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Information on EC 5.3.3.21 - DELTA3,5-DELTA2,4-dienoyl-CoA isomerase
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EC Tree
5.3.3.21 DELTA3,5-DELTA2,4-dienoyl-CoA isomeraseIUBMB 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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Word Map
- 5.3.3.21
- peroxisomal
-
beta-oxidation
-
oleic
- unsaturated
-
hydratase
- oleate
-
thioesterase
-
delta3,delta2-enoyl-coa
-
palmitic
The enzyme appears in viruses and cellular organisms
Synonyms
yor180c, dienoyl-coa isomerase, delta3,5-delta2,4-dienoyl-coa isomerase, delta3,5,delta2,4-dienoyl-coa isomerase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
3,5-tetradecadienoyl-CoA isomerase
-
-
-
-
DCI1
DELTA3,5,DELTA2,4-dienoyl-CoA isomerase
DELTA3,5-DELTA2,4-dienoyl-CoA isomerase
dienoyl-CoA isomerase
YOR180c
DCI1
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
a (3E,5Z)-alka-3,5-dienoyl-CoA = a (2E,4E)-alka-2,4-dienoyl-CoA
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
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,
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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.
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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
2-trans-4,7,10-hexadecatetraenoyl-CoA
3,5,7,10-hexadecatetraenoyl-CoA
-
-
-
-
?
3,5,8,11,14-eicosapentaenoyl-CoA
2,4,8,11,14-eicosapentaenoyl-CoA
-
22% and 13% activity in peroxisomes and mitochondria, respectively, compared to 3,5-octadienoyl-CoA
-
-
?
3,5-octadienoyl-CoA
2,4-octadienoyl-CoA
-
100% activity in peroxisomes and mitochondria
-
-
?
3,5-tetradecadienoyl-CoA
2,4-tetradecadienoyl-CoA
-
29% and 36% activity in peroxisomes and mitochondria, respectively, compared to 3,5-octadienoyl-CoA
-
-
?
DELTA3,DELTA5-dodecadienoyl-CoA
trans-2,trans-4-dodecadienoyl-CoA
-
-
-
-
?
DELTA3,DELTA5-tetradecadienoyl-CoA
trans-2,trans-4-tetradecadienoyl-CoA
-
-
-
-
?
3,5,8,11,14-eicosapentenoyl-CoA
2,4,8,11,14-eicosapentenoyl-CoA
-
-
-
-
?
3,5,8,11,14-eicosapentenoyl-CoA
2,4,8,11,14-eicosapentenoyl-CoA
-
-
-
-
?
3,5,8,11,14-eicosapentenoyl-CoA
2,4,8,11,14-eicosapentenoyl-CoA
-
-
-
-
?
a (3E,5Z)-alka-3,5-dienoyl-CoA
a (2E,4E)-alka-2,4-dienoyl-CoA
-
-
-
-
?
a (3E,5Z)-alka-3,5-dienoyl-CoA
a (2E,4E)-alka-2,4-dienoyl-CoA
-
-
-
?
a (3E,5Z)-alka-3,5-dienoyl-CoA
a (2E,4E)-alka-2,4-dienoyl-CoA
-
-
-
?
a (3E,5Z)-alka-3,5-dienoyl-CoA
a (2E,4E)-alka-2,4-dienoyl-CoA
-
-
-
-
?
a (3E,5Z)-alka-3,5-dienoyl-CoA
a (2E,4E)-alka-2,4-dienoyl-CoA
-
-
-
-
?
additional information
?
-
-
no activity with 2-trans-5-trans-octadienoyl-CoA
-
-
?
additional information
?
-
the enzyme also has a low 2-enoyl-CoA hydratase 1 (crotonase) activity, generating L-3-hydroxydecanoyl-CoA from trans-2-decenoyl-CoA. The enzyme has no activity with trans-3-decenoyl-CoA
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-
?
additional information
?
-
-
the recombinant enzyme also exhibits DELTA3,5,7,DELTA2,4,6-trienoyl-CoA isomerase activity
-
-
?
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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
a (3E,5Z)-alka-3,5-dienoyl-CoA
a (2E,4E)-alka-2,4-dienoyl-CoA
-
-
-
-
?
a (3E,5Z)-alka-3,5-dienoyl-CoA
a (2E,4E)-alka-2,4-dienoyl-CoA
-
-
-
?
a (3E,5Z)-alka-3,5-dienoyl-CoA
a (2E,4E)-alka-2,4-dienoyl-CoA
-
-
-
?
a (3E,5Z)-alka-3,5-dienoyl-CoA
a (2E,4E)-alka-2,4-dienoyl-CoA
-
-
-
-
?
a (3E,5Z)-alka-3,5-dienoyl-CoA
a (2E,4E)-alka-2,4-dienoyl-CoA
-
-
-
-
?
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.06
with 3,5,8,11,14-eicosapentaenoyl-CoA as substrate, pH and temperature not specified in the publication
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
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
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). DCI1_ARATH
278
0
29920
Swiss-Prot
other Location (Reliability: 2)
A0A7R8D1X4_LEPSM
297
0
33142
TrEMBL
Mitochondrion (Reliability: 2)
A0A6J8CJF6_MYTCO
305
0
34013
TrEMBL
Mitochondrion (Reliability: 5)
A0A812D9L0_SEPPH
303
0
33502
TrEMBL
Mitochondrion (Reliability: 4)
ECHM_RAT
290
0
31516
Swiss-Prot
Secretory Pathway (Reliability: 3)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homohexamer
homotetramer
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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
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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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
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DEAE-Sephacel column chromatography, Resource S column chromatography, and Superdex 200 gel filtration
hydroxylapaptite column chromatography and S-Sepharose column chromatography
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PEG precipitation, Q Sepharo column chromatography, Sepharose CL-6B column chromatography, and hydroxylapatite column chromatography
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
enzyme expression is oleic acid-inducible
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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
brenda
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
brenda
Kovalyov, L.; Kovalyova, M.; Kovalyov, P.; Serebryakova, M.; Moshkovskii, S.; Shishkin, S.
Polymorphism of DELTA3,5-DELTA2,4-dienoyl-coenzyme A isomerase (the ECH1 gene product protein) in human striated muscle tissue
Biochemistry
71
448-453
2006
Homo sapiens
brenda
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
brenda
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
brenda
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)
brenda
Gurvitz, A.; Mursula, A.; Yagi, A.; Hartig, A.; Ruis, H.; Rottensteiner, H.; Hiltunen, J.
Alternatives to the isomerase-dependent pathway for the beta-oxidation of oleic acid are dispensable in Saccharomyces cerevisiae. Identification of YOR180c/DCI1 encoding peroxisomal DELTA3,5-DELTA2,4-dienoyl-CoA isomerase
J. Biol. Chem.
274
24514-24521
1999
Saccharomyces cerevisiae, Saccharomyces cerevisiae BJ1991
brenda
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
brenda
Goepfert, S.; Vidoudez, C.; Rezzonico, E.; Hiltunen, J.; Poirier, Y.
Molecular identification and characterization of the Arabidopsis DELTA3,5, DELTA2,4-dienoyl-coenzyme A isomerase, a peroxisomal enzyme participating in the beta-oxidation cycle of unsaturated fatty acids
Plant Physiol.
138
1947-1956
2005
Arabidopsis thaliana
brenda
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)
brenda
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