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Information on EC 1.3.1.34 - 2,4-dienoyl-CoA reductase [(2E)-enoyl-CoA-producing] and Organism(s) Homo sapiens

for references in articles please use BRENDA:EC1.3.1.34
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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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This record set is specific for:
Homo sapiens
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Word Map
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  • 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
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
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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2,4-dienoyl-CoA reductase [NADPH]
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4-enoyl-CoA reductase (NADPH)
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4-enoyl-CoA reductase [NADPH]
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DECR
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peroxisomal 2,4-dienoyl CoA reductase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
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redox reaction
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reduction
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PATHWAY SOURCE
PATHWAYS
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].
CAS REGISTRY NUMBER
COMMENTARY hide
82869-38-3
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(2E,4E)-2,4-decadienoyl-CoA + NADPH
?
show the reaction diagram
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-
?
(2E,4E)-2,4-hexadienoyl-CoA + NADPH
?
show the reaction diagram
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?
2,4,7,10,13,16,19-docosaheptaenoyl-CoA + NADPH
?
show the reaction diagram
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-
-
?
2,4-hexadienoyl-CoA + NADPH
trans-3-hexenoyl-CoA + NADP+
show the reaction diagram
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-
-
?
2,4-trans-decadienoyl-CoA + NADPH
? + NADP+
show the reaction diagram
2,4-trans-hexadienoyl-CoA + NADPH
trans-3-hexenoyl-CoA + NADP+
show the reaction diagram
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-
-
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?
2-trans,4-trans-decadienoyl-CoA + NADPH
3-decenoyl-CoA + NADP+
show the reaction diagram
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?
additional information
?
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key enzyme in the beta-oxidation of unsaturated fatty acids
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?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
additional information
?
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key enzyme in the beta-oxidation of unsaturated fatty acids
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?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADPH
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
albumin
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.21
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purified recombinant truncated His-tagged enzyme, substrate 2,4-trans-hexadienoyl-CoA
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6
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assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22
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assay at room temperature
30
enzyme essay
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
DECR2_HUMAN
292
0
30778
Swiss-Prot
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DECR_HUMAN
335
0
36068
Swiss-Prot
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
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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
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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%)
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22
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purified recombinant truncated enzyme is highly stable at room temperature
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-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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sensitive to freezing, activity loss upon storage on ice
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni-NTA chromatography
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
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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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team