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Information on EC 5.3.3.21 - DELTA3,5-DELTA2,4-dienoyl-CoA isomerase and Organism(s) Rattus norvegicus and UniProt Accession Q62651

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EC Tree
     5 Isomerases
         5.3 Intramolecular oxidoreductases
             5.3.3 Transposing C=C bonds
                5.3.3.21 DELTA3,5-DELTA2,4-dienoyl-CoA isomerase
IUBMB Comments
The enzyme participates in an alternative degradation route of fatty acids with cis-double bonds on odd-number carbons such as oleate and linoleate. The main physiological substrate is (3E,5Z)-tetradeca-3,5-dienoyl-CoA, but other (3E,5Z)-dienoyl-CoAs with varying carbon chain lengths are also substrates.
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This record set is specific for:
Rattus norvegicus
UNIPROT: Q62651
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The taxonomic range for the selected organisms is: Rattus norvegicus
The enzyme appears in selected viruses and cellular organisms
Synonyms
yor180c, dienoyl-coa isomerase, delta3,5,delta2,4-dienoyl-coa isomerase, delta3,5-delta2,4-dienoyl-coa isomerase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
DELTA3,5,DELTA2,4-dienoyl-CoA isomerase
-
dienoyl-CoA isomerase
-
3,5-tetradecadienoyl-CoA isomerase
-
-
-
-
DCI1
-
-
-
-
DELTA3,5,DELTA2,4-dienoyl-CoA isomerase
-
-
DELTA3,5-DELTA2,4-dienoyl-CoA isomerase
-
DELTA3,DELTA5-t-2,t-4-dienoyl-CoA isomerase
-
-
dienoyl-CoA isomerase
-
-
enoyl-CoA hydratase
-
PATHWAY SOURCE
PATHWAYS
-
-, -
SYSTEMATIC NAME
IUBMB Comments
(3E,5Z)-alka-3,5-dienoyl-CoA DELTA3,5-DELTA2,4 isomerase
The enzyme participates in an alternative degradation route of fatty acids with cis-double bonds on odd-number carbons such as oleate and linoleate. The main physiological substrate is (3E,5Z)-tetradeca-3,5-dienoyl-CoA, but other (3E,5Z)-dienoyl-CoAs with varying carbon chain lengths are also substrates.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
3-trans,5-cis-dienoyl-CoA
2-trans,4-trans-dienoyl-CoA
show the reaction diagram
-
-
-
?
a (3E,5Z)-alka-3,5-dienoyl-CoA
a (2E,4E)-alka-2,4-dienoyl-CoA
show the reaction diagram
-
-
-
?
2-trans-4,7,10-hexadecatetraenoyl-CoA
3,5,7,10-hexadecatetraenoyl-CoA
show the reaction diagram
-
-
-
-
?
3,5,8,11,14-eicosapentaenoyl-CoA
2,4,8,11,14-eicosapentaenoyl-CoA
show the reaction diagram
-
22% and 13% activity in peroxisomes and mitochondria, respectively, compared to 3,5-octadienoyl-CoA
-
-
?
3,5-cis-octadienoyl-CoA
2,4-octadienoyl-CoA
show the reaction diagram
-
best substrate
-
-
?
3,5-cis-octadienoyl-CoA
?
show the reaction diagram
-
-
-
-
?
3,5-octadienoyl-CoA
2,4-octadienoyl-CoA
show the reaction diagram
-
100% activity in peroxisomes and mitochondria
-
-
?
3,5-tetradecadienoyl-CoA
2,4-tetradecadienoyl-CoA
show the reaction diagram
-
29% and 36% activity in peroxisomes and mitochondria, respectively, compared to 3,5-octadienoyl-CoA
-
-
?
3,5-trans-octadienoyl-CoA
2,4-octadienoyl-CoA
show the reaction diagram
-
-
-
-
?
a (3E,5Z)-alka-3,5-dienoyl-CoA
a (2E,4E)-alka-2,4-dienoyl-CoA
show the reaction diagram
DELTA3,DELTA5-decadienoyl-CoA
trans-2,trans-4-decadienoyl-CoA
show the reaction diagram
-
-
-
-
?
DELTA3,DELTA5-dienoyl-CoA
trans-2,trans-4-dienoyl-CoA
show the reaction diagram
-
-
-
-
?
DELTA3,DELTA5-dodecadienoyl-CoA
trans-2,trans-4-dodecadienoyl-CoA
show the reaction diagram
-
-
-
-
?
DELTA3,DELTA5-tetradecadienoyl-CoA
trans-2,trans-4-tetradecadienoyl-CoA
show the reaction diagram
-
-
-
-
?
additional information
?
