acetoacetyl-CoA reductase

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




(3R)-hydroxyacyl-CoA dehydrogenase, (R)-3-hydroxyacyl-CoA dehydrogenase, acetoacetyl CoA reductase, acetoacetyl coenzyme A reductase, acetoacetyl-CoA reductase, AKR1B15, aldo-keto reductase 1B15, beta-ketoacyl reductase, beta-ketoacyl-CoA reductase, beta-ketoacyl-coenzyme A reductase, D(-)-beta-hydroxybutyryl CoA-NADP oxidoreductase, D-3-hydroxyacyl-CoA dehydrogenase, D-3-hydroxyacyl-CoA reductase, D-specific 3-hydroxyacyl-CoA dehydrogenase, hydroxyacyl coenzyme-A dehydrogenase, KCR, MFE-2, More, NADP-linked acetoacetyl CoA reductase, NADPH-dependent acetoacetyl coenzyme A reductase, NADPH-dependent acetoacetyl-CoA reductase, NADPH-linked acetoacetyl-CoA reductase, NADPH:acetoacetyl-CoA reductase, PHA-specific acetoacetyl-CoA reductase, PhaB, PhbB, polyhydroxyalkanoate-specific acetoacetyl coenzyme A reductase, polyhydroxybutyrate enzyme, short chain beta-ketoacetyl(acetoacetyl)-CoA reductase


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


Crystallization on EC - acetoacetyl-CoA reductase

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5 mg/ml purified recombinant, detagged truncated enzyme, amino acid residues 1-604, by vapor diffusion technique, 20°C, in 30% PEG 4000, 0.1 M sodium acetate, pH 4.2, 0.2 M ammonium acetate, equal volume of 0.002 ml of protein and precipitant solution, 11% v/v glycerol as cryoprotectant, X-ray diffraction structure determination and analysis at 2.22-2.36 A resolution, the wild-type enzyme, comprising amino acid residues 1-906, is unstable and not crystallizable
hanging-drop vapour diffusion
purified recombinant His-tagged wild-type and mutant enzymes in complex with NADP+ and acetoacetyl-CoA, wild-type protein crystals grow from 0.1 M MES, pH 7.1, 0.9 mM NADP+, 0.9 mM acetoacetyl-CoA, 1.6 M ammonium sulfate, and 10% 1,4-dioxane, mutant crystals grow from 0.6-1.2 M sodium-potassium tartrate, 0.16-0.20 M lithium sulfate, and 0.1 M CHES, pH 8.9-9.9, X-ray diffraction structure determination and analysis at 1.8 A and 2.0-2.9 A resolution, respectively, molecular replacement method using the structure of FabG from Escherichia coli, PDB ID 1I01, as the search probe
selenomethionine-labeled recombinant truncated enzyme, X-ray diffraction structure determination and analysis at 2.38 A resolution