Any feedback?
Information on EC 5.3.3.8 - DELTA3-DELTA2-enoyl-CoA isomerase and Organism(s) Rattus norvegicus and UniProt Accession P23965
for references in articles please use BRENDA:EC5.3.3.8Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
5.3.3.8 DELTA3-DELTA2-enoyl-CoA isomeraseIUBMB Comments
The enzyme participates in the beta-oxidation of fatty acids with double bonds at an odd position. Processing of these substrates via the beta-oxidation system results in intermediates with a cis- or trans-double bond at position C3, which cannot be processed further by the regular enzymes of the beta-oxidation system. This enzyme isomerizes the bond to a trans bond at position C2, which can be processed further. The reaction rate is ten times higher for the (3Z) isomers than for (3E) isomers. The enzyme can also catalyse the isomerization of 3-acetylenic fatty acyl thioesters to 2,3-dienoyl fatty acyl thioesters.
Specify your search results
Word Map
- 5.3.3.8
-
beta-oxidation
- peroxisomal
- unsaturated
-
hydratase
-
auxiliary
-
2,4-dienoyl-coa
-
isomerization
-
oleic
-
odd-numbered
- 3-ketoacyl-coa
- crotonase
-
trifunctional
-
thiolase
-
protic
- d-3-hydroxyacyl-coa
-
4.2.1.17
-
1.3.1.34
- medicine
The taxonomic range for the selected organisms is: Rattus norvegicus
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Synonyms
eci1p, delta3,delta2-enoyl-coa isomerase, 3,2-trans-enoyl-coa isomerase, ateci3, ateci2, delta3-delta2-enoyl-coa isomerase, 3-cis-2-trans-enoyl-coa isomerase, 2,3-enoyl-coa isomerase, 3-2trans-enoyl-coa isomerase, d3,d2-enoyl-coa isomerase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
2,3-Enoyl-CoA isomerase
-
-
-
-
3,2-trans-Enoyl-CoA isomerase
-
-
-
-
3-2trans-Enoyl-CoA isomerase
-
-
-
-
3-cis-2-trans-Enoyl-CoA isomerase
-
-
-
-
Acetylene-allene isomerase
-
-
-
-
D3,D2-enoyl-CoA isomerase
-
-
-
-
DELTA3,DELTA2-enoyl-CoA isomerase
DELTA3-cis,DELTA2-trans-Enoyl-CoA isomerase
-
-
-
-
DELTA3-cis-DELTA2-trans-enoyl-CoA isomerase
-
-
-
-
Dodecenoyl-CoA delta-isomerase
-
-
-
-
dodecenoyl-CoA DELTA3-cis-DELTA2-trans-isomerase
-
-
-
-
ECI
Hepatocellular carcinoma-associated antigen 88
-
-
-
-
Isomerase, dodecenoyl coenzyme A Delta-
-
-
-
-
Long-chain DELTA3,DELTA2-enoyl-CoA isomerase
-
-
-
-
Short chain DELTA3,DELTA2-enoyl-CoA isomerase
-
-
-
-
DELTA3,DELTA2-enoyl-CoA isomerase
-
-
-
-
ECI
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
isomerization
-
-
-
-
intramolecular oxidoreduction
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
-
-, -, -, -, -, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
(3Z/3E)-alk-3-enoyl-CoA (2E)-isomerase
The enzyme participates in the beta-oxidation of fatty acids with double bonds at an odd position. Processing of these substrates via the beta-oxidation system results in intermediates with a cis- or trans-double bond at position C3, which cannot be processed further by the regular enzymes of the beta-oxidation system. This enzyme isomerizes the bond to a trans bond at position C2, which can be processed further. The reaction rate is ten times higher for the (3Z) isomers than for (3E) isomers. The enzyme can also catalyse the isomerization of 3-acetylenic fatty acyl thioesters to 2,3-dienoyl fatty acyl thioesters.
CAS REGISTRY NUMBER
COMMENTARY
62213-29-0
-
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,5-cis-tetradecadienoyl-CoA
3-cis,5-cis-tetradecadienoyl-CoA
-
-
-
?
trans-2-hexenoyl-CoA + H2O
3-hydroxyhexanoyl-CoA
K242C mutation allows Delta3-Delta2-enoyl-CoA isomerase to acquire enoyl-CoA hydratase activity
-
-
?
additional information
?
-
the enzyme is involved in beta-oxidation of unsaturated fatty acids
-
?
additional information
?
-
-
in addition to the peroxisomal trifunctional enzyme and the mitochondrial enzyme which shows a preference for short-chain substrates, a separate isomerase with a preference for C10-C12 substrates is observed
-
-
?
additional information
?
