzopyran-7-yl)oxy]acetamide
32.9% inhibition at 0.01 mM
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2-[(4-methyl-2-oxo-2H-1-benzopyran-7-yl)oxy]propanoic acid
6.1% inhibition at 0.01 mM
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2H-furo[2,3-h][1]benzopyran-2-one
71.7% inhibition at 0.01 mM
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3,4,10-trimethyl-2H,6H-benzo[1,2-b:5,4-b']dipyran-2,6-dione
20.8% inhibition at 0.01 mM
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3-benzyl-4-methyl-2-oxo-2H-1-benzopyran-7-yl methanesulfonate
13.1% inhibition at 0.01 mM
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3-tert-butyl-5,6-dimethyl-7H-furo[3,2-g][1]benzopyran-7-one
13.0% inhibition at 0.01 mM
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3-thionicotinamide adenine dinucleotide
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strong inhibition versus beta-NAD+, isoenzyme E2; substrate inhibition, isoenzyme E1
4-methyl-7-(2-oxo-2-phenylethoxy)-2H-1-benzopyran-2-one
32.9% inhibition at 0.01 mM
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4-methyl-7-(2-oxopropoxy)-2H-1-benzopyran-2-one
35.9% inhibition at 0.01 mM
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4-methyl-7-[(3-methylbut-2-en-1-yl)oxy]-2H-1-benzopyran-2-one
76.4% inhibition at 0.01 mM
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4-methyl-7-[(prop-2-en-1-yl)oxy]-2H-1-benzopyran-2-one
90.5% inhibition at 0.01 mM
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5-benzyl-2,3-dimethyl-7H-furo[3,2-g][1]benzopyran-7-one
18.4% inhibition at 0.01 mM
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6-benzyl-3,5-dimethyl-7H-furo[3,2-g][1]benzopyran-7-one
11.1% inhibition at 0.01 mM; 9.7% inhibition at 0.01 mM
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6-bromo-3-[(1E)-N-hydroxyethanimidoyl]-2H-1-benzopyran-2-one
8.3% inhibition at 0.01 mM
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6-methyl-3,4-dihydro-2H,8H-benzo[1,2-b:5,4-b']dipyran-2,8-dione
46.4% inhibition at 0.01 mM
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7-methoxy-4-methyl-2H-1-benzopyran-2-one
63.6% inhibition at 0.01 mM
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8,9-dimethyl-2,3-dihydrocyclopenta[c]furo[3,2-g][1]benzopyran-4(1H)-one
12.9% inhibition at 0.01 mM
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9,10-dimethyl-1,2,3,4-tetrahydro-5H-6,8-dioxacyclopenta[b]phenanthren-5-one
5.9% inhibition at 0.01 mM
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9,10-dimethyl-5H-6,8-dioxacyclopenta[b]phenanthren-5-one
6.6% inhibition at 0.01 mM
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acetaldehyde
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strong substrate inhibition
acetone
10% (v/v), 21% inhibition
benomyl
potent irreversible inhibitor of ALDH. Benomyl increases superoxide production as much as nitroglycerin
benzoate
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non-competitive with respect to either NAD+ or benzaldehyde
beta-NADP+
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substrate inhibition, isoenzyme E1
Cd2+
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100% inhibition at 1 mM; 1 mM, 100% inhibition
Co2+
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89% residual activity at 1 mM
diethyl dicarbonate
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2% residual activity at 2.5 mM
dimethyl ampal thiolester
complete inhibition of isozyme ALDH3 at 0.0075 mM
DMSO
10% (v/v), 32% inhibition
EDTA
50 mM, 22% inhibition
ethanediol
10% (v/v), 60% inhibition
ethyl acetimidate
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71% residual activity at 250 mM
Fe2+
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88% residual activity at 1 mM
guanidine hydrochloride
10% (v/v), 42% inhibition
H2O2
the loss of activity induced by H2O2 can be restored by reducing agents, although a decrease of the restored activity is observed upon addition of 10 mM dithiothreitol
kolaflavanone
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the enzyme shows crucial non-canonical and non-catalytic interaction with kolaflavanone, a component of kolaviron, and a major bioflavonoid isolated from Garcinia kola (Bitter kola). The enzyme has one binding site for kolaflavanone with a binding constant (Ka) of 25700 l/mol and effective Forster resonance energy transfer (FRET) of 4.87 nm. The bonding process is enthalpically driven and the reaction not spontaneous. The flavonoid bonding slightly perturbed the secondary and tertiary structures of ALDH that is tryptophangated. The interaction is regulated by both diffusion and ionic strength. Kolaflavanone has a marked effect on the ellipticity of ALDH structure. Molecular docking shows that the binding of kolaflavanone is at the active site of ALDH and the participation of some amino acid residues in the complex formation. Protein-ligand interaction analysis, kinetics, detailed overview. The profiles of atomic fluctuations indicates the rigidity of the ligand-binding site during the simulation. With these, ALDH is hereby proposed as a subtle nanoparticle determinant of kolaviron bioavailability and efficacy. Temperature dependency of ligand-protein binding, Stern-Volmer dynamic quenching constants, and thermodynamic parameters. Binding is reduced by Na+
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methyl ampal thiolester
78% inhibition of isozyme ALDH3 at 0.0075 mM
Mg2+
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89% residual activity at 1 mM
Mn2+
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89% residual activity at 1 mM
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
5.74% inhibition at 0.01 mM, pH 7.5, 25°C
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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
