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Information on EC 1.3.1.124 - 2,4-dienoyl-CoA reductase [(3E)-enoyl-CoA-producing]
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1.3.1.124 2,4-dienoyl-CoA reductase [(3E)-enoyl-CoA-producing]IUBMB Comments
This enzyme, characterized from eukaryotic organisms, catalyses the reduction of either (2E,4E)-2,4-dienoyl-CoA or (2E,4Z)-2,4-dienoyl-CoA to (3E)-3-enoyl-CoA. The best substrates for the enzyme from bovine liver have a chain-length of 8 or 10 carbons. Mammals possess both mitochondrial and peroxisomal variants of this enzyme. cf. EC 1.3.1.34, 2,4-dienoyl-CoA reductase [(2E)-enoyl-CoA-producing].
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Word Map
The enzyme appears in viruses and cellular organisms
Reaction Schemes
a (2E)-2-enoyl-CoA
+
=
a (2E,4E)-2,4-dienoyl-CoA
+
+
a (3E)-3-enoyl-CoA
+
=
a (2E,4E)-2,4-dienoyl-CoA
+
+
a (3E)-3-enoyl-CoA
+
=
a (2E,4Z)-2,4-dienoyl-CoA
+
+
Synonyms
decr1, sps19, 4-enoyl-coa reductase, decr2, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
2,4-dienoyl-CoA reductase
4-enoyl-CoA reductase
DECR
additional information
-
enzyme belongs to the short-chain dehydrogenase/reductase family with a distinctive catalytic center
2,4-dienoyl-CoA reductase
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
a (2E)-2-enoyl-CoA + NADP+ = a (2E,4E)-2,4-dienoyl-CoA + NADPH + H+
reaction mechanism, E276 is the proton donor in catalysis
-
a (2E)-2-enoyl-CoA + NADP+ = a (2E,4E)-2,4-dienoyl-CoA + NADPH + H+
reaction mechanism, enzyme-ligand interactions in a distinctive short-chain reductase active site, catalytic site structure, stabilization of the dienolate reaction intermediate by Tyr199 and Asn148, and NADP+, overview
-
a (2E)-2-enoyl-CoA + NADP+ = a (2E,4E)-2,4-dienoyl-CoA + NADPH + H+
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PATHWAY SOURCE
PATHWAYS
MetaCyc
10-cis-heptadecenoyl-CoA degradation (yeast), 10-trans-heptadecenoyl-CoA degradation (reductase-dependent, yeast), fatty acid beta-oxidation IV (unsaturated, even number), fatty acid beta-oxidation V (unsaturated, odd number, di-isomerase-dependent), oleate beta-oxidation (reductase-dependent, yeast)
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SYSTEMATIC NAME
IUBMB Comments
(3E)-3-enoyl-CoA:NADP+ 4-oxidoreductase
This enzyme, characterized from eukaryotic organisms, catalyses the reduction of either (2E,4E)-2,4-dienoyl-CoA or (2E,4Z)-2,4-dienoyl-CoA to (3E)-3-enoyl-CoA. The best substrates for the enzyme from bovine liver have a chain-length of 8 or 10 carbons. Mammals possess both mitochondrial and peroxisomal variants of this enzyme. cf. EC 1.3.1.34, 2,4-dienoyl-CoA reductase [(2E)-enoyl-CoA-producing].
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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)-hexa-2,4-dienoyl-CoA + NADPH + H+
(3E)-hex-3-enoyl-CoA + NADP+
-
-
-
?
2,4,7,10,13,16,19-docosaheptaenoyl-CoA + NADPH
?
-
assay contains additionally 0.06% Triton X-100
-
?
2-cis,4-cis/trans-dienoyl-CoA + NADPH + H+
3-trans-enoyl-CoA + NADP+
-
-
-
?
2-fluoro-trans-trans-2,4-octadienoyl-CoA + NADPH
2-fluoro-trans-3-octenoyl-CoA + NADP+
-
substrate analogue, recombinant enzyme, reaction mechanism
-
?
2-trans,4-cis-decadienoylcarnitine + ?
?
-
abnormal unsaturated fatty acid oxidation
-
?
5-methyl-trans-trans-2,4-hexadienoyl-CoA + NADPH
5-methyl-trans-3-hexenoyl-CoA + NADP+
-
substrate analogue, recombinant enzyme
-
?
trans-2,3-didehydroacyl-CoA + NADP+
trans,trans-2,3,4,5-tetradehydroacyl-CoA + NADPH + H+
-
-
-
?
