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Information on EC 1.3.1.34 - 2,4-dienoyl-CoA reductase [(2E)-enoyl-CoA-producing]
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1.3.1.34 2,4-dienoyl-CoA reductase [(2E)-enoyl-CoA-producing]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].
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Word Map
- 1.3.1.34
-
beta-oxidation
- unsaturated
-
polyunsaturated
-
odd-numbered
-
even-numbered
- 3-hydroxyacyl-coa
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5.3.3.8
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chain-shortened
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trans-2
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tetradecylthioacetic
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reductase-dependent
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petroselinic
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delta3-delta2-enoyl-coa
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omega-oxidation
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3,delta
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Reaction Schemes
Synonyms
2,4-dienoyl-coa reductase, 2,4-dienoyl coenzyme a reductase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
2,4-dienoyl coenzyme A reductase
-
-
-
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2,4-dienoyl-CoA reductase
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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DCR
FADH
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
a (2E)-2-enoyl-CoA + NADP+ = a (2E,4Z)-2,4-dienoyl-CoA + NADPH + H+
(2)
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-
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a (2E)-2-enoyl-CoA + NADP+ = a (2E,4E)-2,4-dienoyl-CoA + NADPH + H+
reaction mechanism, active site structure, substrate binding site, His252 is the catalytic residue
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a (2E)-2-enoyl-CoA + NADP+ = a (2E,4E)-2,4-dienoyl-CoA + NADPH + H+
(1)
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-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
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-
-
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redox reaction
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-
-
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reduction
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-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
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SYSTEMATIC NAME
IUBMB Comments
(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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CAS REGISTRY NUMBER
COMMENTARY
82869-38-3
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(2E,4E)-2,4-decadienoyl-CoA + NADPH + H+
(2E)-2-decaenoyl-CoA + NADP+
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-
-
-
?
2,4-cis-tetradecadienoyl-CoA + NADPH
2-cis-dehydroacyl-CoA + NADP+
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low activity
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-
?
2,4-trans-tetradecadienoyl-CoA + NADPH
2-trans-dehydroacyl-CoA + NADP+
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-
-
-
?
2-trans,4-cis-decadienoyl-CoA + NADPH
2-decenoyl-CoA + NADP+
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-
initial reaction product
?
2-trans,4-cis-decadienoyl-CoA + NADPH
3-trans-decenoyl-CoA + NADP+
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-
-
-
?
2-trans,4-trans-decadienoyl-CoA + NADPH
3-trans-decenoyl-CoA + NADP+
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3-trans-decenoyl-CoA is the product of the mutant enzymes Y166F, H252A, and H252A/Y166F
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?
trans-trans-2,4-hexadecadienoyl-CoA + NADPH
trans-2-hexadecenoyl-CoA + NADP+
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step in the beta-oxidation of oleoyl-CoA via 2-trans-5-cis-tetradecadienoyl-CoA in mitochondria via the reductase-dependent pathway, enzyme is not involved in the isomerase-dependent pathway, overview
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-
?
2,4-hexadienoyl-CoA + NADPH
trans-3-hexenoyl-CoA + NADP+
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-
-
?
2-trans,4-trans-decadienoyl-CoA + NADPH
2-trans-decenoyl-CoA + NADP+
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-
-
-
?
2-trans,4-trans-decadienoyl-CoA + NADPH
2-trans-decenoyl-CoA + NADP+
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2-trans-decenoyl-CoA is the normal product of the wild type enzyme in bacteria
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?
additional information
?
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key enzyme in the beta-oxidation of unsaturated fatty acids
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?
additional information
?
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3,5-cis-tetradecadienoyl-CoA is also converted by the reductase pathway of beta-oxidation in mitochondria via 2,4-cis-didehydrotetradecadienoyl-CoA
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-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
trans-trans-2,4-hexadecadienoyl-CoA + NADPH
trans-2-hexadecenoyl-CoA + NADP+
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step in the beta-oxidation of oleoyl-CoA via 2-trans-5-cis-tetradecadienoyl-CoA in mitochondria via the reductase-dependent pathway, enzyme is not involved in the isomerase-dependent pathway, overview
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?
additional information
?