-
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
a (3E,5Z)-alka-3,5-dienoyl-CoA
a (2E,4E)-alka-2,4-dienoyl-CoA
show the reaction diagram
-
-
-
?
a (3E,5Z)-alka-3,5-dienoyl-CoA
a (2E,4E)-alka-2,4-dienoyl-CoA
show the reaction diagram
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Nycodenz
-
-
Triton X-100
-
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0075 - 0.03
3,5-cis-octadienoyl-CoA
0.0118
3,5-trans-octadienoyl-CoA
-
at pH 8.0 and 25°C
0.0109
DELTA3,DELTA5-decadienoyl-CoA
-
at pH 8.0 and 37°C
0.0059
DELTA3,DELTA5-dodecadienoyl-CoA
-
at pH 8.0 and 37°C
0.0014
DELTA3,DELTA5-tetradecadienoyl-CoA
-
at pH 8.0 and 37°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0038
-
mutant enzyme D204N, at pH 8.0 and 25°C
0.0065
-
mutant enzyme E196Q, at pH 8.0 and 25°C
0.018
-
mutant enzyme D204A, at pH 8.0 and 25°C
0.06
with 3,5,8,11,14-eicosapentaenoyl-CoA as substrate, pH and temperature not specified in the publication
32
-
mutant enzyme E196D, at pH 8.0 and 25°C
960
-
wild type enzyme, at pH 8.0 and 25°C
98
-
mutant enzyme D176A, at pH 8.0 and 25°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 10
-
half-maximal activities at pH 5.0 and 10.0
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5
-
isoelectric focusing
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
ECH1_RAT
327
0
36172
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
126000
-
gel filtration
170000
gel filtration
200000
-
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexamer
x-ray crystallography
homohexamer
homotetramer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, using 1.75 M magnesium sulphate, 100 mM Tris-HCl, pH 8.75, 2% (w/v) ethylene glycol, 1 mM dithiothreitol, 1 mM EDTA, and 1 mM sodium azide
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D176A
-
the mutant shows 10% of wild type activity
D204A
-
the mutant shows 0.019% of wild type activity
D204N
-
the mutant shows 0.004% of wild type activity
E196D
-
the mutant shows 3.3% of wild type activity
E196Q
-
the mutant shows 0.0068% of wild type activity
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, Matrex gel red A, blue Sepharose, DEAE-cellulose, CM-cellulose, hydroxylapatite, and Sepharose CL6B column chromatographies, and gel fitration
-
DEAE-Sephacel column chromatography, Resource S column chromatography, and Superdex 200 gel filtration
hydroxylapaptite column chromatography and S-Sepharose column chromatography
-
PEG precipitation, Q Sepharo column chromatography, Sepharose CL-6B column chromatography, and hydroxylapatite column chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
expressed in Escherichia coli BL21(DE3) cells
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the enzyme expression is inducible by clofibrate treatment
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
He, X.; Shoukry, K.; Chu, S.; Yang, J.; Sprecher, H.; Schulz, H.
Peroxisomes contain DELTA3,5,DELTA2,4-dienoyl-CoA isomerase and thus possess all enzymes required for the beta-oxidation of unsaturated fatty acids by a novel reductase-dependent pathway
Biochem. Biophys. Res. Commun.
215
15-22
1995
Rattus norvegicus
Manually annotated by BRENDA team
Chen, L.; Jin, S.; Tserng, K.
Purification and mechanism of DELTA3,DELTA5-t-2,t-4-dienoyl-CoA isomerase from rat liver
Biochemistry
33
10527-10534
1994
Rattus norvegicus
Manually annotated by BRENDA team
Luo, M.; Smeland, T.; Shoukry, K.; Schulz, H.
DELTA3,5,DELTA2,4-dienoyl-CoA isomerase from rat liver mitochondria purification and characterization of a new enzyme involved in the beta-oxidation of unsaturated fatty acids
J. Biol. Chem.
269
2384-2388
1994
Rattus norvegicus
Manually annotated by BRENDA team
Luthria, D.; Baykousheva, S.; Sprecher, H.
Double bond removal from odd-numbered carbons during peroxisomal beta-oxidation of arachidonic acid requires both 2,4-dienoyl-CoA reductase and DELTA3,5,DELTA2,4-dienoyl-CoA isomerase
J. Biol. Chem.
270
13771-13776
1995
Rattus norvegicus
Manually annotated by BRENDA team
Filppula, S.A.; Yagi, A.I.; Kilpelaeinen, S.H.; Novikov, D.; FitzPatrick, D.R.; Vihinen, M.; Valle, D.; Hiltunen, J.K.
DELTA3,5-DELTA2,4-dienoyl-CoA isomerase from rat liver. Molecular characterization
J. Biol. Chem.
273
349-355
1998
Rattus norvegicus (P14604)
Manually annotated by BRENDA team
Zhang, D.; Liang, X.; He, X.; Alipui, O.; Yang, S.; Schulz, H.
DELTA3,5,DELTA2,4-dienoyl-CoA isomerase is a multifunctional isomerase. A structural and mechanistic study
J. Biol. Chem.
276
13622-13627
2001
Rattus norvegicus
Manually annotated by BRENDA team
Modis, Y.; Filppula, S.; Novikov, D.; Norledge, B.; Kalervo Hiltunen, J.; Wierenga, R.
The crystal structure of dienoyl-CoA isomerase at 1.5 A resolution reveals the importance of aspartate and glutamate sidechains for catalysis
Structure
6
957-970
1998
Rattus norvegicus (Q62651)
Manually annotated by BRENDA team