2-trans,4-cis-decadienoyl-CoA + NADPH
3-trans-decenoyl-CoA + NADP+
-
-
-
?
2-trans,4-cis-decadienoyl-CoA + NADPH
3-trans-decenoyl-CoA + NADP+
-
-
stereochemistry not determined
?
2-trans,4-trans-decadienoyl-CoA + NADPH
3-decenoyl-CoA + NADP+
-
-
-
?
trans-trans-2,4-hexadienoyl-CoA + NADPH
trans-3-hexenoyl-CoA + NADP+
-
reaction mechanism
-
?
trans-trans-2,4-hexadienoyl-CoA + NADPH
trans-3-hexenoyl-CoA + NADP+
-
substrate binding mechanism and structure
-
r
additional information
?
-
-
enzyme is the key enzyme of beta-oxidation of unsaturated fatty acid in mitochondria and to a lesser extent in peroxisomes, three accessory proteins are involved in the pathway
-
?
additional information
?
-
-
key enzyme in the beta-oxidation of unsaturated fatty acids, naturally occuring lethal enzyme deficiency
-
?
additional information
?
-
-
2,4-dienoyl-CoA reductase as an auxiliary enzyme in the mitochondrial beta-oxidation of unsaturated fatty acids
-
?
additional information
?
-
-
DECR may also play a role in the degradation of fatty acids containing odd-numbered double bonds because the intermediate 2,5-dienoyl-CoA may be isomerized by enoyl-CoA isomerase to 3,5-dienoyl-CoA and then converted to 2,4-dienoyl-CoA by a specific delta3,5,delta2,4-dienoyl-CoA isomerase
-
?
additional information
?
-
-
in eukaryotes, double bonds in even-numbered positions are reduced by an NADPH-dependent 2,4-dienoyl-CoA reductase to 3-enoyl-CoA, which is then isomerized by enoyl-CoA isomerase to trans-2-enoyl-CoA, suitable for further oxidation
-
?
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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
2-cis,4-cis/trans-dienoyl-CoA + NADPH + H+
3-trans-enoyl-CoA + NADP+
-
-
-
-
?
2-trans,4-cis-decadienoylcarnitine + ?
?
-
abnormal unsaturated fatty acid oxidation
-
-
?
trans-2,3-didehydroacyl-CoA + NADP+
trans,trans-2,3,4,5-tetradehydroacyl-CoA + NADPH + H+
-
-
-
-
?
additional information
?
-
-
enzyme is the key enzyme of beta-oxidation of unsaturated fatty acid in mitochondria and to a lesser extent in peroxisomes, three accessory proteins are involved in the pathway
-
-
?
additional information
?
-
-
key enzyme in the beta-oxidation of unsaturated fatty acids, naturally occuring lethal enzyme deficiency
-
-
?
additional information
?
-
-
2,4-dienoyl-CoA reductase as an auxiliary enzyme in the mitochondrial beta-oxidation of unsaturated fatty acids
-
-
?
additional information
?
-
-
DECR may also play a role in the degradation of fatty acids containing odd-numbered double bonds because the intermediate 2,5-dienoyl-CoA may be isomerized by enoyl-CoA isomerase to 3,5-dienoyl-CoA and then converted to 2,4-dienoyl-CoA by a specific delta3,5,delta2,4-dienoyl-CoA isomerase
-
-
?
additional information
?
-
-
in eukaryotes, double bonds in even-numbered positions are reduced by an NADPH-dependent 2,4-dienoyl-CoA reductase to 3-enoyl-CoA, which is then isomerized by enoyl-CoA isomerase to trans-2-enoyl-CoA, suitable for further oxidation
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Clofibrate
-
ethyl alpha-(p-chlorophenoxy)isobutyrate, activation ATP-stimulated
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Breast Neoplasms
Elevated expression of DecR1 impairs ErbB2/Neu-induced mammary tumor development.
Carcinogenesis
Elevated expression of DecR1 impairs ErbB2/Neu-induced mammary tumor development.
Neoplasm Metastasis
Human DECR1 is an androgen-repressed survival factor that regulates PUFA oxidation to protect prostate tumor cells from ferroptosis.
Neoplasms
2,4-dienoyl-CoA reductase regulates lipid homeostasis in treatment-resistant prostate cancer.
Neoplasms
Elevated expression of DecR1 impairs ErbB2/Neu-induced mammary tumor development.
Neoplasms
Human DECR1 is an androgen-repressed survival factor that regulates PUFA oxidation to protect prostate tumor cells from ferroptosis.