-
-
no specificity for DELTA3-cis-enoyl-CoA esters of chain length between C6 and C16
-
-
?
additional information
?
-
-
MECI is most active in catalyzing the 3-cis/2-trans isomerization, ECI has a preference for the 3-trans/2-trans isomerization, and MFE1 is the optimal isomerase for the 2,5-/3,5-isomerization. 3-cis/2-trans and 2,5/3,5 isomerization in mitochondria are catalyzed overwhelmingly by MECI, whereas ECI contributes significantly to the 3-trans/2-trans isomerization. In peroxisomes, ECI is predicted to be the dominant enzyme for the 3-cis/2-trans and 3-trans/2-trans isomerization of long chain intermediates
-
?
additional information
?
-
-
key enzyme in mitochondrial beta-oxidation of unsaturated fatty acids
-
-
?
additional information
?
-
-
enzyme is responsible for the positional and geometric isomerization of beta,gamma-unsaturated fatty acyl-CoA intermediates arising during beta-oxidation of unsaturated long-chain fatty acids
-
-
?
additional information
?
-
-
mitochondrial enzyme is markedly induced by peroxisome proliferators, di-(2-ethylhexyl)phthalate and clofibrate
-
-
?
additional information
?
-
-
enzyme is important for the degradation of unsaturated fatty acids in the beta-oxidation system
-
-
?
additional information
?
-
-
enzyme is important for the degradation of unsaturated fatty acids in the beta-oxidation system
-
-
?
additional information
?
-
-
key enzyme in the degradation of unsaturated fatty acids
-
-
?
additional information
?
-
-
involved in the enzymatic degradation of the cis-olefinic system of monounsaturated and polyunsaturated fatty acids
-
-
?
additional information
?
-
-
auxiliary enzyme that is essential for the operation of the major pathway of oleate beta-oxidation
-
?
additional information
?
-
-
key enzyme for the beta-oxidation of unsaturated fatty acids
-
?
additional information
?
-
-
one of the key enzymes involved in fatty acid oxidation
-
-
?
additional information
?
-
one of the key enzymes involved in fatty acid oxidation
-
-
?
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
additional information
?
-
the enzyme is involved in beta-oxidation of unsaturated fatty acids
-
?
additional information
?
-
-
key enzyme in mitochondrial beta-oxidation of unsaturated fatty acids
-
-
?
additional information
?
-
-
enzyme is responsible for the positional and geometric isomerization of beta,gamma-unsaturated fatty acyl-CoA intermediates arising during beta-oxidation of unsaturated long-chain fatty acids
-
-
?
additional information
?
-
-
mitochondrial enzyme is markedly induced by peroxisome proliferators, di-(2-ethylhexyl)phthalate and clofibrate
-
-
?
additional information
?
-
-
enzyme is important for the degradation of unsaturated fatty acids in the beta-oxidation system
-
-
?
additional information
?
-
-
enzyme is important for the degradation of unsaturated fatty acids in the beta-oxidation system
-
-
?
additional information
?
-
-
key enzyme in the degradation of unsaturated fatty acids
-
-
?
additional information
?
-
-
involved in the enzymatic degradation of the cis-olefinic system of monounsaturated and polyunsaturated fatty acids
-
-
?
additional information
?
-
-
auxiliary enzyme that is essential for the operation of the major pathway of oleate beta-oxidation
-
?
additional information
?
-
-
key enzyme for the beta-oxidation of unsaturated fatty acids
-
?
additional information
?
-
-
one of the key enzymes involved in fatty acid oxidation
-
-
?
additional information
?
