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(2E,4E)-2,4-decadienoyl-CoA + NADPH + H+
(3E)-3-decaenoyl-CoA + NADP+
(2E,4E)-2,4-decadienoyl-CoA + NADPH + H+
(3E)-deca-3-enoyl-CoA + NADP+
(2E,4E)-2,4-hexadienoyl-CoA + NADPH + H+
(3E)-3-hexenoyl-CoA + NADP+
-
-
-
?
(2E,4E)-2,4-hexadienoyl-CoA + NADPH + H+
(3E)-hexa-3-enoyl-CoA + NADP+
(2E,4E)-2,4-octadienoyl-CoA + NADPH + H+
(3E)-3-octaenoyl-CoA + NADP+
(2E,4E)-hexa-2,4-dienoyl-CoA + NADPH + H+
(3E)-hex-3-enoyl-CoA + NADP+
-
-
-
-
?
(2E,4Z)-2,4-decadienoyl-CoA + NADPH + H+
(3E)-3-decaenoyl-CoA + NADP+
2,4,7,10,13,16,19-docosaheptaenoyl-CoA + NADPH
?
-
assay contains additionally 0.06% Triton X-100
-
-
?
2,4,7,10,13,16,19-docosaheptaenoyl-CoA + NADPH + H+
(3E)-3,7,10,13,16,19-docosahexaenoyl-CoA + NADP+
2,4-hexadienoyl-CoA + NADPH
trans-3-hexenoyl-CoA + NADP+
-
-
-
-
?
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-decadienoyl-CoA + NADPH
3-trans-decenoyl-CoA + NADP+
2-trans,4-cis-decadienoylcarnitine + ?
?
-
abnormal unsaturated fatty acid oxidation
-
-
?
2-trans,4-trans-decadienoyl-CoA + NADPH
3-decenoyl-CoA + NADP+
2-trans,4-trans-hexadienoyl-CoA + NADPH
?
5-methyl-trans-trans-2,4-hexadienoyl-CoA + NADPH
5-methyl-trans-3-hexenoyl-CoA + NADP+
-
substrate analogue, recombinant enzyme
-
-
?
5-phenyl-(2E,4E)-2,4-pentadienoyl-CoA + NADPH + H+
5-phenyl-(3E)-penta-3-enoyl-CoA + NADP+
-
-
-
-
?
pent-2,4-dienoyl-CoA + NADPH
?
-
-
-
-
?
trans, trans-2,4-decadienoyl-CoA + NADPH + H+
trans-deca-3-enoyl-CoA + NADP+
-
-
-
-
?
trans-2,3-didehydroacyl-CoA + NADP+
trans,trans-2,3,4,5-tetradehydroacyl-CoA + NADPH + H+
-
-
-
-
?
trans-trans-2,4-hexadienoyl-CoA + NADPH
trans-3-hexenoyl-CoA + NADP+
additional information
?
-
(2E,4E)-2,4-decadienoyl-CoA + NADPH + H+
(3E)-3-decaenoyl-CoA + NADP+
-
-
-
-
?
(2E,4E)-2,4-decadienoyl-CoA + NADPH + H+
(3E)-3-decaenoyl-CoA + NADP+
-
-
-
?
(2E,4E)-2,4-decadienoyl-CoA + NADPH + H+
(3E)-3-decaenoyl-CoA + NADP+
-
-
-
-
?
(2E,4E)-2,4-decadienoyl-CoA + NADPH + H+
(3E)-deca-3-enoyl-CoA + NADP+
preferred substrate
-
-
?
(2E,4E)-2,4-decadienoyl-CoA + NADPH + H+
(3E)-deca-3-enoyl-CoA + NADP+
preferred substrate
-
-
?
(2E,4E)-2,4-decadienoyl-CoA + NADPH + H+
(3E)-deca-3-enoyl-CoA + NADP+
preferred substrate
-
-
?
(2E,4E)-2,4-hexadienoyl-CoA + NADPH + H+
(3E)-hexa-3-enoyl-CoA + NADP+
-
-
-
?
(2E,4E)-2,4-hexadienoyl-CoA + NADPH + H+
(3E)-hexa-3-enoyl-CoA + NADP+
-
-
-
?
(2E,4E)-2,4-hexadienoyl-CoA + NADPH + H+
(3E)-hexa-3-enoyl-CoA + NADP+
-
-
-
?
(2E,4E)-2,4-octadienoyl-CoA + NADPH + H+
(3E)-3-octaenoyl-CoA + NADP+
-
-
-
?
(2E,4E)-2,4-octadienoyl-CoA + NADPH + H+
(3E)-3-octaenoyl-CoA + NADP+
-
-
-
-
?
(2E,4Z)-2,4-decadienoyl-CoA + NADPH + H+
(3E)-3-decaenoyl-CoA + NADP+
-
-
-
-
?
