1.3.1.34: 2,4-dienoyl-CoA reductase [(2E)-enoyl-CoA-producing]
This is an abbreviated version!
For detailed information about 2,4-dienoyl-CoA reductase [(2E)-enoyl-CoA-producing], go to the full flat file.
Word Map on EC 1.3.1.34
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1.3.1.34
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beta-oxidation
-
unsaturated
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polyunsaturated
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odd-numbered
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even-numbered
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3-hydroxyacyl-coa
-
5.3.3.8
-
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
- 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
Reaction
Synonyms
2,4-dienoyl coenzyme A reductase, 2,4-dienoyl-CoA reductase, 2,4-dienoyl-CoA reductase (NADPH), 2,4-dienoyl-CoA reductase [NADPH], 4-enoyl-CoA reductase (NADPH), 4-enoyl-CoA reductase [NADPH], DCR, DECR, FADH, pDCR, peroxisomal 2,4-dienoyl CoA reductase
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Reference
Reference on EC 1.3.1.34 - 2,4-dienoyl-CoA reductase [(2E)-enoyl-CoA-producing]
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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
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
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
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
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
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
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
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
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
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
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)
Semini, G.; Paape, D.; Blume, M.; Sernee, M.F.; Peres-Alonso, D.; Calvignac-Spencer, S.; Doellinger, J.; Jehle, S.; Saunders, E.; McConville, M.J.; Aebischer, T.
Leishmania encodes a bacterium-like 2,4-dienoyl-coenzyme A reductase that is required for fatty acid beta-oxidation and intracellular parasite survival
mBio
11
e01057
2020
Leishmania major
Ogawa, T.; Hirose, K.; Yusuf, Y.; Kawamoto, J.; Kurihara, T.
Bioconversion from docosahexaenoic acid to eicosapentaenoic acid in the marine bacterium Shewanella livingstonensis Ac10
Front. Microbiol.
11
1104
2020
Shewanella livingstonensis (A0A6F8TML5), Shewanella livingstonensis, Shewanella livingstonensis Ac10 (A0A6F8TML5)
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