Non-alcoholic Fatty Liver Disease
Protein interaction mapping interpretation of none alcoholic fatty liver disease model of rats after fat diet feeding.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0065
2-fluoro-trans-trans-2,4-octadienoyl-CoA
-
recombinant His-tagged truncated wild-type enzyme, pH 6.0, 22°C
0.016
5-methyl-trans-trans-2,4-hexadienoyl-CoA
-
recombinant His-tagged truncated wild-type enzyme, pH 6.0, 22°C
0.0045
trans-trans-2,4-hexadienoyl-CoA
-
recombinant His-tagged mutant D300A, pH 6.0, 22°C
0.014
trans-trans-2,4-hexadienoyl-CoA
-
recombinant His-tagged truncated wild-type enzyme, pH 6.0, 22°C
0.041
trans-trans-2,4-hexadienoyl-CoA
-
recombinant His-tagged mutant E227A, pH 6.0, 22°C
0.067
trans-trans-2,4-hexadienoyl-CoA
-
recombinant His-tagged mutant E276A, pH 6.0, 22°C
0.154
trans-trans-2,4-hexadienoyl-CoA
-
recombinant His-tagged mutant E154A, pH 6.0, 22°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.00281
-
4-cis-decenoyl-CoA, NADPH, protein fraction virtually free of 2-enoyl-CoA reductase activity
0.00882
-
2-trans,4-trans-hexadienoyl-CoA, NADPH, protein fraction virtually free of 2-enoyl-CoA reductase activity
0.0331
-
trans-2-trans-4-hexedienoyl-CoA as a substrate, clofibrate-treated
0.0461
-
pent-2,4-dienoyl-CoA, NADPH, fed partially hydrogenated marine oils
0.0605
-
hexa-2,4-dienoyl-CoA, NADPH, fed partially hydrogenated marine oils
0.0895
-
pent-2,4-dienoyl-CoA, NADPH, fed partially hydrogenated marine oils
0.5
-
reductase activity for wild-type and Decr-/- mice, the observed residual activity represents the activity of mitochondrial 2-enoyl thioester reductase, which functions in mitochondrial fatty acid synthesis and can also reduce 2,4-hexadienoyl-CoA in vitro
additional information
additional information
-
analysis of liver fatty acids after the mice are fasted for 24 h indicates that fasting has a minor effect on the lipid content of wild type liver, with an overall increase of 29% in the concentration of fatty acids, in Decr-/- mice, the overall concentration of fatty acids increases by 108% after fasting
additional information
-
Decr-/- mice show decreased blood glucose and elevated non-esterified fatty acids concentrations after fasting in comparison to wild type mice
additional information
-
fasting increases the total concentration of acylcarnitines by 2fold in wild type mice (567 nM), in Decr-/- mice, a markedly higher 9fold increase is observed (2150 nM)
additional information
-
immunoblotting of mitochondrial extracts from liver, muscle and heart with an antibody against human DECR reveals a detectable signal from wild type mice, whereas no signal can be detected for homozygous null mutant mice
additional information
-
in Decr-/- mice, the overall concentration of fatty acids increases by 108% after fasting, the most profound changes between fasted wild type and Decr-/- mice are observed for the levels of palmitoleic acid (C16:1), oleic acid, linolenic acid (C18:3) and linoleic acid, which are 2.5- to 3.8fold higher in Decr-/- mice, in comparison to the fed state, the concentrations of monounsaturated fatty acids and polyunsaturated fatty acids increase by 288% and 254%, respectively
additional information
-
mitochondrial 2,4-dienoyl-CoA reductase activity in mice is indispensable for the complete oxidation of (poly)unsaturated fatty acids and for adaptation to metabolic stress
additional information
-
mitochondrial 2,4-dienoyl-CoA reductase deficiency in mice results in severe hypoglycemia with stress intolerance and unimpaired ketogenesis
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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
-
source of the natural substrate 2-trans,4cis-decadienoylcarnitine
brenda
-
-
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
-
brenda
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
31300
-
purified recombinant enzyme, encoded by the gene PDCR, calculated from sequence of cDNA, SDS-PAGE
32410
-
purified recombinant enzyme, electrospray ionization-mass spectrometry
36066
-
4 * 36066, immature monomer of the 120 kDa isoform, RT-PCR, PCR-fragment subcloned to pUC18, sequenced
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homotetramer
-
4 * 36066, immature monomer of the 120 kDa isoform, RT-PCR, PCR-fragment subcloned to pUC18, sequenced
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D117A
-
site-directed mutagenesis, mutant is expressed in inclusion bodies and cannot be refolded to a functional enzyme after extraction from inclusion bodies with 8 M urea as denatured protein