(2E,4Z)-2,4-decadienoyl-CoA + NADPH + H+
(3E)-3-decaenoyl-CoA + NADP+
-
preferred over substrate (2E,4E)-2,4-decadienoyl-CoA
-
-
?
2,4,7,10,13,16,19-docosaheptaenoyl-CoA + NADPH + H+
(3E)-3,7,10,13,16,19-docosahexaenoyl-CoA + NADP+
-
-
-
?
2,4,7,10,13,16,19-docosaheptaenoyl-CoA + NADPH + H+
(3E)-3,7,10,13,16,19-docosahexaenoyl-CoA + NADP+
-
-
-
?
2-trans,4-cis-decadienoyl-CoA + NADPH
3-trans-decenoyl-CoA + NADP+
-
-
-
?
2-trans,4-cis-decadienoyl-CoA + NADPH
3-trans-decenoyl-CoA + NADP+
-
-
-
-
?
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+
-
-
-
-
?
2-trans,4-trans-decadienoyl-CoA + NADPH
3-decenoyl-CoA + NADP+
-
-
-
-
?
2-trans,4-trans-decadienoyl-CoA + NADPH
3-decenoyl-CoA + NADP+
-
-
-
?
2-trans,4-trans-hexadienoyl-CoA + NADPH
?
-
-
-
-
ir
2-trans,4-trans-hexadienoyl-CoA + NADPH
?
-
-
-
-
ir
trans-trans-2,4-hexadienoyl-CoA + NADPH
trans-3-hexenoyl-CoA + NADP+
-
-
-
-
r
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
?
-
-
the 3',5'-ADP moiety of 2,4-dienoyl-CoA thioesters contributes a substantial part to the binding of these compounds to 2,4-dienoyl-CoA reductases
-
-
-
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
-
-
?
additional information
?
-
products are DELTA3-enoyl-CoAs but not Delta2-enoyl-CoAs
-
-
-
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0.006 - 0.0154
(2E,4E)-2,4-decadienoyl-CoA
0.0265 - 0.059
(2E,4E)-2,4-hexadienoyl-CoA
0.0158
(2E,4E)-2,4-octadienoyl-CoA
pH 7.4, 25°C
0.102 - 0.155
2,4,7,10,13,16,19-docosaheptaenoyl-CoA
0.006
2,4-decadienoyl-CoA
-
-
0.0065
2-fluoro-trans-trans-2,4-octadienoyl-CoA
-
recombinant His-tagged truncated wild-type enzyme, pH 6.0, 22°C
0.00046 - 0.108
2-trans,4-trans-hexadienoyl-CoA
0.016
5-methyl-trans-trans-2,4-hexadienoyl-CoA
-
recombinant His-tagged truncated wild-type enzyme, pH 6.0, 22°C
0.0045 - 0.154
trans-trans-2,4-hexadienoyl-CoA
0.006
(2E,4E)-2,4-decadienoyl-CoA
presence of 0.1% albumin, pH 7.4, 30°C
0.0062
(2E,4E)-2,4-decadienoyl-CoA
pH 6.0, 23°C
0.0154
(2E,4E)-2,4-decadienoyl-CoA
pH 7.4, 25°C
0.0265
(2E,4E)-2,4-hexadienoyl-CoA
pH 6.0, 23°C
0.059
(2E,4E)-2,4-hexadienoyl-CoA
presence of 0.1% albumin, pH 7.4, 30°C
0.102
2,4,7,10,13,16,19-docosaheptaenoyl-CoA
absence of albumin, pH 7.4, 30°C
0.155
2,4,7,10,13,16,19-docosaheptaenoyl-CoA
-
-
0.00046
2-trans,4-trans-hexadienoyl-CoA
-
-
0.108
2-trans,4-trans-hexadienoyl-CoA
-
-
0.0025
NADPH
-
-
0.008
NADPH
-
recombinant His-tagged truncated wild-type enzyme, pH 6.0, 22°C
0.014
NADPH
-
recombinant His-tagged mutant E227A, pH 6.0, 22°C
0.0605
NADPH
pH 6.0, 23°C
0.131
NADPH
-
recombinant His-tagged mutant E276A, pH 6.0, 22°C
0.195
NADPH
-
recombinant His-tagged mutant D300A, pH 6.0, 22°C
0.215
NADPH
-
recombinant His-tagged mutant E154A, 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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0.00281
-
4-cis-decenoyl-CoA, NADPH, protein fraction virtually free of 2-enoyl-CoA reductase activity
0.003
-
2-trans,4-trans-decadienoyl-CoA, NADPH, muscle
0.0046
-
2-trans,4-cis-decadienoyl-CoA, NADPH, muscle
0.0084
-
2-trans,4-trans-decadienoyl-CoA, NADPH, liver
0.00882
-
2-trans,4-trans-hexadienoyl-CoA, NADPH, protein fraction virtually free of 2-enoyl-CoA reductase activity
0.0124
-
trans-2-trans-4-hexedienoyl-CoA as a substrate
0.013
-
2-trans,4-cis-decadienoyl-CoA, NADPH, liver
0.0274
-
hexa-2,4-dienoyl-CoA, NADPH, normally fed
0.0331
-
trans-2-trans-4-hexedienoyl-CoA as a substrate, clofibrate-treated
0.0394
-
hexa-2,4-dienoyl-CoA, NADPH, fed soy-bean oil
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
2.2
-
reductase activity measured in liver mitochondrial extract
2.6
-
reductase activity measured in muscle mitochondrial extract
2.8
-
substrate (2E,4E)-2,4-octadienoyl-CoA, pH 6.5, 25°C
20
-
2-trans,4-trans-decadienoyl-CoA, NADPH
4.1
-
2-trans,4-trans-decadienoyl-CoA, NADPH
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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metabolism
