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Information on EC 5.3.3.8 - DELTA3-DELTA2-enoyl-CoA isomerase and Organism(s) Saccharomyces cerevisiae and UniProt Accession Q05871
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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.
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Word Map
- 5.3.3.8
-
beta-oxidation
- peroxisomal
- unsaturated
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hydratase
-
auxiliary
-
2,4-dienoyl-coa
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isomerization
-
oleic
-
odd-numbered
- 3-ketoacyl-coa
- crotonase
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trifunctional
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thiolase
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protic
- d-3-hydroxyacyl-coa
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4.2.1.17
-
1.3.1.34
- medicine
The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
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, ateci1, 3-cis-2-trans-enoyl-coa isomerase, 2,3-enoyl-coa isomerase, 3-2trans-enoyl-coa isomerase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
2,3-Enoyl-CoA isomerase
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-
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3,2-trans-Enoyl-CoA isomerase
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-
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3-2trans-Enoyl-CoA isomerase
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-
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3-cis-2-trans-Enoyl-CoA isomerase
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-
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Acetylene-allene isomerase
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D3,D2-enoyl-CoA isomerase
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DELTA3,DELTA2-enoyl-CoA isomerase
DELTA3-cis,DELTA2-trans-Enoyl-CoA isomerase
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DELTA3-cis-DELTA2-trans-enoyl-CoA isomerase
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Dodecenoyl-CoA delta-isomerase
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dodecenoyl-CoA DELTA3-cis-DELTA2-trans-isomerase
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ECI
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Hepatocellular carcinoma-associated antigen 88
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Isomerase, dodecenoyl coenzyme A Delta-
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Long-chain DELTA3,DELTA2-enoyl-CoA isomerase
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Short chain DELTA3,DELTA2-enoyl-CoA isomerase
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DELTA3,DELTA2-enoyl-CoA isomerase
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
isomerization
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-
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intramolecular oxidoreduction
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-
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PATHWAY SOURCE
PATHWAYS
BRENDA
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-, -, -, -, -, -, -, -, -, -, -
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
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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
additional information
?
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the enzyme is essential for the beta-oxidation of unsaturated fatty acids
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?
additional information
?
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the enzyme is essential for the beta-oxidation of unsaturated fatty acids
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?
additional information
?
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only one catalytic base, Glu158, is involved in shuttling the proton from the C2 carbon atom of the substrate, DELTA3-enol-CoA, to the C4 atom of the product DELTA2-enoyl-CoA
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?
additional information
?
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auxiliary enzyme required for beta-oxidation of unsaturated fatty acids
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?
additional information
?
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main pathway for 9-cis,11-trans-octadecadienoic acid degradation requires the participation of DELTA3,DELTA2-enoyl-CoA isomerase
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-
?
additional information
?
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the synthesis of polyhydroxyalkanoate in cells grown in media containing 10-cis-heptadecenoic acid is dependent on the presence of DELTA3,DELTA2-enoyl-CoA isomerase activity. Degradation of 10-trans-heptadecenoic acid through beta-oxidation is severly reduced in mutants devoid of DELTA3,DELTA2-enoyl-CoA isomerase. The synthesis of the intermediate 3-trans-enoyl-CoA in the absence of the DELTA3,DELTA2-enoyl-CoA isomerase leads to the blockage of the direct multifunctional enzyme dependent pathway in vivo
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?
additional information
?
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the peroxisomal protein Yor180Cp associates with the enzyme in vivo
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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
additional information
?
-
the enzyme is essential for the beta-oxidation of unsaturated fatty acids
-
?
additional information
?
-
-
the enzyme is essential for the beta-oxidation of unsaturated fatty acids
-
?
additional information
?
-
-
auxiliary enzyme required for beta-oxidation of unsaturated fatty acids
-
?
additional information
?
-
-
main pathway for 9-cis,11-trans-octadecadienoic acid degradation requires the participation of DELTA3,DELTA2-enoyl-CoA isomerase
-
-
?
additional information
?
-
-
the synthesis of polyhydroxyalkanoate in cells grown in media containing 10-cis-heptadecenoic acid is dependent on the presence of DELTA3,DELTA2-enoyl-CoA isomerase activity. Degradation of 10-trans-heptadecenoic acid through beta-oxidation is severly reduced in mutants devoid of DELTA3,DELTA2-enoyl-CoA isomerase. The synthesis of the intermediate 3-trans-enoyl-CoA in the absence of the DELTA3,DELTA2-enoyl-CoA isomerase leads to the blockage of the direct multifunctional enzyme dependent pathway in vivo
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-
?
