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EC Tree
IUBMB Comments This bacterial enzyme catalyses the reduction of either (2E,4E)-2,4-dienoyl-CoA or (2E,4Z)-2,4-dienoyl-CoA to (2E)-2-enoyl-CoA. The enzyme from Escherichia coli contains FAD, FMN, and an [4Fe-4S] iron sulfur cluster. cf. EC 1.3.1.124, 2,4-dienoyl-CoA reductase [(3E)-enoyl-CoA-producing].
Word Map
1.3.1.34
beta-oxidation
unsaturated
polyunsaturated
odd-numbered
even-numbered
3-hydroxyacyl-coa
5.3.3.8
chain-shortened
trans-2
tetradecylthioacetic
reductase-dependent
petroselinic
delta3-delta2-enoyl-coa
omega-oxidation
3,delta
The taxonomic range for the selected organisms is: Homo sapiens The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
2,4-dienoyl-coa reductase, 2,4-dienoyl coenzyme a reductase,
more
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2,4-dienoyl-CoA reductase
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peroxisomal 2,4-dienoyl CoA reductase
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2,4-dienoyl coenzyme A reductase
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2,4-dienoyl-CoA reductase
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2,4-dienoyl-CoA reductase (NADPH)
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-
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2,4-dienoyl-CoA reductase [NADPH]
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-
-
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4-enoyl-CoA reductase (NADPH)
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-
-
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4-enoyl-CoA reductase [NADPH]
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-
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(2E)-2-enoyl-CoA:NADP+ 4-oxidoreductase
This bacterial enzyme catalyses the reduction of either (2E,4E)-2,4-dienoyl-CoA or (2E,4Z)-2,4-dienoyl-CoA to (2E)-2-enoyl-CoA. The enzyme from Escherichia coli contains FAD, FMN, and an [4Fe-4S] iron sulfur cluster. cf. EC 1.3.1.124, 2,4-dienoyl-CoA reductase [(3E)-enoyl-CoA-producing].
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(2E,4E)-2,4-decadienoyl-CoA + NADPH
?
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?
(2E,4E)-2,4-hexadienoyl-CoA + NADPH
?
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-
-
?
2,4,7,10,13,16,19-docosaheptaenoyl-CoA + NADPH
?
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-
-
?
2,4-hexadienoyl-CoA + NADPH
trans-3-hexenoyl-CoA + NADP+
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-
-
?
2,4-trans-decadienoyl-CoA + NADPH
? + NADP+
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-
-
?
2-trans,4-trans-decadienoyl-CoA + NADPH
3-decenoyl-CoA + NADP+
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-
-
?
2,4-trans-decadienoyl-CoA + NADPH
? + NADP+
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-
-
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?
2,4-trans-hexadienoyl-CoA + NADPH
trans-3-hexenoyl-CoA + NADP+
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-
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?
additional information
?
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key enzyme in the beta-oxidation of unsaturated fatty acids
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?
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additional information
?
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key enzyme in the beta-oxidation of unsaturated fatty acids
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?
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2,4-dienoyl-coa reductase [(2e)-enoyl-coa-producing] deficiency
Mitochondrial 2,4-dienoyl-CoA reductase deficiency in mice results in severe hypoglycemia with stress intolerance and unimpaired ketogenesis.
2,4-dienoyl-coa reductase [(2e)-enoyl-coa-producing] deficiency
[2,4-Dienoyl-CoA reductase deficiency]
Autoimmune Diseases
Epithelial cell specificity and apotope recognition by serum autoantibodies in primary biliary cirrhosis.
Hypoglycemia
Mitochondrial 2,4-dienoyl-CoA reductase deficiency in mice results in severe hypoglycemia with stress intolerance and unimpaired ketogenesis.
Infertility
Comparative testis proteome of cattleyak from different developmental stages.
Prostatic Neoplasms
2,4-dienoyl-CoA reductase regulates lipid homeostasis in treatment-resistant prostate cancer.
