1.1.1.35: 3-hydroxyacyl-CoA dehydrogenase

This is an abbreviated version, for detailed information about 3-hydroxyacyl-CoA dehydrogenase, go to the full flat file.

Reaction

(S)-3-hydroxyacyl-CoA
+
NAD+
=
3-oxoacyl-CoA
+
NADH
+
H+

Synonyms

(S)-3-hydroxyacyl-CoA dehydrogenase/enoyl-CoA hydratase, (S)-3-hydroxybutyryl-CoA dehydrogenase, (S)-stereospecific 3-hydroxyacyl-CoA dehydrogenase/enoyl-CoA hydratase, 1-specific DPN-linked beta-hydroxybutyric dehydrogenase, 17beta-HSD10, 3-hydroxyacetyl-coenzyme A dehydrogenase, 3-hydroxyacyl coenzyme A dehydrogenase, 3-hydroxyacyl-CoA dehydrogenase, 3-hydroxyacyl-CoA dehydrogenase II, 3-hydroxyacyl-coenzyme A dehydrogenase, 3-hydroxyadipyl-CoA dehydrogenase, 3-hydroxyadipyl-CoA dehydrogenase (NAD+) (probably (S)-3-specific), 3-hydroxybutyryl-CoA dehydrogenase, 3-hydroxyisobutyryl-CoA dehydrogenase, 3-keto reductase, 3-ketoacyl-CoA reductase, 3-L-hydroxyacyl-CoA dehydrogenase, 3-L-hydroxybutyryl-CoA dehydrogenase, 3beta-hydroxyacyl coenzyme A dehydrogenase, beta hydroxyacyl dehydrogenase, beta-hydroxy acid dehydrogenase, beta-hydroxyacyl CoA dehydrogenase, beta-hydroxyacyl-coenzyme A synthetase, beta-hydroxybutyrylcoenzyme A dehydrogenase, beta-keto-reductase, beta-ketoacyl reductase, beta-ketoacyl-CoA reductase, beta-ketoacyl-coenzyme A reductase, betahydroxyacylcoenzyme A dehydrogenase, CbHBD, endoplasmic reticulum-associated amyloid beta-peptide binding protein, F54C8.1, FadB, FadB', FadB2, Ferp_1035, Fum13p, H16_A0461, HAD, HADH, HADH2, HADHSC, HCDH, KCR1, KCR2, L-3-hydroxyacyl CoA dehydrogenase, L-3-hydroxyacyl-CoA dehydrogenase, L-3-hydroxyacyl-CoA dehydrogenase, short chain, L-3-hydroxyacylcoenzyme A dehydrogenase, L-3-hydroxybutyryl CoA dehydrogenase, L-specific 3-hydroxyacyl-CoA dehydrogenase, LIC13300, medium- and short-chain-3-hydroxyacyl-CoA dehydrogenase, medium- and short-chain-3-hydroxyacyl-coenzyme A dehydrogenase, More, Msed_0399, multifunctional beta-oxidation enzyme, PaaH, PaaH1, RePaaH1, SCHAD, SCHAD I, SCHAD II, SCHSD, Scully protein, short chain L-3-hydroxyacyl-CoA dehydrogenase, short-chain 3-hydroxyacyl-CoA dehydrogenase, short-chain 3-hydroxyacyl-coenzyme A dehydrogenase, short-chain hydroxyacyl CoA dehydrogenase, short-chain L-3-hydroxyacyl-CoA dehydrogenase, TFP, type 10 17beta-hydroxysteroid dehydrogenase, type II HADH

ECTree

     1 Oxidoreductases
         1.1 Acting on the CH-OH group of donors
             1.1.1 With NAD+ or NADP+ as acceptor
                1.1.1.35 3-hydroxyacyl-CoA dehydrogenase

