Information on EC 5.3.3.8 - dodecenoyl-CoA isomerase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY
5.3.3.8
-
RECOMMENDED NAME
GeneOntology No.
dodecenoyl-CoA isomerase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
(3Z)-dodec-3-enoyl-CoA = (2E)-dodec-2-enoyl-CoA
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
intramolecular oxidoreduction
-
-
-
-
isomerization
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
fatty acid beta-oxidation I
-
fatty acid beta-oxidation III (unsaturated, odd number)
-
fatty acid beta-oxidation V (unsaturated, odd number, di-isomerase-dependent)
-
Fatty acid degradation
-
oleate beta-oxidation (isomerase-dependent, yeast)
-
unsaturated, even numbered fatty acid beta-oxidation
-
SYSTEMATIC NAME
IUBMB Comments
dodecenoyl-CoA (3Z)-(2E)-isomerase
Also catalyses the interconversion of 3-acetylenic fatty acyl thioesters and (+)-2,3-dienoyl fatty acyl thioesters, with fatty acid chain lengths C6 to C12.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
2,3-Enoyl-CoA isomerase
-
-
-
-
2,3-trans-enoyl-CoA isomerase
P42126
-
3,2-trans-Enoyl-CoA isomerase
-
-
-
-
3,2-trans-Enoyl-CoA isomerase
P42126
-
3,2-trans-enoyl-coenzyme A isomerase
P42126
-
3-2trans-Enoyl-CoA isomerase
-
-
-
-
3-cis-2-trans-Enoyl-CoA isomerase
-
-
-
-
Acetylene-allene isomerase
-
-
-
-
D3,D2-enoyl-CoA isomerase
-
-
-
-
DCI
P42126
-
DELTA3,DELTA2-enoyl CoA isomerase
-
-
DELTA3,DELTA2-enoyl-CoA isomerase
-
-
-
-
DELTA3,DELTA2-enoyl-CoA isomerase
-
-
DELTA3,DELTA2-enoyl-CoA isomerase
-
-
DELTA3,DELTA2-enoyl-CoA isomerase
-
-
DELTA3,DELTA2-enoyl-CoA isomerase
-
-
DELTA3,DELTA2-enoyl-CoA isomerase
Saccharomyces cerevisiae BJ1991
-
;
-
DELTA3-cis,DELTA2-trans-Enoyl-CoA isomerase
-
-
-
-
DELTA3-cis-DELTA2-trans-enoyl-CoA isomerase
-
-
-
-
Delta3-Delta2-enoyl-CoA isomerase
-
-
Dodecenoyl-CoA delta-isomerase
-
-
-
-
dodecenoyl-CoA DELTA3-cis-DELTA2-trans-isomerase
-
-
-
-
dodecenoyl-coenzyme A DELTA isomerase
P42126
-
ECI
-
-
-
-
ECI
-
monofunctional enoyl CoA isomerase
ECI
P23965
-
Hepatocellular carcinoma-associated antigen 88
-
-
-
-
Isomerase, dodecenoyl coenzyme A Delta-
-
-
-
-
Long-chain DELTA3,DELTA2-enoyl-CoA isomerase
-
-
-
-
MECI
-
mitochondrial enoyl-CoA isomerase, present only in the mitochondria
MFE1
-
multifunctional enzyme 1
Short chain DELTA3,DELTA2-enoyl-CoA isomerase
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
62213-29-0
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
genes AtECI1, AtECI2, AtECI3
-
-
Manually annotated by BRENDA team
multienzyme complex of fatty acid oxidation
-
-
Manually annotated by BRENDA team
multienzyme complex which exhibits activity of EC 4.2.1.17, EC 1.1.1.35, EC 2.3.1.16, EC 5.1.2.3 and EC 5.3.3.8
-
-
Manually annotated by BRENDA team
multienzyme complex which exhibits activity of EC 4.2.1.17, EC 1.1.1.35, EC 2.3.1.16, EC 5.1.2.3 and EC 5.3.3.8; wild-type and mutant enzymes alpha/Glu139Gln and alphaArg134Gln with mutations in the large alpha-subunit
-
-
Manually annotated by BRENDA team
strain B
-
-
Manually annotated by BRENDA team
at least 2 isoforms in liver: 1. monofunctional mitochondrial enzyme, 2. peroxisomal enzyme forming a part of a multifunctional enzyme
-
-
Manually annotated by BRENDA team
monofunctional enzyme
-
-
Manually annotated by BRENDA team
multifunctional enzyme with activity of Ec 5.3.3.8, EC 4.2.1.17 and EC 1.1.1.35
