1.3.1.34: 2,4-dienoyl-CoA reductase [(2E)-enoyl-CoA-producing]

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For detailed information about 2,4-dienoyl-CoA reductase [(2E)-enoyl-CoA-producing], go to the full flat file.

Reaction

Synonyms

2,4-dienoyl coenzyme A reductase, 2,4-dienoyl-CoA reductase, 2,4-dienoyl-CoA reductase (NADPH), 2,4-dienoyl-CoA reductase [NADPH], 4-enoyl-CoA reductase (NADPH), 4-enoyl-CoA reductase [NADPH], DCR, DECR, FADH, pDCR, peroxisomal 2,4-dienoyl CoA reductase

ECTree

     1 Oxidoreductases

         1.3 Acting on the CH-CH group of donors

             1.3.1 With NAD⁺ or NADP⁺ as acceptor

                1.3.1.34 2,4-dienoyl-CoA reductase [(2E)-enoyl-CoA-producing]

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Results	in table
5089	AA Sequence
1	CAS Registry Number
8	Cloned(Commentary)
12	Cofactor
2	Crystallization (Commentary)
12	Disease/ Diagnostics
1	Expression
3	General Information
4	Inhibitors
17	KM Value [mM]
6	Localization
3	Metals/Ions
5	Molecular Weight [Da]
3	Natural Substrates/ Products (Substrates)
191	Organism
2	Pathway
21	PDB ID
3	pH Optimum
3	pH Stability
14	Protein Variants
9	Purification (Commentary)
3	Reaction
3	Reaction Type
16	Reference
5	Source Tissue
11	Specific Activity [micromol/min/mg]
4	Storage Stability
26	Substrates and Products (Substrate)
3	Subunits
25	Synonyms
1	Systematic Name
2	Temperature Optimum [°C]
1	Temperature Stability [°C]
7	Turnover Number [1/s]

Crystallization

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Crystallization on EC 1.3.1.34 - 2,4-dienoyl-CoA reductase [(2E)-enoyl-CoA-producing]

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

15 mg/ml purified recombinant enzyme, hanging drop vapour diffusion method, reservoir solution: 30% PEG 5000 monomethyl ether, 0.2 M sodium acetate, 0.1 M ammonium sulfate, 0.1 M 3-(N-morpholino)ethane sulfonic acid, pH 6.5, precipitant solution: 18% PEG 5000 monomethyl ether, 180 mM sodium acetate, 90 mM ammonium sulfate, 90 mM 3-(N-morpholino)ethane sulfonic acid, mixture in a ratio 1:1.5, 1 week, no cryoprotection, X-ray diffraction structure determination and analysis at 2.2 A resolution, heavy atom derivatives

Escherichia coli

-

656161

the crystal structure of a ternary complex of peroxisomal 2,4-dienoyl CoA reductases (pDCR) with hexadienoyl CoA and NADP is described. The structure of pDCR refined to 1.84 A resolution reveals the absence of the tyrosine-serine pair seen in the active site of mitochondrial DCR. Instead, aspartate hydrogen-bonded to the Calpha hydroxyl via a water molecule perturbs the water molecule for protonation of the substrate

Homo sapiens

Q9NUI1

725482