-
one of the key enzymes involved in fatty acid oxidation
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00062
trans-2-hexenoyl-CoA
pH 8, hydratase activity, mutant enzyme K242T
0.0026
trans-2-hexenoyl-CoA
pH 8, hydratase activity, mutant enzyme K242D
0.31
trans-2-hexenoyl-CoA
pH 8, hydratase activity, mutant enzyme K242C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.013
trans-2-hexenoyl-CoA
pH 8, hydratase activity, mutant enzyme K242D
0.021
trans-2-hexenoyl-CoA
pH 8, hydratase activity, mutant enzyme K242T
1
trans-2-hexenoyl-CoA
pH 8, hydratase activity, mutant enzyme K242C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
-
-
at least three isoenzymes: 1. mitochondrial short-chain isomerase, 2. mitochondrial long-chain preferring isomerase, 3. peroxisomal isoenzyme, which is part of a multifunctional protein
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
-
-
in addition to the peroxisomal trifunctional enzyme and the mitochondrial enzyme which shows a preference for short-chain substrates, a separate isomerase with a preference for C10-C12 substrates is observed
-
enzyme is synthesized with a N-terminal mitochondrial targeting sequence which is cleaved during mitochondrial import
-
in addition to the peroxisomal trifunctional enzyme and the mitochondrial enzyme which shows a preference for short-chain substrates, a separate isomerase with a preference for C10-C12 substrates is observed
-
trifunctional enzyme which exhibits the activities of EC5.3.3.8, EC 4.2.1.17 and EC 1.1.1.35
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). ECI1_RAT
289
0
32254
Swiss-Prot
Mitochondrion (Reliability: 1)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
29256
-
x * 29256, calculation from nucleotide sequence of cDNA, the subunit is synthesized with an amino-terminal extrasequence of 35 amino acid residues and processed to the mature enzyme with MW 29256
29300
30000
78000
-
1 * 78000, trifunctional enzyme which exhibits the activities of EC 5.3.3.8, EC 4.2.1.17 and EC 1.1.1.35, SDS-PAGE
78511
-
1 * 78511, peroxisomal isoenzyme, which is a part of a multifunctional protein
83000
-
trifunctional enzyme which exhibits the activities of EC 5.3.3.8, EC 4.2.1.17 and EC 1.1.1.35, gel filtration
29300
-
x * 29300, short chain preferring DELTA3,DELTA2-enoyl-CoA isomerase, calculation from cDNA-derived nucleotide sequence
30000
-
2 * 30000, SDS-PAGE, enzyme has a strong tendency to form a dimer, monomeric form is also active
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
monomer
?
-
x * 29256, calculation from nucleotide sequence of cDNA, the subunit is synthesized with an amino-terminal extrasequence of 35 amino acid residues and processed to the mature enzyme with MW 29256
?
-
x * 29300, short chain preferring DELTA3,DELTA2-enoyl-CoA isomerase, calculation from cDNA-derived nucleotide sequence
dimer
-
2 * 30000, SDS-PAGE, enzyme has a strong tendency to form a dimer, monomeric form is also active
monomer
-
1 * 78000, trifunctional enzyme which exhibits the activities of EC 5.3.3.8, EC 4.2.1.17 and EC 1.1.1.35, SDS-PAGE
monomer
-
1 * 78511, peroxisomal isoenzyme, which is a part of a multifunctional protein
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
K242C
decrease in catalytic activity, mutants shows additional hydratase activity on 2-hexenoyl-CoA with Vmax of 1.9 micromol per min and mg
K242D
decrease in catalytic activity, mutants shows slight additional hydratase activity on 2-hexenoyl-CoA with Vmax of 0.026 micromol per min and mg
K242T
decrease in catalytic activity, mutants shows additional hydratase activity on 2-hexenoyl-CoA with Vmax of 0.041 micromol per min and mg
D149E
turnover number for trans-3-hexenoyl-CoA is 2.3fold lower than wild-type value, Km-value for trans-3-hexenoyl-CoA is fold higher than wild-type enzyme
E151X
-
site-directe mutagenesis of putative active-site amino acid residues. Exchange of Arg151 and Asp211 leads to a reduced expression of the recombinant enzyme accompanied by a reduced activity. The replacement of Glu165 by Gln leads to a strongly reduced enzymatic activity. Tyr150 is not involved in isomerase catalysis
E165Q
-
site-directe mutagenesis of putative active-site amino acid residues. Exchange of Arg151 and Asp211 leads to a reduced expression of the recombinant enzyme accompanied by a reduced activity. The replacement of Glu165 by Gln leads to a strongly reduced enzymatic activity. Tyr150 is not involved in isomerase catalysis
