1.1.1.1: alcohol dehydrogenase

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

Reaction

a primary alcohol
+
NAD+
=
an aldehyde
+
NADH
+
H+

Synonyms

(R)-specific alcohol dehydrogenase, 40 kDa allergen, Aadh1, ADH, ADH 1, ADH class III, ADH I, ADH II, ADH-10, ADH-A, ADH-A2, ADH-B2, ADH-C2, ADH-HT, ADH-I, ADH1, ADH1B, ADH1C, ADH1C*1, ADH1C*2, Adh1p, ADH2, ADH3, ADH4, ADH5, ADH6Hp, ADH8, AdhA, AdhB, AdhC, AdhD, AdhE, ADS1, AFPDH, alcohol dehydrogenase, alcohol dehydrogenase (NAD), alcohol dehydrogenase 1, alcohol dehydrogenase 10, alcohol dehydrogenase 2, alcohol dehydrogenase 3, alcohol dehydrogenase 5, alcohol dehydrogenase I, alcohol dehydrogenase II, Alcohol dehydrogenase-B2, alcohol dependent dehydrogenase, alcohol-aldehyde/ketone oxidoreductase, NAD+-dependent, alcohol:NAD+ oxidoreductase, aldehyde dehydrogenase, aldehyde reductase, aldehyde/alcohol dehydrogenase, ALDH, aliphatic alcohol dehydrogenase, APE2239, APE_2239.1, ARAD1B16786p, bifunctional alcohol/aldehyde dehydrogenase, CHY1186, class I ADH, class I ALDH, class II ADH, class III ADH, class III alcohol dehydrogenase, class IV ADH, Cm-ADH2, Cthe_0423, DADH, dehydrogenase, alcohol, ethanol dehydrogenase, FALDH, FDH, Gastric alcohol dehydrogenase, Glutathione-dependent formaldehyde dehydrogenase, GSH-FDH, HLAD, HpADH3, HtADH, HvADH1, HVO_2428, iron-containing alcohol dehydrogenase, KlADH4, KlDH3, KmADH3, KmADH4, long-chain alkyl alcohol dehydrogenase, LSADH, medium chain alcohol dehydrogenase, medium-chain NAD+-dependent ADH, medium-chain secondary alcohol dehydrogenase, NAD(H)-dependent alcohol dehydrogenase, NAD+-ADH, NAD+-dependent (S)-stereospecific alcohol dehydrogenase, NAD+-dependent alcohol dehydrogenase, NAD-dependent alcohol dehydrogenase, NAD-dependent medium-chain ADH, NAD-specific aromatic alcohol dehydrogenase, NADH-alcohol dehydrogenase, NADH-aldehyde dehydrogenase, NADH-dependent alcohol dehydrogenase, Octanol dehydrogenase, PF0991 protein, PF1960, primary alcohol dehydrogenase, Retinol dehydrogenase, SaADH, SaADH2, Saci_1232, SADH, SCAD, sec-ADH A, short-chain ADH, short-chain NAD(H)-dependent dehydrogenase/reductase, SSADH, SsADH-10, SSO2536, ST0053, Ta1316 ADH, TaDH, TBADH, Teth39_0206, Teth39_0218, Teth514_0627, TK0845, Tsac_0416, Y-ADH, YADH, YADH-1, yeast alcohol dehydrogenase

ECTree

     1 Oxidoreductases
         1.1 Acting on the CH-OH group of donors
             1.1.1 With NAD+ or NADP+ as acceptor
                1.1.1.1 alcohol dehydrogenase

