1.1.1.21: aldehyde reductase

This is an abbreviated version, for detailed information about aldehyde reductase, go to the full flat file.

Reaction

alditol
+
NAD(P)+
=
aldose
+
NAD(P)H
+
H+

Synonyms

17betaHSD5, 20-alpha-HSD, 20-alpha-hydroxysteroid dehydrogenase, AdhA, AKR1B, AKR1B1, AKR1B10, AKR1B13, AKR1B14, AKR1B3, AKR1C3, AKR4C7, aldehyde reductase, alditol/NADP+ oxidoreductase, alditol: NADP+ 1-oxidoreductase, alditol:NAD(P)+1oxidoreductase, alditol:NADP 1-oxidoreductase, alditol:NADP oxidoreductase, aldo-keto reductase, aldo-keto reductase family 1 member B7, aldoketo reductase 1C3, aldose reductase, aldose reductase 2, aldose reductase-like, aldose reductase-like protein, aldose xylose reductase, ALDRXV4, ALR, ALR1, ALR2, AR, ARI, BAR, Fibroblast growth factor regulated protein, FR-1 protein, GRE3, HAR, HRAR, isobutyraldehyde reductase, More, MVDP, NADPH-aldopentose reductase, NADPH-aldose reductase, polyol dehydrogenase (NADP2), RLAR, small intestine reductase, TPN-polyol dehydrogenase, VAS deferens androgen-dependent protein, YqhD

ECTree

     1 Oxidoreductases
         1.1 Acting on the CH-OH group of donors
             1.1.1 With NAD+ or NADP+ as acceptor
                1.1.1.21 aldehyde reductase

