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1.2.1.3: aldehyde dehydrogenase (NAD+)

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

Word Map on EC 1.2.1.3

Reaction

an aldehyde
+
NAD+
 +
H2O
=
a carboxylate
 +
NADH
 +
H+

Synonyms

ADH, AdhE, AHD-M1, ALD1A1, ALD4, ALD6, ALDDH, aldehyde dehydrogenase, aldehyde dehydrogenase (NAD), aldehyde dehydrogenase 1, aldehyde dehydrogenase 16, aldehyde dehydrogenase 1A1, aldehyde dehydrogenase 1A3, aldehyde dehydrogenase 1B1, aldehyde dehydrogenase 2, aldehyde dehydrogenase 3A1, aldehyde dehydrogenase 6, aldehyde dehydrogenase 7A1, aldehyde dehydrogenase class 1, aldehyde dehydrogenase type 2, Aldehyde dehydrogenase [NAD+], Aldehyde dehydrogenase, cytosolic, Aldehyde dehydrogenase, microsomal, aldehyde dehydrogenase-2, aldehyde dehydrogenase7, aldehyde:NAD+ oxidoreductase, ALDH, ALDH 2, ALDH I, ALDH II, ALDH-2, ALDH-E1, ALDH-E2, ALDH1, ALDH1-NL, ALDH16, ALDH1A1, Aldh1a2, Aldh1a3, Aldh1a7, Aldh1b1, ALDH2, ALDH2(1), ALDH2(2), ALDH2(3), ALDH22A1, ALDH2B8, ALDH2C4, ALDH3A1, ALDH3A2, Aldh3b1, ALDH3H1, ALDH3I1, ALDH5A, ALDH7, Aldh7a1, ALDH7B4, Aldh8a1, ALDHI, ALDHTt, ALDHX, ALHDII, Allergen Alt a 10, aryl-aldehyde dehydrogenases, BADH, benzaldehyde dehydrogenase, Brassica turgor-responsive/drought-induced gene 26 protein, Bt-Aldh, Btg-26, class 1 aldehyde dehydrogenase, class 2 aldehyde dehydrogenase, class I ALDH, CoA-independent aldehyde dehydrogenase, coniferyl-aldehyde dehydrogenase, Cphy_1178, EC 1.1.1.70, ETA-crystallin, FeaB-K-12, gamma-aminobutyraldehyde dehydrogenase, hALDH2, HsALDH16A1, irreversible NAD+-dependent aldehyde dehydrogenase, K(+)-ACDH, K(+)-activated acetaldehyde dehydrogenase, KGSADH, LsALDH16, m-methylbenzaldehyde dehydrogenase, Matured fruit 60 kDa protein, MF-60, Mg(2+)-ACDH, Mg(2+)-activated acetaldehyde dehydrogenase, mitochondrial aldehyde dehydrogenase, More, NAD+-dependent aldehyde dehydrogenase, NAD+-dependent ALDH, NAD+-linked aldehyde dehydrogenase, NAD+-pimelic semialdehyde-dependent aldehyde dehydrogenase, NAD+-specific ALDH, NAD-aldehyde dehydrogenase, NAD-dependent 4-hydroxynonenal dehydrogenase, NAD-dependent aldehyde dehydrogenase, NAD-linked aldehyde dehydrogenase, Non-lens ALDH1, p-ALDH2, P51, phenylacetaldehyde dehydrogenase, PhnN, phnY, phosphonoacetaldehyde dehydrogenase, phosphonoacetaldehyde oxidase, PM-ALDH9, PnAA dehydrogenase, propionaldehyde dehydrogenase, PuuC, R-aminobutyraldehyde dehydrogenase, RALDH, RALDH(II), RalDH1, Retinal dehydrogenase, retinal dehydrogenase type I, sALDH, salvery aldehyde dehydrogenase, ThnG, TTC0513, Turgor-responsive protein 26G, yALDH, YneI

ECTree

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

Crystallization

Crystallization on EC 1.2.1.3 - aldehyde dehydrogenase (NAD+)

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, using 0.15 M DL-malic acid pH 7.0, 18%(w/v) PEG 3350
-
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
in complex with NAD+, sitting drop vapor diffusion method, using 0.1 M sodium acetate pH 4.7, 1.8 M ammonium sulfate
purified recombinant wild-type enzyme LsALDH16 and enzyme mutant C295A free or in complex with NAD+ or NADH or 4-nitrophenylacetate, hanging drop vapor diffusion, mixing of 6 mg/ml in 20 mM Tris-HCl, pH 8.0, 100 mM NaCl, 2.5% glycerol, and 0.5 mM tris(2-carboxyethyl)phosphine, with reservoir solution and microseeding solution in a volume ratio of 1:1:0.2, where the reservoir solution comprisess 20% w/v PEG 3350, 200 mM ammonium sulfate, and 100 mM Bis-Tris, pH 5.5, and the microseed solution is made from crushed crystals diluted 1:100 in reservoir, at room temperature, crystals of mutant C295A complexed with 4-nitrophenylacetate are prepared by soaking the apo crystals with the reservoir solution supplemented with 10 mM ligand for about 30 minutes, X-ray diffraction structure determination and analysis at 1.49-2.30 A resolution
-
apoenzyme and in complex with PnA und NAD+, hanging drop vapor diffusion method, using 22%-25% PEG3350, 0.1 M sodium cacodylate (pH 6.5), 0.2 M sodium phosphate dibasic, and 5%-10% glycerol
hanging drop vapor diffusion method, using 22%-25% (w/v) PEG3350, 0.1 M sodium cacodylate (pH 6.5), 0.2 M sodium phosphate dibasic, and 5%-10% (v/v) glycerol
purified recombinant enzyme in apoform and in complex with NAD(P)+ and propanal, sitting drop vapor diffusion method, mixing of 20 mg/ml protein in 50 mM Tris-HCl, pH 7.5, 5 mM 2-mercaptoethanol, and 150 mM NaCl, with or without 1 mM NAD(P)+ and 50 mM propanal, with crystallization solution containing 50 mM MOPS, pH 7.5, and 1.2 M ammonium sulfate, 20°C, X-ray diffraction structure determination and analysis