Crystallization

Crystallization on EC 1.1.1.1 - alcohol dehydrogenase

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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
multiple anomalous dispersion techniques, X-ray diffraction structure determination and analysis at 1.62 A resolution
-
the zinc-containing enzyme has been crystallized by the sitting-drop vapour-diffusion method using PEG 600 as precipitant. Single orthorhombic crystals with maximum dimensions of 0.4 * 0.4 * 1 mm grow from 0.1 M PIPES pH 6.75 containing 13% PEG 600 and 0.5 mM NADH in approximately four weeks. The crystals diffract to better than 1.5 A using synchrotron radiation and belong to the orthorhombic space group P2(1)2(1)2, with unit-cell parameters a = 100.7, b = 103.2, c = 67.5 A
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1 A resolution crystal structures of liver alcohol dehydrogenase in complex with NADH and two inhibitors: dimethyl sulfoxide and isobutyramide
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10 mg/ml purified double mutant H51Q/K228R in complex with NAD+ and 2,3- or 2,4-difluorobenzyl alcohol, in 50 mM ammonium N-[tris(hydroxymethyl)-methyl]-2-aminoethanesulfonate, pH 7.0, 5°C, 1 mM NAD+, 10 mM 2,3-difluorobenzyl alcohol or 2,4-difluorobenzyl alcohol, equilibrated against increasing concentrations of 2-methyl-2,4-pentanediole, crystal formation at 12% 2-methyl-2,4-pentanediole, X-ray diffraction structure determination and analysis
-
enzyme in complex with trifluoroethanol and without NAD+, X-ray diffraction structure determination and analysis at 2.35 A resolution
structure of the alcohol dehydrogenase domain of the ADHE protein 2.5 A resolution and docking of the aldehyde dehydrogenase domain. The aldehyde dehydrogenase and alcohol dehydrogenase domains of a single ADHE may form dimers with different ADHE monomers rather than both with the same molecule
isozyme alphaalpha in complex with inhibitor N-cyclopentyl-N-cyclobutylformamide, isozyme beta(1)beta(1) in complex with inhibitors N-benzylformamide and N-heptylformamide, and isozyme gamma(2)gamma(2) in complex with inhibitor N-1-methylheptylformamide, X-ray diffraction structure determination and analysis at 1.45-2.5 A resolution, structure modeling
-
purified recombinant N-terminally His-tagged Adh3, hanging drop vapour diffusion method, mixing of 0.002 ml of 80mg/ml protein in 50 mM Tris, pH 7.0, with 0.002 ml of reservoir solution, comprising 0.1 M MES, pH 6.5, 16% w/w PEG 20000, and 0.001 ml of 50 mM CaCl2, 20°C, X-ray diffraction structure determination and analysis
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enzyme-NADP+-cofactor complex, X-ray diffraction strcuture determination and analysis, computational structure modeling
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ternary complex of enzyme with NADH and ethylene glycol, X-ray diffraction structure determination and analysis at 2.3 A resolution, molecular replacement method
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structural modeling of ethanol-tolerant mutant protein
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isozyme YADH-1, crystal structure analysis
-
three-dimensional model of the enzyme structure suggest that Ca2+ can be displaced by replacing Met-168 by an Arg residue
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trigonal crystal form alcohol dehydrogenase I: evidence for the existence of Zn ions in the crystal, from 20% PEG 4000, 20% 2-propanol, 0.1 M sodium citrate, pH 5.6, and 1 mM NAD+, X-ray diffraction structure determination and analysis at 3.0 A resolution
-
the crystal structure of the binary complex SaADH2–NADH, determined at 1.75 A resolution, reveals details of the active site providing hints on the structural basis of the enzyme enantioselectivity
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apoenzyme and ternary complex of enzyme with NADH and 2-ethoxyethanol bound to each subunit, X-ray diffraction structure determination and analysis at 2.3 A resolution
-
crystals are grown in the Advanced Protein Crystallization Facility during the Life and Microgravity Sciences Spacelab mission on the US Space Shuttle. Large diffracting crystals are obtained by dialysis, whereas only poor-quality crystals are obtained by vapour diffusion. The quality of both the microgravity and ground-based crystals is analysed by X-ray diffraction. There is some improvement in terms of size and diffraction resolution limit for the microgravity crystals. The twinning observed in the Earthgrown crystals is also present for those grown in microgravity
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holo-enzyme form and apo-enzyme form
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microbatch method
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microbatch method in 100 mM Tris-HCl (pH 7.8), 10 mM dithiotreitol with the same volume of 12% (w/v) PEG 4000, 12% (v/v) 2-propanol, 100 mM sodium citrate (pH 5.6) at 20°C
-
twinned crystals are grown with the sitting drop vapour diffusion method using 2-methyl-2,4-pentanediol (50% v/v), Tris/HCl buffer (150 mM, pH 8.4), and NADH (1 mM), prismatic crystals are grown at 4°C and 20°C by microbatch and free interface diffusion methods with Tris/HCl buffer (130 mM, pH 8.0), NADH (2 mM), polyethyleneglycol 4000 (16% w/v), propan-2-ol or propan-1-ol (16% v/v) in trisodium citrate (100 mM, pH 4.8-5.6)
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