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1.2.1.5: aldehyde dehydrogenase [NAD(P)+]

This is an abbreviated version!
For detailed information about aldehyde dehydrogenase [NAD(P)+], go to the full flat file.

Word Map on EC 1.2.1.5

Reaction

an aldehyde
+
NAD(P)+
 +
H2O
=
a carboxylate
 +
NAD(P)H
 +
H+

Synonyms

acetaldehyde dehydrogenase, ALD4, aldehyde dehydrogenase, aldehyde dehydrogenase 1A3, aldehyde dehydrogenase 2, aldehyde dehydrogenase 3A1, aldehyde: NAD(P)+ oxidoreductase, ALDH, ALDH1, ALDH13, ALDH17, ALDH1a, ALDH1A1, Aldh1a3, ALDH1b, ALDH2, ALDH2a, ALDH2b, ALDH3, ALDH3A1, Aldh3b1, ALDH3F1, ALDH3H1, ALDH3I1, ALDH7B7, ALDH9, ALDHC, ALDHIII, BcALDH, BCP54, chromosomally encoded box pathway ALDH, class 3 aldehyde dehydrogenase, Corneal 15.8 kDa protein, Corneal protein 54, dehydrogenase, aldehyde (nicotinamide adenine dinucleotide (phosphate)), HTC-ALDH, K-ACDH, MI dehydrogenase, More, myo-inositol dehydrogenase, NAD(P)(+)-dependent aldehyde dehydrogenase, NAD(P)+-dependent aldehyde dehydrogenase, NAD+-dependent Ald4, nicotinprotein aldehyde dehydrogenase, OsALDH2-1, OsALDH2-2, OsALDH2-3, OsALDH2-4, OsALDH2-5, OsALDH22, OsALDH3-1, OsALDH3-2, OsALDH3-3, OsALDH3-4, OsALDH3-5, OsALDH5, OsALDH7, PEG-ALDH, PuuC, ST0064, succinic semialdehyde dehydrogenase, Transparentin, Tumor-associated aldehyde dehydrogenase, ybcD

ECTree

     1 Oxidoreductases
         1.2 Acting on the aldehyde or oxo group of donors
             1.2.1 With NAD+ or NADP+ as acceptor
                1.2.1.5 aldehyde dehydrogenase [NAD(P)+]

Inhibitors

Inhibitors on EC 1.2.1.5 - aldehyde dehydrogenase [NAD(P)+]

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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,2-Cyclohexanedione
-
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
-
2,3-dimethyl-5-propyl-7H-furo[3,2-g][1]benzopyran-7-one
19.6% inhibition at 0.01 mM
-
2,4-Dinitro-1-fluorobenzene
-
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
-
2-[(4-methyl-2-oxo-2H-1-benzopyran-7-yl)oxy]propanoic acid
6.1% inhibition at 0.01 mM
-
2H-furo[2,3-h][1]benzopyran-2-one
71.7% inhibition at 0.01 mM
-
3,4,10-trimethyl-2H,6H-benzo[1,2-b:5,4-b']dipyran-2,6-dione
20.8% inhibition at 0.01 mM
-
3-benzyl-4-methyl-2-oxo-2H-1-benzopyran-7-yl methanesulfonate
13.1% inhibition at 0.01 mM
-
3-tert-butyl-5,6-dimethyl-7H-furo[3,2-g][1]benzopyran-7-one
13.0% inhibition at 0.01 mM
-
3-thionicotinamide adenine dinucleotide
-
strong inhibition versus beta-NAD+, isoenzyme E2; substrate inhibition, isoenzyme E1
4-hydroxy-2-nonenal
-
-
4-methyl-7-(2-oxo-2-phenylethoxy)-2H-1-benzopyran-2-one
32.9% inhibition at 0.01 mM
-
4-methyl-7-(2-oxopropoxy)-2H-1-benzopyran-2-one
35.9% inhibition at 0.01 mM
-
4-methyl-7-[(3-methylbut-2-en-1-yl)oxy]-2H-1-benzopyran-2-one
76.4% inhibition at 0.01 mM
-
4-methyl-7-[(prop-2-en-1-yl)oxy]-2H-1-benzopyran-2-one
90.5% inhibition at 0.01 mM
-
5-benzyl-2,3-dimethyl-7H-furo[3,2-g][1]benzopyran-7-one
18.4% inhibition at 0.01 mM
-
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
-
6-bromo-3-[(1E)-N-hydroxyethanimidoyl]-2H-1-benzopyran-2-one
8.3% inhibition at 0.01 mM
-
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
-
7-methoxy-4-methyl-2H-1-benzopyran-2-one
63.6% inhibition at 0.01 mM
-
8,9-dimethyl-2,3-dihydrocyclopenta[c]furo[3,2-g][1]benzopyran-4(1H)-one
12.9% inhibition at 0.01 mM
-
9,10-dimethyl-1,2,3,4-tetrahydro-5H-6,8-dioxacyclopenta[b]phenanthren-5-one
5.9% inhibition at 0.01 mM
-
9,10-dimethyl-5H-6,8-dioxacyclopenta[b]phenanthren-5-one
6.6% inhibition at 0.01 mM
-
acetaldehyde
-
strong substrate inhibition
acetone
10% (v/v), 21% inhibition
benomyl
potent irreversible inhibitor of ALDH. Benomyl increases superoxide production as much as nitroglycerin
benzoate
-
non-competitive with respect to either NAD+ or benzaldehyde
beta-NADP+
-
substrate inhibition, isoenzyme E1
Cd2+
-
100% inhibition at 1 mM; 1 mM, 100% inhibition
Chloral hydrate
Co2+
-
89% residual activity at 1 mM
diethyl dicarbonate
-
2% residual activity at 2.5 mM
dimethyl ampal thiolester
complete inhibition of isozyme ALDH3 at 0.0075 mM
Disulfiram
DMSO
10% (v/v), 32% inhibition
EDTA
50 mM, 22% inhibition
ethanediol
10% (v/v), 60% inhibition
ethyl acetimidate
-
71% residual activity at 250 mM
Fe2+
-
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
-
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+
-
methyl ampal thiolester
78% inhibition of isozyme ALDH3 at 0.0075 mM
Mg2+
-
89% residual activity at 1 mM
Mn2+
-
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
-
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
-
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
-
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
-
N-Acetylimidazole
-
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
-
N-bromosuccinimide
-
66% residual activity at 0.5 mM
nitroglycerin
p-chloromercuribenzoate
-
50 microM, 80% inhibition
p-hydroxymercuribenzoate
p-mercuribenzoate
-
80% inhibition at 0.05 mM
Pb2+
-
100% inhibition at 1 mM; 1 mM, 100% inhibition
PEG-400
10% (v/v), 16% inhibition
pentanal
-
extremely strong substrate inhibition
phenylmethylsulfonyl fluoride
-
73% residual activity at 2.5 mM
PMSF
50 mM, no loss of activity
pyrazole
-
100% inhibition at 1 mM; 1 mM, 100% inhibition
trans-4-(N,N-dimethylamino)-cinnamaldehyde
-
1 mM, 58% inhibition; 58% inhibition at 1 mM
Urea
500 mM, 44% inhibition
Woodward's reagent K
-
71% residual activity at 50 mM
ZnCl2
-
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
-
additional information
-