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key enzyme in the beta-oxidation of unsaturated fatty acids
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-
?
additional information
?
-
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3,5-cis-tetradecadienoyl-CoA is also converted by the reductase pathway of beta-oxidation in mitochondria via 2,4-cis-didehydrotetradecadienoyl-CoA
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-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
FAD
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determined by HPLC or fluorometrically, molar ratio of cofactor to enzyme: 1
FMN
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determined by HPLC or fluorometrically, molar ratio of cofactor to enzyme: 1
NADPH
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hydrogen transfer of a hydride ion from NADPH to the substrate via the enzyme bound FAD
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Iron
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
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NADH inhibits mitochondrial beta-oxidation, while acetyl-CoA has no effect
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
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.
Prostatic Neoplasms
2,4-dienoyl-CoA reductase regulates lipid homeostasis in treatment-resistant prostate cancer.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
additional information
additional information
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kinetics of oleoyl-CoA degradation in mitochondrial protein extract
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0.00044
NADPH
mutant enzyme Y166F, in 50 mM potassium phosphate buffer (pH 7.4)
0.0008
NADPH
wild type enzyme, in 50 mM potassium phosphate buffer (pH 7.4)
0.00141
NADPH
mutant enzyme C337A, in 50 mM potassium phosphate buffer (pH 7.4)
0.0024
NADPH
mutant enzyme H252A/Y166F, in 50 mM potassium phosphate buffer (pH 7.4)
0.00534
NADPH
mutant enzyme E164A, in 50 mM potassium phosphate buffer (pH 7.4)
0.00548
NADPH
mutant enzyme H252A, in 50 mM potassium phosphate buffer (pH 7.4)
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.008
NADPH
mutant enzyme C337A, in 50 mM potassium phosphate buffer (pH 7.4)
0.011
NADPH
mutant enzyme H252A, in 50 mM potassium phosphate buffer (pH 7.4)
0.15
NADPH
mutant enzyme E164A, in 50 mM potassium phosphate buffer (pH 7.4)
0.44
NADPH
mutant enzyme H252A/Y166F, in 50 mM potassium phosphate buffer (pH 7.4)
2.5
NADPH
mutant enzyme Y166F, in 50 mM potassium phosphate buffer (pH 7.4)
9.5
NADPH
wild type enzyme, in 50 mM potassium phosphate buffer (pH 7.4)
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.0015
mutant enzyme C334A/C337A, with 2-trans,4-trans-decadienoyl-CoA as substrate
0.0067
mutant enzyme C337A, with 2-trans,4-trans-decadienoyl-CoA as substrate
0.007
mutant enzyme H252A, with 2-trans,4-trans-decadienoyl-CoA as substrate
0.095
mutant enzyme E164A, with 2-trans,4-trans-decadienoyl-CoA as substrate
0.33
mutant enzyme H252A/Y166F, with 2-trans,4-trans-decadienoyl-CoA as substrate
2.02
mutant enzyme Y166F, with 2-trans,4-trans-decadienoyl-CoA as substrate
7.21
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purified recombinant truncated His-tagged enzyme, substrate 2,4-trans-hexadienoyl-CoA
7.54
wild type enzyme, with 2-trans,4-trans-decadienoyl-CoA as substrate
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
physiological function
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DECR is the major reductase involved in polyunsaturated fatty acid beta-oxidation. DECR is related to bacterial reductases. A DECR null mutant is unable to catabolize unsaturated fatty acids and accumulates the intermediate 2,4-decadienoyl-CoA. The mutant is unable to survive in macrophages and is avirulent in BALB/c mice
malfunction
the gene disruption of fadH, which 2,4-dienoyl-CoA reductase, impairs production of eicosapentaenoic acid under docosahexaenoic acid-supplemented conditions, and the estimated conversion rate decreases by 86% compared to that of the parent strain
malfunction
