1.1.1.30: 3-hydroxybutyrate dehydrogenase

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

Reaction

(R)-3-hydroxybutanoate
+
NAD+
=
acetoacetate
+
NADH
+
H+

Synonyms

3-D-hydroxybutyrate dehydrogenase, 3-HBDH, 3-hydroxybutyrate dehydrogenase, 3-hydroxybutyrate dehydrogenase 2, 3-hydroxybutyrate dehydrogenase-2, 3HBDH, acetoacetyl-CoA reductase, BDH, BDH1, BDH2, BDH3, BdhA, beta-hydroxybutyrate dehydrogenase, beta-hydroxybutyric acid dehydrogenase, beta-hydroxybutyric dehydrogenase, D(-)-3-hydroxybutyrate dehydrogenase, D-(-)-3-hydroxybutyrate dehydrogenase, D-3-hydroxybutyrate dehydrogenase, D-beta-hydroxybutyrate dehydrogenase, DHRS6, HBD, HBDH, hydroxybutyrate oxidoreductase, More, NAD-beta-hydroxybutyrate dehydrogenase

ECTree

     1 Oxidoreductases
         1.1 Acting on the CH-OH group of donors
             1.1.1 With NAD+ or NADP+ as acceptor
                1.1.1.30 3-hydroxybutyrate dehydrogenase

Crystallization

Crystallization on EC 1.1.1.30 - 3-hydroxybutyrate dehydrogenase

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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystallization of the enzyme in the apo form and in the holo form with acetate as a substrate analogue, method screening, mother liquor consists of 30% w/v PEG 4000, 0.2 M sodium acetate trihydrate and 100 mM Tris-HCl, pH 8.5, at 20°C, X-ray diffraction structure determination and analysis at 2.2 A resolution, molecular-replacement method
-
in complex with NAD+, malonate, or methylmalonate, hanging drop vapor diffusion method, using 30-34% (w/v) PEG 4000
-
in the presence of the substrate D-3-hydroxybutyrate and the cofactor NAD+ at the optimum pH for the catalytic reaction. At 277 and 293 K using the hanging-drop vapour-diffusion method, to 2.3 A resolution. Structure is isomorphous to that of the complex with the substrate analogue acetate
-
sitting drop vapor diffusion method at 20°C, structure determined at a resolution of 1.8 A in complex with NAD(H)
-
crystals of ternary complex of HBDH-NAD+-L-3-hydroxybutyrate and the binary complex of HBDH-NAD+. The former structure shows a closed-form conformation, which is considered an active form for catalysis, while the latter stays mostly in a open-form conformation. Crystals of mutants T190S and T190A
-
hanging-drop vapor-diffusion method, ligand-free enzyme and enzyme-NAD+ complex, 2.0 A resolution
-
hanging-drop vapour-diffusion method using PEG 3000 as a precipitating agent. The crystals belong to the orthorhombic group P2(1)2(1)2, with unit-cell parameters a = 64.3, b = 99.0, c = 110.2 A. The crystals are most likely to contain two tetrameric subunits in the asymmetric unit
hanging drop vapour diffusion method with 17-20% polyethylene glycol 1500, 0.1 M Tris-HCl, pH 7.1, 0.2 mM CaCl2 and 10 mM acetoacetate; recombinant enzyme, hanging drop vapor diffusion method, 0.003 ml of HBDH, 10 mg/ml, is mixed with an equal volume of crystallization buffer containing 17-20% PEG 1500, 0.1 M Tris-HCl, pH 7.1, 0.2 mM CaCl2, and 10 mM acetoacetate, room temperature/22°C, three different crystal forms, X-ray diffraction structure determination and analysis at resolutions between 1.9 and 2.1 A
-