key enzyme required for beta-oxidation of polyunsaturated fatty acids
malfunction
cold intolerance of Decr-/- mice is due to failure in maintaining appropriate heat production at least partly due to failure of brown adipose tissue (BAT) thermogenesis
malfunction
enzyme (DECR1) knockout induces ER stress and sensitises castration-resistant prostate cancer cells to ferroptosis. In vivo, DECR1 deletion impairs lipid metabolism and reduces tumour growth of castration-resistant prostate cancer, emphasizing the importance of DECR1 in the development of treatment resistance
physiological function
an SPS19 deleted strain is unable to utilize petroselineate (cis-C18:1(6)) as the sole carbon source, but remains viable on oleate (cis-C18:1(9)). SPS19 is dispensable for growth and sporulation on solid acetate and oleate media, but is essential for these processes to occur on petroselineate
physiological function
cold intolerance of Decr?/? mice is due to failure in maintaining appropriate heat production at least partly due to failure of brown adipose tissue thermogenesis. Activation of lipolysis is attenuated despite of functional norepinephrine-signaling and inappropriate expression of genes contributing to thermogenesis in interscapular brown adipose rissue when the Decr?/? mice are exposed to cold
physiological function
DECR1 participates in redox homeostasis by controlling the balance between saturated and unsaturated phospholipids. DECR1 knockout induces ER stress and sensitizes castration-resistant prostate cancer cells to ferroptosis. In vivo, DECR1 deletion impairs lipid metabolism and reduces castration-resistant prostate cancer tumor growth
physiological function
-
dienoyl-CoA and NADPH bind to the 2,4-dienoyl-CoA reductase via a sequential kinetic mechanism with a random order of nucleotide and dienoyl-CoA addition. A proton transfer step is rate limiting for (2E,4E)-hexa-2,4-dienoyl-CoA substrate, addition of a phenyl ring to the diene in 5-phenyl-(2E,4E)-2,4-pentadienoyl-CoA results in the reversal of the rate-determining step. The chemical mechanism is stepwise where hydride transfer from NADPH occurs followed by protonation of the dienolate intermediate
physiological function
human mitochondrial 2,4-reductase functions in the beta-oxidation of unsaturated fatty acids. A yeast sps19D mutant expressing human 2,4-reductase ending with the native C-terminus cannot grow on petroselinic acid medium but can grow when the protein is extended with a peroxisomal targeting tripeptide, Ser-Lys-Leu
physiological function
-
in vitro, 4-cis-decenoyl-CoA is only degraded when the 2,4-dienoyl-CoA reductase step in linoleic acid degradation is not blocked by lack of NADPH
physiological function
-
metabolism of unsaturated fatty acids occurs mainly in the mitochondria and the peroxisomes of the proximal tubule in the kidney
physiological function
SPS19 is induced during sporulation in diploids. Under oleate induction conditions, SPS19 is transcribed via an oleate response element (ORE) independently of ploidy or sporulation.The SPS19 ORE is the binding target of the Pip2p and Oaf1p transcription factors
physiological function
the reductase does not seem to constitute a rate limiting step in the peroxisomal degradation of docosahexaenoic acid. The reduction of docosaheptaenoyl-CoA is severely decreased in the presence of albumin
physiological function
the removal of double bonds from odd-numbered carbons in arachidonic acid requires both NADPH-dependent 2,4-dienoyl-CoA reductase and delta 3,5,delta 2,4-dienoyl-CoA isomerase. One complete cycle of 5,8-14:2 and 5,8,11,14-20:4 beta-oxidation yields, respectively, 6-dodecenoic and 6,9,12-octadecatrienoic acids
physiological function
the enzyme regulates lipid homeostasis in treatment-resistant prostate cancer
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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
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