-
-
Manually annotated by BRENDA team
at least 3 DELTA3,DELTA2-enoyl-CoA isomerases: 1.mitochondrial clofibrate-inducible short-chain isomerase, 2.mitochondrial non-inducible long-chain isomerase, 3.peroxisomal isoenzyme, which is a part of a multifunctional protein
-
-
Manually annotated by BRENDA team
at least three isoenzymes in liver: 1. mitochondrial short-chain preferring isomerase, 2. mitochondrial long-chain preferring isomerase, 3. peroxisomal isoenzyme, which is part of a multifunctional protein
-
-
Manually annotated by BRENDA team
monofunctional DELTA3-DELTA2-enoyl-CoA isomerase
SwissProt
Manually annotated by BRENDA team
trifunctional enzyme which exhibits the activities of EC 5.3.3.8, EC 4.2.1.17 and EC 1.1.1.35
-
-
Manually annotated by BRENDA team
rat mitochondrial enoyl-CoA isomerase
-
-
Manually annotated by BRENDA team
Saccharomyces cerevisiae BJ1991
strain BJ1991
-
-
Manually annotated by BRENDA team
hog
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
physiological function
-
2,3-trans-enoyl-CoA isomerase is involved in mitochondrial beta-oxidation of unsaturated fatty acids
physiological function
-
the enzyme is involved in mitochondrial beta-oxidation of unsaturated fatty acids
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(3E)-undecenoyl CoA
(2E)-undecenoyl CoA
show the reaction diagram
-
intermediate of beta-oxidation of (10Z)-heptadecenoic acid. In vivo enzyme activity tests of the proteins encoded by AtECI1, AtECI2, and AtECI3 by complementation of the Saccharomyces cerevisiae double mutant eciDELTAdci1DELTA with deletions of the genes, DELTA2,DELTA3-enoyl-CoA isomerase and DELTA3,4,DELTA2,4-dienoyl CoA isomerase
-
-
?
(3E,7Z)-tridecedienoyl CoA
(2E,7Z)-tridecedienoyl CoA
show the reaction diagram
-
intermediate of beta-oxidation of 10Z-heptadecenoic acid. In vivo enzyme activity tests of the proteins encoded by AtECI1, AtECI2, and AtECI3 by complementation of the Saccharomyces cerevisiae double mutant eciDELTAdci1DELTA with deletions of the genes, DELTA2,DELTA3-enoyl-CoA isomerase and DELTA3,4,DELTA2,4-dienoyl CoA isomerase
-
-
?
(3Z)-nonenoyl CoA
(2Z)-nonenoyl CoA
show the reaction diagram
-
intermediate of beta-oxidation of (10Z)-heptadecenoic acid. In vivo enzyme activity tests of the proteins encoded by AtECI1, AtECI2, and AtECI3 by complementation of the Saccharomyces cerevisiae double mutant eciDELTAdci1DELTA with deletions of the genes, DELTA2,DELTA3-enoyl-CoA isomerase and DELTA3,4,DELTA2,4-dienoyl CoA isomerase
-
-
?
2-trans,5-cis-octadienoyl-CoA
3-cis,5-cis-octadienoyl-CoA
show the reaction diagram
-
-
-
?
2-trans,5-cis-tetradecadienoyl-CoA
3-cis,5-cis-octadienoyl-CoA
show the reaction diagram
-
-
-
?
2-trans,5-cis-tetradecadienoyl-CoA
3,5-cis-tetradecadienoyl-CoA
show the reaction diagram
-
-
-
-
?
3-cis-dodecenoyl-CoA
2-trans-dodecenoyl-CoA
show the reaction diagram
-
-
-
-
-
3-cis-dodecenoyl-CoA
2-trans-dodecenoyl-CoA
show the reaction diagram
-
-
-
-
3-cis-Hexenoyl-CoA
?
show the reaction diagram
-
-
-
-
-
3-cis-Hexenoyl-CoA
?
show the reaction diagram
-
most effective substrate
-
-
-
3-cis-hexenoyl-CoA
2-trans-hexenoyl-CoA
show the reaction diagram
-
-
-
?
3-cis-octenoyl-CoA
2-trans-octenoyl-CoA
show the reaction diagram
-
-
-
?
3-cis-octenoyl-CoA
2-trans-octenoyl-CoA
show the reaction diagram
-
-
-
?
