Any feedback?
Please rate this page
(all_enzymes.php)
(0/150)

BRENDA support

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.

Word Map on EC 1.1.1.35

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-HADH, 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, 3HA-CoA 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, HBD, 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, NADH-3HB-CoA dehydrogenase, NADH-dependent (S)-3-hydroxyacyl-CoA dehydrogenase, NADH-dependent 3-hydroxyacyl-CoA dehydrogenase, 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

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
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
apoenzyme, hanging drop vapor diffusion method, using 1.25% (w/v) PEG 400, 2.2 M ammonium sulfate, 0.1 M HEPES-NaOH pH 7.5. Enzyme in complex with NAD+, hanging drop vapor diffusion method, using 17.5% (w/v) PEG 3350, 200 mM sodium thiocyanate
-
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
-