3-hydroxyacyl-CoA dehydrogenase

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




(S)-3-hydroxybutyryl-CoA dehydrogenase, 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-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, endoplasmic reticulum-associated amyloid beta-peptide binding protein, FadB, FadB2, Ferp_1035, Fum13p, 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, 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, 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


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


Crystallization on EC - 3-hydroxyacyl-CoA dehydrogenase

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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