D300A
-
site-directed mutagenesis, reduced activity and altered kinetics compared to the wild-type enzyme
E154A
-
site-directed mutagenesis, reduced activity and altered kinetics compared to the wild-type enzyme
E227A
-
site-directed mutagenesis, reduced activity and altered kinetics compared to the wild-type enzyme
E276A
-
site-directed mutagenesis, reduced activity and altered kinetics compared to the wild-type enzyme
additional information
additional information
-
synthesis of polyhydroxyalkanoate from 10-trans-heptadecenoic acid in mutants devoid of 2,4-dienoyl-CoA reductase reveals degradation of the trans fatty acid directly via the enoyl-CoA hydratase II activity of the multifunctional enzyme. Level of polyhydroxyalkanoate is 10-25% to that of wild-type in mutants lacking 2,4-dienoyl-CoA reductase
additional information
-
synthesis of polyhydroxyalkanoate from 10-trans-heptadecenoic acid in mutants devoid of 2,4-dienoyl-CoA reductase reveals degradation of the trans fatty acid directly via the enoyl-CoA hydratase II activity of the multifunctional enzyme. Level of polyhydroxyalkanoate is 10-25% to that of wild-type in mutants lacking 2,4-dienoyl-CoA reductase
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged truncated wild-type and of mutant enzymes from Escherichia coli strain BL21(DE3) by one-step nickel affinity chromatography, to over 95% purity
-
recombinant wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, to homogeneity
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
creation of a DECR-deficient mouse line, fasted Decr-/- mice display increased serum acylcarnitines, especially decadienoylcarnitine, a product of the incomplete oxidation of linoleic acid (C18:2), urinary excretion of unsaturated dicarboxylic acids, and hepatic steatosis, wherein unsaturated fatty acids accumulate in liver triacylglycerols, metabolically challenged Decr-/- mice turn on ketogenesis, but unexpectedly develop hypoglycemia
-
expressed in Escherichia coli
overexpression of His-tagged truncated wild-type and of mutant enzymes in Escherichia coli strain BL21(DE3), expression as soluble protein, except for mutant D117A
-
overexpression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3), expression of selenomethionine enzyme in Escherichia coli strain B834(DE3)
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression of 2,4-dienoyl-CoA reductase is up-regulated in pancreas of alcohol-fed rats
-
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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
mutant D117A is expressed in inclusion bodies and cannot be refolded to a functional enzyme after extraction from inclusion bodies with 8 M urea as denatured protein
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Clejan, S.; Schulz, H.
Effect of growth hormone on fatty acid oxidation: growth hormone increases the activity of 2,4-dienoyl-CoA reductase in mitochondria
Arch. Biochem. Biophys.
246
820-828
1986
Rattus norvegicus
brenda
Osmundsen, H.; Cervenka, J.; Bremer, J.
A role for 2,4-enoyl-CoA reductase in mitochondrial beta-oxidation of polyunsaturated fatty acids. Effects of treatment with clofibrate on oxidation of polyunsaturated acylcarnitines by isolated rat liver mitochondria
Biochem. J.
208
749-757
1982
Rattus norvegicus
brenda
Dommes, V.; Baumgart, C.; Kunau, W.H.
Degradation of unsaturated fatty acids in peroxisomes. Existence of a 2,4-dienoyl-CoA reductase pathway
J. Biol. Chem.
256
8259-8262
1981
Rattus norvegicus
brenda
Kunau, W.H.; Dommes, P.
Degradation of unsaturated fatty acids. Identification of intermediates in the degradation of cis-4-decenoyl-CoA by extracts of beef-liver mitochondria
Eur. J. Biochem.
91
533-544
1978
Bos taurus
brenda
Kunau, W.H.; Dommes, V.; Dommes, P.
Degradation of unsaturated fatty acids. 4-Enoyl-CoA reductase: purification, characterization and physiological function
Prog. Lipid Res.
20
327-330
1981
Bos taurus
brenda
Hiltunen, J.K.; Davis, E.J.
Metabolism of pent-4-enoate in rat heart. Reduction of the double bond
Biochem. J.
194
427-432
1981
Rattus norvegicus, Rattus norvegicus Wistar
brenda
Borrebaek, B.; Osmundsen, H.; Christiansen, E.N.; Bremer, J.
Increased 4-enoyl-CoA reductase activity in liver mitochondria of rats fed high-fed diets and its effect on fatty acid oxidation and the inhibitory action of pent-4-enoate
FEBS Lett.
121
23-24
1980
Rattus norvegicus
brenda
Borrebaek, B.; Osmundsen, H.; Bremer, J.