Crystallization

Crystallization on EC 1.1.1.21 - aldehyde reductase

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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
in complex with citrate and inhibitor fidarestat, resolution of 0.82 A. After the catalytic event, a rearrangement of a bound ligand can trigger the opening of the safety-belt loop of G213-S226, initiating the release of the oxidized cofactor
-
in complex with inhibitor IDD552, crystallized at pH 5 and 8
-
in complex with inhibitor zenarestat
-
in complex with inhibitors tolrestat, 2-(carboxymethyl)-1-oxo-1,2-dihydronaphtho[1,2-d]isothiazole-4-carboxylic acid 3,3-dioxide and 2-[2-(carboxymethoxy)-2-oxoethyl]-1-oxo-1,2-dihydronaphtho[1,2-d]isothiazole-4-carboxylic acid 3,3-dioxide. Unlike tolrestat, the naphthol[1,2-d]isothiazole inhibitors leave the specificity pocket in the closed state and ligand 2-(carboxymethyl)-1-oxo-1,2-dihydronaphtho[1,2-d]isothiazole-4-carboxylic acid 3,3-dioxide extends the catalytic pocket by opening a novel subpocket. Inhibitor 2-[2-(carboxymethoxy)-2-oxoethyl]-1-oxo-1,2-dihydronaphtho[1,2-d]isothiazole-4-carboxylic acid 3,3-dioxide provokes less pronounced induced-fit adaptations of the binding cavity
-
in complex with NADP+ and inhibitor 4-[3-(3-nitrophenyl)-1,2,4-oxadiazol-5-yl]butanoic acid, 1.43 A resolution. The inhibitor occupies the active site with its carboxylate head group located at the catalytic cavity. In complex with inhibitor {[5-(5-nitrofuran-2-yl)-1,3,4-oxadiazol-2-yl]sulfanyl}acetic acid at 1.55 A resolution. The nitro-aromatic moiety of both inhibitors occupies the specificity pocket of the enzyme, binding to the bottom of the pocket and provoking remarkable induced-fit adaptations
-
in complex with statil
-
in complex with the inhibitor IDD 594, hanging drop vapour diffusion method, using 40% (w/v) PEG 6000 in 50 mM diammonium hydrogen citrate at pH 5
-
molecular modeling of complex with NADP+ and inhibitor (2Z)-3-(3,4-dihydroxyphenyl)-2-[(4-methylphenyl)carbonyl]prop-2-enoic acid
-
purified recombinant ALR2, with the oxidized form of beta-NADPH, pH 5.0, 4C, X-ray diffraction structure determination and analysis at 1.8 A resolution
-
purified recombinant enzyme ALR2 in complex with inhibitor 17744184, hanging drop vapour diffusion method, mixing of 15 mg/mL ALR2 protein solution with reservoir solution containing 5% w/v PEG 6000, 5.15 mg/mL DTT, 0.66 mg/mL NADP+, and 50 mM diammonium hydrogen citrate, pH 5.0, equilibration against 1 mL of well solution containing 20% w/v PEG 6000 in 120 mM diammonium hydrogen citrate, pH 5.0, 3 days at 4C and 2-4 days at 18C, X-ray diffraction structure determination and analysis at 1.26 A resolution
-
purified recombinant enzyme in complex with 6-[(5-chloro-3-methyl-1-benzofuran-2-yl)sulfonyl]pyridazin-3(2H)-one, 20 mg/ml protein in 50 mM diammonium hydrogen citrate, pH 5.0, mixed with NADP+-containing solution in a ratio 1:3, hanging drop vapour diffusion method, soaking in 6-[(5-chloro-3-methyl-1-benzofuran-2-yl)sulfonyl]pyridazin-3(2H)-one solution, containing 5% v/v isopropanol, 5% v/v DMSO, 5% w/v beta-cyclodextrin, 25% w/v PEG 6000, 50 mM diammonium hydrogen citrate pH 5.0, and saturated pyridazinone-type inhibitor, 20C, 3 days, X-ray diffraction structure determination and analysis at 0.95-1.43 A resolution, modeling
-
purified recombinant His-tagged ALR2 in complex with inhibitors sulindac, sulindac sulfide, sulindac sulfone, and tolmetin, hanging drop vapor diffusion method, 25 mg/ml enzyme with two equivalents of NADP+ and 7.5% PEG 6000 were equilibrated against a well containing 1 ml of 120 mM ammonium citrate, pH 5.0, 20% m/v PEG 6000, soaking of crystals in inhibitor saturated solution containing 25% m/v PEG 6000, 50 mM ammonium citrate, pH 5.0, and 5% v/v DMSO, X-ray diffraction structure determination and analysis
-
purified recombinant R268A mutant enzyme, hanging drop vapour diffusion method, 30 mg/ml protein in 5 mM phosphate, pH 7.0, mixing with equal volume of well solution containing 20% v/v PEG 6000, 25 mM MES, pH 6.0, and 16 mM ammonium sulfate, 3 weeks, X-ray diffraction structure determination and analysis at 2.8 A resolution
-
purified recombinant wild-type enzyme and mutant AKR1B10 V301L holoenzyme in complex with inhibitor fidarestat and NADP+, X-ray diffraction structure determination and analysis 1.60 A resolution by replacement soaking of crystals containing inhibitor tolrestat for 14 days in 25 mM fidarestat dissolved in the reservoir solution. For crystallization of the enzyme with tolrestat by hanging-drop vapour diffusion method, 0.001 ml of 18 mg/ml protein solution containing 2 mM tolrestat is mixed with 0.001 ml of reservoir solution containing 100 mM sodium cacodylate, pH 9.0, and 30% v/v PEG, 6000, at 24C
-
purified recombinant wild-type enzyme complexed with inhibitors phenylacetic acid, 2-hydroxyphenylacetic acid, 2,6-dichlorophenylacetic acid, hexanoic acid, and lipoic acid, hanging drop vapor diffusion method, 4C, 23-25 mg/ml protein in 0.10 M sodium phosphate buffer, pH 7.0, mixed with well solution containing 20% w/v PEG 6000 and 50 mM sodium citrate, pH 5.0, microseeding, 1 month, crystal stabilization by 0.1 to 1.0% glutaraldehyde, X-ray diffraction structure determination and analysis at 1.7-2.0 A resolution
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single-crystal x-ray data, neutron Laue data analysis and quantum mechanical modeling of aldose reductase. Quantum model of catalysis
-
structural model
-
in complex with NADPH, to 2.4 A resolution. Space group P412121 or P43212
-
hanging drop vapour diffusion method, using 0.1 M HEPES pH 7.5, 20% (w/v) polyethylene glycol 4000 and 10% (v/v) 2-propanol
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purified recombinant enzyme in ternary/binary complex with inhibitor nitazoxanide and/or NADP+, or with NADP+ and glyceraldehyde, for enzyme-NADP+-nitazoxanide complex, enzyme-NADP+ crystals are soaked in a saturated solution of nitazoxanide containing 50% N,N-dimethylformamide, 50 mM ammonium citrate, pH 5.0, and 12.5% PEG 6000, for enzyme-NADP+-D-glyceraldehyde complex, enzyme-NADP+ crystals are soaked in a solution containing 20% pyridine, 0.3 M D,L-glyceraldehyde, 50 mM ammonium citrate, pH 5.0, and 12.5% m/v PEG 6000, X-ray diffraction structure determination and analysis, modeling
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purified enzyme in complex with inhibitor fidaresta, X-ray diffraction structure determination and analysis at 1.85 A resolution
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space group P212121, resolution to 2.0 A
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