6.05% inhibition at 0.01 mM, pH 7.5, 25°C
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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
5.26% inhibition at 0.01 mM, pH 7.5, 25°C
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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
9.09% inhibition at 0.01 mM, pH 7.5, 25°C
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N-Acetylimidazole
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75% residual activity at 2.5 mM
N-benzyl-3-(2,3,5-trimethyl-7-oxo-7H-furo[3,2-g][1]benzopyran-6-yl)propanamide
31.7% inhibition at 0.01 mM
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N-bromosuccinimide
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66% residual activity at 0.5 mM
p-chloromercuribenzoate
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50 microM, 80% inhibition
p-mercuribenzoate
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80% inhibition at 0.05 mM
Pb2+
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100% inhibition at 1 mM; 1 mM, 100% inhibition
PEG-400
10% (v/v), 16% inhibition
pentanal
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extremely strong substrate inhibition
phenylmethylsulfonyl fluoride
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73% residual activity at 2.5 mM
PMSF
50 mM, no loss of activity
pyrazole
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100% inhibition at 1 mM; 1 mM, 100% inhibition
trans-4-(N,N-dimethylamino)-cinnamaldehyde
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1 mM, 58% inhibition; 58% inhibition at 1 mM
Urea
500 mM, 44% inhibition
Woodward's reagent K
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71% residual activity at 50 mM
ZnCl2
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50% inhibition at 0.035 mM, enzyme form ALDH1
[(4-methyl-2-oxo-2H-1-benzopyran-7-yl)oxy]acetonitrile
79.6% inhibition at 0.01 mM
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Chloral hydrate
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Chloral hydrate
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50% inhibition of isoenzyme F1 by 0.25 mM, 50% inhibition of isoenzyme F2 by 0.4 mM
Cu2+
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20% residual activity at 1 mM
Cu2+
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100% inhibition at 1 mM; 1 mM, 100% inhibition
Disulfiram
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Disulfiram
0.01 mM; 0.01 mM; 0.01 mM
Disulfiram
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0.025 mM, 99% inhibition of activity with NADP+, 80% inhibition of activity with activity with NAD+
Disulfiram
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0.025 mM or 0.05 mM, 99% inhibition of activity with NADP+, 60% inhibition of activity with NAD+
Hg2+
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complete inhibition at 0.25 mM
Hg2+
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100% inhibition at 1 mM; 1 mM, 100% inhibition
NADH
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NADH
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competitive with respect to NAD+ and non-competitive with respect to either benzaldehyde or glycolaldehyde
nitroglycerin
induces nitrate tolerance. Expression and activity of ALDH-2 is decreased in nitrate-tolerant rats
nitroglycerin
more than half of the original activity is retained in the presence of 5.5 mM nitroglycerin and approximate 80% of the activity is lost by the addition of 11 mM nitroglycerin. Dithiothreitol and alpha-lipoic acid can also restore the nitroglycerin inactivated dehydrogenation to more than half of the original activity
p-hydroxymercuribenzoate
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p-hydroxymercuribenzoate
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0.05 mM
p-hydroxymercuribenzoate
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additional information
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not inhibited by EDTA
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additional information
design, synthesis of 1,3-dimethylpyrimidine-2,4-diones as potent and selective aldehyde dehydrogenase 1A1 (ALDH1A1, EC 1.2.1.36) inhibitors and comparison of inhibitory activities on different ALDH isozymes, overview. Poor inhibition by 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-(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-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-(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-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-methoxybenzyl)-N-(1,3-dimethyl-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)-3-(4-(4-isopropylbenzoyl)piperazin-1-yl)propanamide, and CM026
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additional information
inhibition of the aldehyde dehydrogenase 1/2 family by psoralen and coumarin derivatives, structure-function relationships, overview. 3,5-dimethyl-6-propyl-7H-furo[3,2-g][1]benzopyran-7-one, 2,3,5,6-tetramethyl-7H-furo[3,2-g][1]benzopyran-7-one, methyl 2-[(4-methyl-2-oxo-2H-1-benzopyran-7-yl)oxy]propanoate, 2,3,5,6,9-pentamethyl-7H-furo[3,2-g][1]benzopyran-7-one, 3,4-dimethyl-6,7,8,9-tetrahydro-2H-[1]benzofuro[3,2-g][1]benzopyran-2-one, 2,3,5-trimethyl-6-[3-oxo-3-(piperidin-1-yl)propyl]-7H-furo[3,2-g][1]benzopyran-7-one, 5-methyl-2-[(3-oxobutan-2-yl)oxy]-7H-furo[3,2-g][1]benzopyran-7-one, 7-(2-oxopropoxy)-2H-1-benzopyran-2-one, 3,4,8,9-tetramethyl-7H-furo[2,3-f][1]benzopyran-7-one, 2-[(4-methyl-2-oxo-2H-1-benzopyran-7-yl)oxy]-N-phenylacetamide, 7-(diethylamino)-4-methyl-2H-1-benzopyran-2-one, 3-[(3-oxobutan-2-yl)oxy]-6H-dibenzo[b,d]pyran-6-one, 3-(7-hydroxy-4-methyl-2-oxo-2H-1-benzopyran-3-yl)propanoic acid, and N-(4,7-dimethyl-2-oxo-2H-1-benzopyran-6-yl)-2-methylpropanamide are inactive as inhibitors
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