Crystallization

Crystallization on EC 1.1.1.35 - 3-hydroxyacyl-CoA dehydrogenase

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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
purified recombinant detagged enzyme, hanging drop vapour diffusion method, 10 mg/ml protein in 25 mM sodium acetate trihydrate, pH 5.0, and 300 mM sodium chloride is mixed with an equal volume of reservoir solution, containing 21% PEG 3350, 0.2 M sodium chloride, 0.1 M MES, pH 6.5, for parallelepiped-shaped crystals and 23% PEG 3350, 0.2 M sodium chloride, 0.1 M bicine, pH 8.0, for cuboid-shaped crystals, equilibration against 0.20 ml reservoir solution, 3-5days at 18°C, X-ray diffraction structure determination and analysis of parallelepiped-shaped cuboid-shaped crystal at 1.60 A and 2.20 A resolution, respectively
-
purified recombinant detagged wild-type enzyme, crystals are grown by hanging drop method from 23% PEG 3350, 0.2 M sodium chloride, 0.1M N,N-bis (2-hydroxyethyl)glycine, pH 8.0, X-ray diffraction structure determination and analysis at 2.20 A resolution, molecular replacement with the human HAD structure as search model, PDB ID 3had
-
hanging drop vapour diffusion method, mixing of 30 mg/ml protein in 40 mM Tris-HCl, pH 8.0, 1 mM DTT, with reservoir solution containing 2 M ammonium sulfate, 0.1 M CAPS, pH 10.5, and 0.2 M lithium sulfate, 22°C, 7 days, X-ray diffraction structure determination and analysis at 2.3 A resolution, molecular replacement method and structure modeling
-
purified recombinant His6-tagged wild-type enzyme in apoform and in complex with substrates acetoacetyl-CoA and NAD+, hanging drop vapour diffusion method, mixing of 30 mg/ml protein in 40 mM Tris-HCl, pH 8.0, 1 mM DTT, with or without 20 mM NAD+, and 20 mM acetoacetyl-CoA, with reservoir solution containing 0.2 M Li2SO4, 0.1 M CAPS, pH 10.5, and 2 M ammonium sulfate, 22°C, 7 days, X-ray diffraction structure determination and analysis at 1.8-2.54 A resolution, molecular replacement and structure modeling
-
purified recombinant enzyme in apoform, as selenomethionine-labeled enzyme, and in complex with substrates acetoacetyl-CoA and NAD+, hanging drop vapour diffusion method, mixing of 50 mg/ml wild-type protein or selenomethionine-labeled enzyme in 40 mM Tris-HCl, pH 8.0, 1 mM DTT, with reservoir solution containing 2 M ammonium sulfate, 0.1 M sodium cacodylate, pH 6.5, and 0.2 M sodium chloride, 22°C, 7 days, X-ray diffraction structure determination and analysis at 2.42-2.7 A resolution, molecular replacement using the crystal structure of the apo-form of RePaaH1, and structure modeling
-
purified recombinant wild-type and selenomethionine-labeled enzymes, hanging drop vapour diffusion method, mixing of 30 mg/ml wild-type protein or 25 mg/ml selenomethionine-labeled enzyme in 40 mM Tris-HCl, pH 8.0, 1 mM DTT, with reservoir solution containing 1.4 M ammonium sulfate, 0.1 M sodium cacodylate, pH 6.0, and 0.2 M sodium chloride, 22°C, 7 days, X-ray diffraction structure determination and analysis at 2.6 A resolution, single-wavelength anomalous dispersion method
-
50 mM N(2-acetamido)-2-iminodiacetic acid, pH 6.5, polyethylene glycol 4000, 5 mM NAD+ hanging drop, crystals within 3 to 5 days at 18°C, enzyme structure is compromised of two domains, a NAD+-binding domain and a helical C-terminal domain
-
50% saturation with ammonium sulfate solution, 0.1 M potassium phosphate, pH 6.8, 1 mM EDTA, 2 mM beta-mercaptoethanol, 4°C, crystals appear after 2 days
-
dialysis against 40% saturated ammonium sulfate containing 100 mM phosphate, 2 mM beta-mercaptoethanol, 1 mM EDTA, pH 6.9, 7.5 or 8.2, vapor diffusion crystallization, crystals are obtained in the ammonium sulfate saturation range of 41% to 48%
-
polyethylene glycol, pH 8, orthorhombic crystals, 2.7 A resolution, crystallisation at pH 5 leads to trigonal space group
-
two dimers of the enzyme in the asymmetric unit of an orthorombic cell, two coenzyme binding sites per dimer
-