K242C
K242D
K242F
turnover number for trans-3-hexenoyl-CoA is 1143fold lower than wild-type value, Km-value for trans-3-hexenoyl-CoA is fold higher than wild-type enzyme
K242R
turnover number for trans-3-hexenoyl-CoA is 3.2fold lower than wild-type value, Km-value for trans-3-hexenoyl-CoA is fold higher than wild-type enzyme
K242T
N211X
-
site-directe mutagenesis of putative active-site amino acid residues. Exchange of Arg151 and Asp211 leads to a reduced expression of the recombinant enzyme accompanied by a reduced activity. The replacement of Glu165 by Gln leads to a strongly reduced enzymatic activity. Tyr150 is not involved in isomerase catalysis
K242C
turnover number for trans-3-hexenoyl-CoA is 14.5fold lower than wild-type value, Km-value for trans-3-hexenoyl-CoA is fold higher than wild-type enzyme
K242C
turnover number for trans-3-hexenoyl-CoA is 160 fold lower than wild-type value, Km-value for trans-3-hexenoyl-CoA is fold higher than wild-type enzyme. Mutation allows DELTA3-DELTA2-enoyl-CoA isomerase to acquire enoyl-CoA hydratase activity
K242D
turnover number for trans-3-hexenoyl-CoA is 12308fold lower than wild-type value, Km-value for trans-3-hexenoyl-CoA is fold higher than wild-type enzyme
K242D
turnover number for trans-3-hexenoyl-CoA is 2667fold lower than wild-type value, Km-value for trans-3-hexenoyl-CoA is fold higher than wild-type enzyme
K242T
turnover number for trans-3-hexenoyl-CoA is 7619fold lower than wild-type value, Km-value for trans-3-hexenoyl-CoA is fold higher than wild-type enzyme
K242T
turnover number for trans-3-hexenoyl-CoA is 842fold lower than wild-type value, Km-value for trans-3-hexenoyl-CoA is fold higher than wild-type enzyme
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
trifunctional enzyme which exhibits the activities of EC 5.3.3.8, EC 4.2.1.17 and EC 1.1.1.35
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
diets enriched with safflower oil as a source high in linoleic acid induce markedly increased hepatic enzyme activities
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Yokota, S.; Tomioka, Y.; Suzuki, H.; Mizugaki, M.
Immunocytochemical localization of DELTA3,DELTA2-enoyl-CoA isomerase and NADPH-dependent-2,4-dienoyl-CoA reductase in rat kidney
Histochemistry
99
463-469
1993
Rattus norvegicus
Stoffel, W.; Ecker, W.
DELTA3-cis,DELTA2-trans-Enoyl-CoA isomerase from rat liver mitochondria
Methods Enzymol.
14
99-105
1979
Rattus norvegicus
-
Stoffel, W.; Grol, M.
Purification and properties of 3-cis-2-trans-enoyl-CoA isomerase (dodecenyl-CoA DELTA-isomerase) from rat liver mitochondria
Hoppe-Seyler's Z. Physiol. Chem.
359
1777-1782
1978
Rattus norvegicus
Lawson, L.D.; Holman, R.T.
beta-Oxidation of the geometric and positional isomers of octadecenoic acid by rat heart and liver mitochondria
Biochim. Biophys. Acta
665
60-65
1981
Rattus norvegicus
Krki,T.; Hakkola, E.; Hassinen, I.E.; Hiltunen, J.K.
beta-Oxidation of polyunsaturated fatty acids in peroxisomes. Subcellular distribution of delta3,delta2-enoyl-CoA isomerase activity in rat liver
FEBS Lett.
215
228-232
1987
Rattus norvegicus
Tomioka, Y.; Aihara, K.; Hirose, A.; Hishinuma, T.; Mizugaki, M.
Detection of heat-stable DELTA3,DELTA2-enoyl-CoA isomerase in rat liver mitochondria and peroxisomes by immunochemical study using specific antibody
J. Biochem.
109
394-398
1991
Rattus norvegicus
Muller-Newen, G.; Stoffel, W.
Mitochondrial 3-2trans-enoyl-CoA isomerase. Purification, cloning, expression, and mitochondrial import of the key enzyme of unsaturated fatty acid beta-oxidation
Biol. Chem. Hoppe-Seyler
372
613-624
1991
Rattus norvegicus
Tomioka, Y.; Hirose, A.; Moritani, H.; Hishinuma, T.; Hashimoto, T.; Mizugaki, M.
cDNA cloning of mitochondrial delta3,delta2-enoyl-CoA isomerase of rat liver
Biochim. Biophys. Acta
1130
109-112
1992
Rattus norvegicus
Palossari, P.M.; Kilponen, J.M.; Sormunen, R.T.; Hassinen, I.E.; Hiltunen, J.K.
DELTA3,DELTA2-Enoyl-CoA isomerases. Characterization of the mitochondrial isoenzyme in the rat
J. Biol. Chem.
265
3347-3353
1990
Bos taurus, Homo sapiens, Rattus norvegicus, Sus scrofa
Palossari, P.M.; Hiltunen, J.K.
Peroxisomal bifunctional protein from rat liver is a trifunctional enzyme possessing 2-enoyl-CoA hydratase, 3-hydroxyacyl-CoA dehydrogenase, and DELTA3,DELTA2-enoyl-CoA isomerase activities
J. Biol. Chem.
265
2446-2449
1990
Rattus norvegicus
Kilponen, J.M.; Palosaari, P.M.; Hiltunen, J.K.
