1.1.1.36: acetoacetyl-CoA reductase

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For detailed information about acetoacetyl-CoA reductase, go to the full flat file.

Reaction

Synonyms

(3R)-hydroxyacyl-CoA dehydrogenase, (R)-3-hydroxyacyl-CoA dehydrogenase, AAR, AcAc-CoA reductase, 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, ketoacyl reductase, MFE-2, More, MSMEG_6753, NADH-preferring acetoacetyl-CoA reductase, NADP-linked acetoacetyl CoA reductase, NADPH-dependent acetoacetyl coenzyme A reductase, NADPH-dependent acetoacetyl-CoA reductase, NADPH-dependent acetoacetyl-coenzyme A 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

ECTree

     1 Oxidoreductases

         1.1 Acting on the CH-OH group of donors

             1.1.1 With NAD⁺ or NADP⁺ as acceptor

                1.1.1.36 acetoacetyl-CoA reductase

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Results	in table
8	Activating Compound
4735	AA Sequence
5	Application
1	CAS Registry Number
24	Cloned(Commentary)
85	Cofactor
6	Crystallization (Commentary)
14	Disease/ Diagnostics
12	General Information
2	General Stability
78	Inhibitors
1	kcat/KM [mM/s]
55	KM Value [mM]
17	Localization
22	Molecular Weight [Da]
53	Natural Substrates/ Products (Substrates)
1	Organic Solvent Stability
87	Organism
15	Pathway
46	PDB ID
13	pH Optimum
2	pH Range
2	pH Stability
39	Protein Variants
25	Purification (Commentary)
2	Reaction
5	Reaction Type
81	Reference
35	Source Tissue
43	Specific Activity [micromol/min/mg]
4	Storage Stability
127	Substrates and Products (Substrate)
20	Subunits
92	Synonyms
1	Systematic Name
14	Temperature Optimum [°C]
19	Turnover Number [1/s]

Crystallization

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Crystallization on EC 1.1.1.36 - acetoacetyl-CoA reductase

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

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

Candida tropicalis

-

654460

hanging-drop vapour diffusion

Candida tropicalis

-

669878

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

Cupriavidus necator

P14697

739901

apo and NADP+-bound enzyme forms, sitting drop vapor diffusion method, using 100 mM Na-HEPES (pH 7.5), 30% (v/v) PEG 400 and 200 mM magnesium chloride hexahydrate for the apo enzyme and 200 mM sodium citrate tribasic dehydrate and 20% (w/v) PEG 3350 for the NADP+-bound enzyme

Mycolicibacterium smegmatis

A0R723

760524

selenomethionine-labeled recombinant truncated enzyme, X-ray diffraction structure determination and analysis at 2.38 A resolution

Rattus norvegicus

-

657366

sitting drop vapor diffusion method, using 10% (w/v) PEG 8000, 8% (w/v) ethylene glycol, 100 mM HEPES-NaOH pH 7.5

Rickettsia felis

Q4UN54

760305