In vivo induction of 4-enoyl-CoA reductase by clofibrate in liver mitochondria and its effect on pent-4-enoate metabolism
Biochem. Biophys. Res. Commun.
93
1173-1180
1980
Rattus norvegicus
brenda
Roe, C.R.; Millington, D.S.; Norwood, D.L.; Sprecher, H.; Mohammed, B.S.; Nada, M.; Schulz, H.; McVie, R.
2,4-Dienolyl-coenzyme A reductase deficiency: a possible new disorder of fatty acid oxidation
J. Clin. Invest.
85
1703-1707
1990
Homo sapiens
brenda
Koivuranta, K.T.; Hakkola, E.H.; Hiltunen, J.K.
Isolation and characterization of cDNA for human 120 kDa mitochondrial 2,4-dienoyl-coenzyme A reductase
Biochem. J.
304
787-792
1994
Homo sapiens
brenda
Mizugaki, M.; Hirose, A.; Suzuki, H.; Miura, K.; Edo, K.; Tomioka, Y.
Subcellular distribution of rat liver NADPH-2,4-dienoyl-CoA reductase
Biol. Pharm. Bull.
19
176-181
1996
Rattus norvegicus
brenda
Fillgrove, K.L.; Anderson, V.E.; Mizugaki, M.
Cloning, expression, and purification of the functional 2,4-dienoyl-CoA reductase from rat liver mitochondria
Protein Expr. Purif.
17
57-63
1999
Rattus norvegicus
brenda
Geisbrecht, B.V.; Liang, X.; Morrell, J.C.; Schulz, H.; Gould, S.J.
The mouse gene PDCR encodes a peroxisomal DELTA2, DELTA4-dienoyl-CoA reductase
J. Biol. Chem.
274
25814-25820
1999
Mus musculus
brenda
Yu, W.; Chu, X.; Chen, G.; Li, D.
Studies of human mitochondrial 2,4-dienoyl-CoA reductase
Arch. Biochem. Biophys.
434
195-200
2005
Homo sapiens
brenda
Alphey, M.S.; Yu, W.; Byres, E.; Li, D.; Hunter, W.N.
Structure and reactivity of human mitochondrial 2,4-dienoyl-CoA reductase: enzyme-ligand interactions in a distinctive short-chain reductase active site
J. Biol. Chem.
280
3068-3077
2005
Homo sapiens
brenda
Robert, J.; Marchesini, S.; Delessert, S.; Poirier, Y.
Analysis of the beta-oxidation of trans-unsaturated fatty acid in recombinant Saccharomyces cerevisiae expressing a peroxisomal PHA synthase reveals the involvement of a reductase-dependent pathway
BIOCHIM. BIOPHYS. ACTA
1734
169-177
2005
Saccharomyces cerevisiae
brenda
Hiltunen, J.K.; Filppula, S.A.; Haeyrinen, H.M.; Koivuranta, K.T.; Hakkola, E.H.
Peroxisomal beta-oxidation of polyunsaturated fatty acids
Biochimie
75
175-182
1993
Rattus norvegicus
brenda
Hiltunen, J.K.
Peroxisomes and beta-oxidation of long-chain unsaturated carboxylic acids
Scand. J. Clin. Lab. Invest. Suppl.
204
33-46
1991
Rattus norvegicus
brenda
Miinalainen, I.; Schmitz, W.; Huotari, A.; Autio, K.; Soininen, R.; Van Themaat, E.; Baes, M.; Herzig, K.; Conzelmann, E.; Hiltunen, J.
Mitochondrial 2,4-dienoyl-CoA reductase deficiency in mice results in severe hypoglycemia with stress intolerance and unimpaired ketogenesis
PLOS Genet.
5
e1000543
2009
Mus musculus
brenda
Satoh, M.; Haruta-Satoh, E.; Yamada, M.; Kado, S.; Nomura, F.
Overexpression of hydroxymethylglutaryl CoA synthase 2 and 2,4-dienoyl-CoA reductase in rat pancreas following chronic alcohol consumption
Pancreas
42
475-482
2013
Rattus norvegicus
brenda
Li, T.P.; Zhu, R.G.; Dong, Y.P.; Liu, Y.H.; Li, S.H.; Chen, G.
Effects of pectin pentaoligosaccharide from Hawthorn (Crataegus pinnatifida Bunge. var. Major) on the activity and mRNA levels of enzymes involved in fatty acid oxidation in the liver of mice fed a high-fat diet
J. Agric. Food Chem.
61
7599-7605
2013
Mus musculus
brenda
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