3-cis-octenoyl-CoA
2-trans-octenoyl-CoA
show the reaction diagram
-
-
-
?
3-cis-Tetradecenoyl-CoA
2-trans-Tetradecenoyl-CoA
show the reaction diagram
-
-
-
-
-
3-cis-Tetradecenoyl-CoA
2-trans-Tetradecenoyl-CoA
show the reaction diagram
-
-
-
?
3-Decenoyl-pantetheine
?
show the reaction diagram
-
-
-
-
-
3-Decynoyl-CoA
?
show the reaction diagram
-
-
-
-
-
3-decynoyl-N-acetylcysteamine
2,3-decadienoyl-N-acetylcysteamine
show the reaction diagram
-
-
-
-
3-dodecynoyl-N-acetylcysteamine
?
show the reaction diagram
-
r
-
-
-
3-Hexynoyl-CoA
?
show the reaction diagram
-
-
-
-
-
3-hexynoyl-N-acetylcysteamine
?
show the reaction diagram
-
-
-
-
-
3-octynoyl-N-acetylcysteamine
?
show the reaction diagram
-
-
-
-
-
3-trans-Decenoyl-CoA
2-trans-Decenoyl-CoA
show the reaction diagram
-
-
-
-
-
3-trans-Decenoyl-CoA
2-trans-Decenoyl-CoA
show the reaction diagram
-
-
-
-
3-trans-Decenoyl-CoA
2-trans-Decenoyl-CoA
show the reaction diagram
-
-
-
-
-
3-trans-Decenoyl-CoA
2-trans-Decenoyl-CoA
show the reaction diagram
-
42% of the activity relative to 3-cis-hexenoyl-CoA
-
-
-
3-trans-dodecenoyl-CoA
2-trans-dodecenoyl-CoA
show the reaction diagram
-
-
-
-
-
3-trans-dodecenoyl-CoA
2-trans-dodecenoyl-CoA
show the reaction diagram
-
-
-
-
-
3-trans-dodecenoyl-CoA
2-trans-dodecenoyl-CoA
show the reaction diagram
-
-
-
-
3-trans-dodecenoyl-CoA
2-trans-dodecenoyl-CoA
show the reaction diagram
-
89% of the activity relative to 3-cis-hexenoyl-CoA
-
-
-
3-trans-Hexadecenoyl-CoA
2-trans-Hexadecenoyl-CoA
show the reaction diagram
-
-
-
-
-
3-trans-Hexenoyl-CoA
2-trans-Hexenoyl-CoA
show the reaction diagram
-
-
-
-
-
3-trans-Hexenoyl-CoA
2-trans-Hexenoyl-CoA
show the reaction diagram
-
-
-
-
3-trans-Hexenoyl-CoA
2-trans-Hexenoyl-CoA
show the reaction diagram
-
-
-
-
3-trans-Hexenoyl-CoA
2-trans-Hexenoyl-CoA
show the reaction diagram
-
-
-
-
-
3-trans-Hexenoyl-CoA
2-trans-Hexenoyl-CoA
show the reaction diagram
-
-
-
?
3-trans-Hexenoyl-CoA
2-trans-Hexenoyl-CoA
show the reaction diagram
-
-
-
?
3-trans-Hexenoyl-CoA
2-trans-Hexenoyl-CoA
show the reaction diagram
-
-
-
-
3-trans-Hexenoyl-CoA
2-trans-Hexenoyl-CoA
show the reaction diagram
-
-
-
-
3-trans-Hexenoyl-CoA
2-trans-Hexenoyl-CoA
show the reaction diagram
Q05871
-
-
?
3-trans-Hexenoyl-CoA
2-trans-Hexenoyl-CoA
show the reaction diagram
P23965
-
-
?
3-trans-Hexenoyl-CoA
2-trans-Hexenoyl-CoA
show the reaction diagram
P23965
-
-
-
?
3-trans-Hexenoyl-CoA
2-trans-Hexenoyl-CoA
show the reaction diagram
-
2.8% of the activity relative to 3-cis-hexenoyl-CoA
-
-
-
3-trans-Octenoyl-CoA
2-trans-Octenoyl-CoA
show the reaction diagram
-
-
-
?