Occurence of a long-chain DELTA3,DELTA2-enoyl-CoA isomerase in rat liver
Biochem. J.
269
223-226
1990
Rattus norvegicus
Zeelen, J.P.; Pauptit, R.A.; Wierenga, R.A.; Kunau, W.H.; Hiltunen, J.K.
Crystallization and preliminary X-ray diffraction studies of mitochondrial short-chain delta3,delta2-enoyl-CoA isomerase from rat liver
J. Mol. Biol.
224
273-275
1992
Rattus norvegicus
Palossari, P.M.; Vihinen, M.; Mntsl.P.I.; Alexson, S.E.H.; Pihlajaniemi, T.; Hiltunen, J.K.
Amino acid sequence similarities of the mitochondrial short chain DELTA3,DELTA2-enoyl-CoA isomerase and peroxisomal multifunctional DELTA3,DELTA2-enoyl-CoA isomerase, 2-enoyl-CoA hydratase, 3-hydroxyacyl-CoA dehydrogenase enzyme in rat liver. The proposed occurence of isomerization and hydratation in the same catalytic domain of the multifunctional enzyme
J. Biol. Chem.
266
10750-10753
1991
Rattus norvegicus
Yokota, S.; Hirose, A.; Mizugaki, M.
Immunocytochemical localization of DELTA3,DELTA2-enoyl-CoA isomerase in rat liver. The effects of di-(2-ethylhexyl)phthalate, a peroxisome proliferator
Biol. Cell.
66
327-334
1989
Rattus norvegicus
Kilponen, J.M.; Palosaari, P.M.; Sormunen, R.T.; Vihinen, M.; Hiltunen, J.K.
Isoenzymes of DELTA3,DELTA2-enoyl-CoA isomerase in rat liver
Prog. Clin. Biol. Res.
375
33-40
1992
Rattus norvegicus
Muller-Newen, G.; Stoffel, W.
Site-directed mutagenesis of putative active-site amino acid residues of 3,2-trans-enoyl-CoA isomerase, conserved within the low-homology isomerase/hydratase enzyme family
Biochemistry
32
11405-11412
1993
Rattus norvegicus
Gurvitz, A.; Wabnegger, L.; Yagi, A.I.; Binder, M.; Hartig, A.; Ruis, H.; Hamilton, B.; Dawes, I.W.; Hiltunen, J.K.; Rottensteiner, H.
Function of human mitochondrial 2,4-dienoyl-CoA reductase and rat monofunctional DELTA3-DELTA2-enoyl-CoA isomerase in beta-oxidation of unsaturated fatty acids
Biochem. J.
344
903-914
1999
Rattus norvegicus (P23965)
-
Zhang, D.; Yu, W.; Geisbrecht, B.V.; Gould, S.J.; Sprecher, H.; Schulz, H.
Functional characterization of DELTA3,DELTA2-enoyl-CoA isomerases from rat liver
J. Biol. Chem.
277
9127-9132
2002
Rattus norvegicus
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
Li, D.; Wong, C.K.; Yu, W.H.; Li, P.
Cloning, expression, and purification of the functional DELTA3-DELTA2-enoyl-CoA isomerase fusion protein
Protein Expr. Purif.
26
35-41
2002
Rattus norvegicus
Yu, W.; Chu, X.; Deng, G.; Liu, X.; Chen, G.; Li, D.
Mutation of Lys242 allows DELTA3-DELTA2-enoyl-CoA isomerase to acquire enoyl-CoA hydratase activity
Biochim. Biophys. Acta
1760
1874-1883
2006
Rattus norvegicus, Rattus norvegicus (P23965)
Justus, J.; Weigand, E.
The effect of a moderate zinc deficiency and dietary fat source on the activity and expression of the DELTA3DELTA2-enoyl-CoA isomerase in the liver of growing rats
Biol. Trace Elem. Res.
158
365-375
2014
Rattus norvegicus
Van Weeghel, M.; Ofman, R.; Argmann, C.; Ruiter, J.; Claessen, N.; Oussoren, S.; Wanders, R.; Aten, J.; Houten, S.
Identification and characterization of Eci3, a murine kidney-specific DELTA3,DELTA2-enoyl-CoA isomerase
FASEB J.
28
1365-1374
2014
Rattus norvegicus, Mus musculus (Q78JN3)
EXTERNAL LINKS (specific for EC-Number 5.3.3.8)
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
