1.3.1.34: 2,4-dienoyl-CoA reductase (NADPH)

This is an abbreviated version!
For detailed information about 2,4-dienoyl-CoA reductase (NADPH), go to the full flat file.

Word Map on EC 1.3.1.34

Reaction

trans-2,3-didehydroacyl-CoA
+
NADP+
=
trans,trans-2,3,4,5-tetradehydroacyl-CoA
+
NADPH
+
H+

Synonyms

2,4-dienoyl coenzyme A reductase, 2,4-dienoyl-CoA reductase, 2,4-dienoyl-CoA reductase [NADPH], 4-enoyl-CoA reductase, 4-enoyl-CoA reductase (NADPH), 4-enoyl-CoA reductase [NADPH], DCR, DECR, More, pDCR, peroxisomal 2,4-dienoyl CoA reductase, SDR, short-chain dehydrogenase

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 (NADPH)

Crystallization

Crystallization on EC 1.3.1.34 - 2,4-dienoyl-CoA reductase (NADPH)

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
the crystal structure of the ternary complex 2,4-dienoyl-CoA reductase-trans-2,trans-4-hexadienoyl-CoA-NADP+ reveals that the carbonyl oxygen of the substrate accepts a hydrogen bond from general acid Y199 and also N148
-
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
-
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
-
wild-type and selenomethionine enzyme, 0.001 ml of protein and of reservoir solution, the latter containing 16% PEG 4000 w/v, 0.18 M ammonium sulfate, 80 mM sodium acetate, pH 4.6, 20% glycerol, addition of 30% ethylene glycol and 4 mM NADP+ for the binary complex of enzyme with NADP+, and 120 mM substrate for the ternary complex of enzyme with NADP+ and substrate trans-trans-2,4-dienoyl-CoA, X-ray diffraction structure determination and analysis at 2.1 A and 1.75 A resolution, respectively
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