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0.0127
(2E,4E)-2,4-decadienoyl-CoA
pH 7.4, 20°C
0.0716
(2E,4E)-2,4-hexadienoyl-CoA
pH 7.4, 20°C
0.102
2,4,7,10,13,16,19-docosaheptaenoyl-CoA
in the absence of albumin
0.006
2,4-decadienoyl-CoA
in the present of 0.1% albumin
0.059
2,4-hexadienoyl-CoA
in the presence of 0.1% albumin
0.0062
2,4-trans-decadienoyl-CoA
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recombinant His-tagged truncated enzyme, pH 6.0, 22°C
0.0265
2,4-trans-hexadienoyl-CoA
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recombinant His-tagged truncated enzyme, pH 6.0, 22°C
0.0605
NADPH
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recombinant His-tagged truncated enzyme, pH 6.0, 22°C
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7.21
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purified recombinant truncated His-tagged enzyme, substrate 2,4-trans-hexadienoyl-CoA
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22
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assay at room temperature
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Uniprot
brenda
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brenda
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brenda
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brenda
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DECR2_HUMAN
292
0
30778
Swiss-Prot
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30780
encoded by the gene pDCR, calculated from sequence of cDNA
34000
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x * 34000, recombinant truncated His-tagged enzyme, SDS-PAGE
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?
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x * 34000, recombinant truncated His-tagged enzyme, SDS-PAGE
additional information
analytical ultracentrifugation analysis of purified pDCR reveals that the protein exists as a mixture of monomers, dimers, and tetramers in solution
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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
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D137A
relative activity: 3.32% (substrate: 2,4-decadienoyl CoA), 1.27% (substrate: 2,4-hexadienoyl CoA) (wild-type: 100%)
D155A
relative activity: 36.3% (substrate: 2,4-decadienoyl CoA), 59.6% (substrate: 2,4-hexadienoyl CoA) (wild-type: 100%)
D186A
relative activity: 6.21% (substrate: 2,4-decadienoyl CoA), 1.86% (substrate: 2,4-hexadienoyl CoA) (wild-type: 100%)
D268A
relative activity: 2.75% (substrate: 2,4-decadienoyl CoA), 1.14% (substrate: 2,4-hexadienoyl CoA) (wild-type: 100%)
D86A
relative activity: 1.70% (substrate: 2,4-decadienoyl CoA), 1.76% (substrate: 2,4-hexadienoyl CoA) (wild-type: 100%)
E215A
relative activity: 28.9% (substrate: 2,4-decadienoyl CoA), 7.59% (substrate: 2,4-hexadienoyl CoA) (wild-type: 100%)
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22
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purified recombinant truncated enzyme is highly stable at room temperature
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sensitive to freezing, activity loss upon storage on ice
-80°C, purified recombinant truncated enzyme, completely stable for at least 6 months
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22°C, room temperature, purified recombinant truncated enzyme, 70% remaining activity after 1 week
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4°C, purified recombinant truncated enzyme, completely stable for 1 week
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recombinant His-tagged truncated enzyme from Escherichia coli strain BL21(DE3) by one-step nickel affinity chromatography, to over 95% purity
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expressed in Escehrichia coli as a His-tagged fusion protein
functional overexpression of truncated His-tagged enzyme in Escherichia coli strain BL21(DE3)
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De Nys, K.; Meyhi, E.; Mannaerts, G.P.; Fransen, M.; Van Veldhoven, P.P.
Characterisation of human peroxisomal 2,4-dienoyl-CoA reductase
Biochim. Biophys. Acta
1533
66-72
2001
Homo sapiens (Q9NUI1), Homo sapiens
brenda
Chu, X.; Yu, W.; Chen, G.; Li, D.
Expression, purification, and characterization of His-tagged human mitochondrial 2,4-dienoyl-CoA reductase
Protein Expr. Purif.
31
292-297
2003
Homo sapiens
brenda
Hua, T.; Wu, D.; Ding, W.; Wang, J.; Shaw, N.; Liu, Z.J.
Studies of human 2,4-dienoyl CoA reductase shed new light on peroxisomal betta-oxidation of unsaturated fatty acids
J. Biol. Chem.
287
28956-28965
2012
Homo sapiens (Q9NUI1)
brenda