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.
Word Map on EC 1.1.1.30
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1.1.1.30
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ketone
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succinate
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acetoacetate
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lipid-requiring
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lecithin
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coa-transferase
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acetoacetyl-coa
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alpha-glycerophosphate
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thiolase
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3-oxoacid
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submitochondrial
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ketogenesis
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enzyme-phospholipid
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analysis
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diagnostics
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synthesis
- 1.1.1.30
- ketone
- succinate
- acetoacetate
-
lipid-requiring
- lecithin
-
coa-transferase
- acetoacetyl-coa
- alpha-glycerophosphate
-
thiolase
-
3-oxoacid
-
submitochondrial
-
ketogenesis
-
enzyme-phospholipid
- analysis
- diagnostics
- synthesis
Reaction
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, Psyc_1428
ECTree
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Crystallization
Crystallization on EC 1.1.1.30 - 3-hydroxybutyrate dehydrogenase
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structures of enzyme complexed to NAD+:acetoacetate and NAD+:3-oxovalerate
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)
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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
structures of enzyme complexed to NAD+:acetoacetate and NAD+:3-oxovalerate