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the gene disruption of fadH, which 2,4-dienoyl-CoA reductase, impairs production of eicosapentaenoic acid under docosahexaenoic acid-supplemented conditions, and the estimated conversion rate decreases by 86% compared to that of the parent strain
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
34000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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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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
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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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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C337A
the mutation results in the loss of most of the iron and acid-labile sulfur and exhibits 0.09% of wild type activity
Y166F
mutant exhibits 27% of the wild type activity, however, the product of the reduction is 3-enoyl-CoA instead of 2-enoyl-CoA
Y166F/H252A
the double mutation exhibits 4.4% of the wild type activity
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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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80°C, purified recombinant truncated enzyme, completely stable for at least 6 months
-
22°C, room temperature, purified recombinant truncated enzyme, 70% remaining activity after 1 week
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ion-exchange chromatography or dye-ligand chromatography, affinity chromatography
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partial, solubilization of enzyme using Triton X-100 from heart mitochondria
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recombinant enzyme from strain BL21(DE3) via DEAE ion exchange and affinity chromatography
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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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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
functional overexpression of truncated His-tagged enzyme in Escherichia coli strain BL21(DE3)
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Mizugaki, M.; Nishimaki, T.; Yamamoto, H.; Nishimura, S.; Sagi, M.; Yamanaka, H.
Studies on the metabolism of unsaturated fatty acids. VIII. Induction of 2,4-dienoyl-CoA reductase in Escherichia coli on the addition of unsaturated fatty acids
J. Biochem.
91
1453-1456
1982
Escherichia coli, Escherichia coli B / ATCC 11303
brenda
Dommes, V.; Luster, W.; Cvetanovic, M.; Kunau, W.H.
Purification by affinity chromatography of 2,4-dienoyl-CoA reductases from bovine liver and Escherichia coli
Eur. J. Biochem.
125
335-341
1982
Bos taurus, Escherichia coli
brenda
Gruvitz, A.; Rottensteiner, H.; Kilpelainen, S.H.; Hartig, A.; Hiltunen, J.K.; Binder, M.; Dawes, I.W.; Hamilton, B.
The Saccharomyces cerevisiae peroxisomal 2,4-dienoyl-CoA reductase is encoded by the oleate-inducible gene SPS19
J. Biol. Chem.
272
22140-22147
1997
Saccharomyces cerevisiae
brenda
He, X.Y.; Yang, S.Y.; Schulz, H.
Cloning and expression of the fadH gene and characterization of the gene product 2,4-dienoyl coenzyme A reductase from Escherichia coli
Eur. J. Biochem.
248
516-520
1997
Escherichia coli
brenda
Liang, X.; Thorpe, C.; Schulz, H.
2,4-Dienoyl-CoA reductase from Escherichia coli is a novel iron-sulfur flavoprotein that functions in fatty acid beta-oxidation
Arch. Biochem. Biophys.
380
373-379
2000
Escherichia coli
brenda
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
Ren, Y.; Schulz, H.
Metabolic functions of the two pathways of oleate beta-oxidation double bond metabolism during the beta-oxidation of oleic acid in rat heart mitochondria
J. Biol. Chem.
278
111-116
2003
Rattus norvegicus
brenda
Hubbard, P.A.; Liang, X.; Schulz, H.; Kim, J.J.
The crystal structure and reaction mechanism of Escherichia coli 2,4-dienoyl-CoA reductase
J. Biol. Chem.
278
37553-37560
2003
Escherichia coli
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
Tu, X.; Hubbard, P.A.; Kim, J.J.; Schulz, H.
Two distinct proton donors at the active site of Escherichia coli 2,4-dienoyl-CoA reductase are responsible for the formation of different products
Biochemistry
47
1167-1175
2008
Escherichia coli (P42593), Escherichia coli
brenda