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.05
3-trans-decenoyl-CoA
wild type enzyme, at pH 8.5 and 25°C
0.072
3-trans-hexenoyl-CoA
wild type enzyme, at pH 8.5 and 25°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
4.4
3-trans-decenoyl-CoA
wild type enzyme, at pH 8.5 and 25°C
1.7
3-trans-hexenoyl-CoA
wild type enzyme, at pH 8.5 and 25°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
90000
3-trans-decenoyl-CoA
wild type enzyme, at pH 8.5 and 25°C
20000
3-trans-hexenoyl-CoA
wild type enzyme, at pH 8.5 and 25°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.26
mutant enzyme F268A, with 3-trans-hexenoyl-CoA as substrate, at pH 8.5 and 25°C
0.35
mutant enzyme F268A, with 3-trans-decenoyl-CoA as substrate, at pH 8.5 and 25°C
0.4
mutant enzyme R100A, with 3-trans-decenoyl-CoA as substrate, at pH 8.5 and 25°C
0.5
mutant enzyme N101A, with 3-trans-hexenoyl-CoA as substrate, at pH 8.5 and 25°C
0.62
mutant enzyme N101A, with 3-trans-decenoyl-CoA as substrate, at pH 8.5 and 25°C
0.93
mutant enzyme R100A, with 3-trans-hexenoyl-CoA as substrate, at pH 8.5 and 25°C
1.93
wild type enzyme, with 3-trans-hexenoyl-CoA as substrate, at pH 8.5 and 25°C
4.4
wild type enzyme, with 3-trans-decenoyl-CoA as substrate, at pH 8.5 and 25°C
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
enzyme in the presence of 5 mM acetoacetyl-CoA or 1.8 mM octanoyl-CoA, sitting drop vapor diffusion method, using 100 mM MES pH 6.5, 1.6 M (NH4)2SO4, 10% (w/v) dioxane
hanging drop vapor diffusion method, 2.1 A structure of a tight hexameric crystal form of the enzyme
vapor diffusion method, unit-cell parameters a = 116.0, b = 116.0, c = 122.9 A, crystals likely have P6322 symmetry
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
F268A
the mutant shows reduced activity compared to the wild type enzyme
N101A
the mutant shows reduced activity compared to the wild type enzyme
R100A
the mutant shows reduced activity compared to the wild type enzyme
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Mursula, A.M.; van Aalten, D.M.; Modis, Y.; Hiltunen, J.K.; Wierenga, R.K.
Crystallization and X-ray diffraction analysis of peroxisomal DELTA3-DELTA2-enoyl-CoA isomerase from Saccharomyces cerevisiae
Acta Crystallogr. Sect. D
56
1020-1023
2000
Saccharomyces cerevisiae
-
Mursula, A.M.; Hiltunen, J.K.; Wierenga, R.K.
Structural studies on DELTA3-DELTA2-enoyl-CoA isomerase: the variable mode of assembly of the trimeric disks of the crotonase superfamily
FEBS Lett.
557
81-87
2004
Saccharomyces cerevisiae (Q05871), Saccharomyces cerevisiae
Geisbrecht, B.V.; Zhu, D.; Schulz, K.; Nau, K.; Morrell, J.C.; Geraghty, M.; Schulz, H.; Erdmann, R.; Gould, S.J.
Molecular characterization of Saccharomyces cerevisiae DELTA3, DELTA2-enoyl-CoA isomerase
J. Biol. Chem.
273
33184-33191
1998
Saccharomyces cerevisiae (Q05871), Saccharomyces cerevisiae
Mursula, A.M.; van Aalten, D.M.; Hiltunen, J.K.; Wierenga, R.K.
The crystal structure of DELTA3-DELTA2-enoyl-CoA isomerase
J. Mol. Biol.
309
845-853
2001
Saccharomyces cerevisiae
Robert, J.; Marchesini, S.; Delessert, S.; Poirier, Y.
Analysis of the beta-oxidation of trans-unsaturated fatty acid in recombinant Saccharomyces cerevisiae expressing a peroxisomal PHA synthase reveals the involvement of a reductase-dependent pathway
BIOCHIM. BIOPHYS. ACTA
1734
169-177
2005
Saccharomyces cerevisiae, Saccharomyces cerevisiae BJ1991
Bogdawa, H.; Delessert, S.; Poirier, Y.
Analysis of the contribution of the beta-oxidation auxiliary enzymes in the degradation of the dietary conjugated linoleic acid 9-cis-11-trans-octadecadienoic acid in the peroxisomes of Saccharomyces cerevisiae
BIOCHIM. BIOPHYS. ACTA
1735
204-213
2005
Saccharomyces cerevisiae, Saccharomyces cerevisiae BJ1991
Geisbrecht, B.; Schulz, K.; Nau, K.; Geraghty, M.; Schulz, H.; Erdmann, R.; Gould, S.
Preliminary characterization of Yor180Cp Identification of a novel peroxisomal protein of Saccharomyces cerevisiae involved in fatty acid metabolism
Biochem. Biophys. Res. Commun.
260
28-34
1999
Saccharomyces cerevisiae, Saccharomyces cerevisiae BY4733
Onwukwe, G.U.; Koski, M.K.; Pihko, P.; Schmitz, W.; Wierenga, R.K.
Structures of yeast peroxisomal DELTA3,DELTA2-enoyl-CoA isomerase complexed with acyl-CoA substrate analogues the importance of hydrogen-bond networks for the reactivity of the catalytic base and the oxyanion hole
Acta Crystallogr. Sect. D
71
2178-2191
2015
Saccharomyces cerevisiae (Q05871)
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