3-trans-Octenoyl-CoA
2-trans-Octenoyl-CoA
show the reaction diagram
-
40% of the activity relative to 3-cis-hexenoyl-CoA
-
-
-
trans-2-hexenoyl-CoA + H2O
3-hydroxyhexanoyl-CoA
show the reaction diagram
P23965
K242C mutation allows Delta3-Delta2-enoyl-CoA isomerase to acquire enoyl-CoA hydratase activity
-
-
?
trans-3-hexenoyl-CoA
trans-2-hexenoyl-CoA
show the reaction diagram
P23965
-
-
-
?
trans-3-hexenoyl-CoA
trans-2-hexenoyl-CoA
show the reaction diagram
Q05871
-
-
-
-
3-trans-tetradecenoyl-CoA
2-trans-tetradecenoyl-CoA
show the reaction diagram
-
-
-
?
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
?
-
-
the velocity ratios with 3-trans-C6:C10:C12-enoyl-CoA is 1:2.1:1.2 for the liver enzyme and 1:3.4:2.3 for the heart enzyme
-
-
-
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
?
-
-
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
-
?
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 required for beta-oxidation of unsaturated 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
?
-
-
the enzyme is essential for the beta-oxidation of unsaturated fatty acids
-
?
additional information
?
-
-
the enzyme is essential for unsaturated fatty acid metabolism
-
?
additional information
?
-
P23965
the enzyme is involved in 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
?
-
-
oleate is mostly (about 90%) degraded via beta-oxidation in Escherichia coli. A small amount of 2-trans,5-cis-tetradecadienoyl-CoA is diverted from the pathway via conversion to 3,5-cis-tetradecadienoyl-CoA by DELTA3,DELTA2-enoyl-CoA isomerase. The CoA-bound intermediate, which would strongly inhibit beta-oxidation if allowed to accumulate, is hydrolyzed and the resultant 3,5-tetradecadienoate is excreted into the growth medium.
-
-
-
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
-
-
-
additional information
?
-
P23965
one of the key enzymes involved in fatty acid oxidation
-
-
-
additional information
?
-
-
enzyme participates in the degradation of unsaturated fatty acids through beta-oxidation
-
-
-
additional information
?
-
-
involved in mitochondrial beta-oxidation of unsaturated fatty acids. Decreased levels of this enzyme in metastatic breast cancer cells might have impact on the aberrant behavior of cancer cells
-
-
-
additional information
?
-
-
catalyzes the transformation of 3-cis- and 3-trans-enoyl-CoA esters arising during the stepwise degradation of cis-, mono-, and polyunsaturated fatty acids to the 2-trans-enoyl-CoA intermediates
-
-
-
additional information
?
-
Saccharomyces cerevisiae BJ1991
-
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
-
-
-
additional information
?
-
Saccharomyces cerevisiae BJ1991
-
main pathway for 9-cis,11-trans-octadecadienoic acid degradation requires the participation of DELTA3,DELTA2-enoyl-CoA isomerase
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
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 required for beta-oxidation of unsaturated 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
?
-
-
the enzyme is essential for the beta-oxidation of unsaturated fatty acids
-
?
additional information
?
-
-
the enzyme is essential for unsaturated fatty acid metabolism
-
?
additional information
?
-
P23965
the enzyme is involved in 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
?
-
-
oleate is mostly (about 90%) degraded via beta-oxidation in Escherichia coli. A small amount of 2-trans,5-cis-tetradecadienoyl-CoA is diverted from the pathway via conversion to 3,5-cis-tetradecadienoyl-CoA by DELTA3,DELTA2-enoyl-CoA isomerase. The CoA-bound intermediate, which would strongly inhibit beta-oxidation if allowed to accumulate, is hydrolyzed and the resultant 3,5-tetradecadienoate is excreted into the growth medium.
-
-
-
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
-
-
-
additional information
?
-
P23965
one of the key enzymes involved in fatty acid oxidation
-
-
-
additional information
?
-
-
enzyme participates in the degradation of unsaturated fatty acids through beta-oxidation
-
-
-
additional information
?
-
-
involved in mitochondrial beta-oxidation of unsaturated fatty acids. Decreased levels of this enzyme in metastatic breast cancer cells might have impact on the aberrant behavior of cancer cells
-
-
-
additional information
?
-
-
catalyzes the transformation of 3-cis- and 3-trans-enoyl-CoA esters arising during the stepwise degradation of cis-, mono-, and polyunsaturated fatty acids to the 2-trans-enoyl-CoA intermediates
-
-
-
additional information
?
-
Saccharomyces cerevisiae BJ1991
-
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
-
-
-
additional information
?
-
Saccharomyces cerevisiae BJ1991
-
main pathway for 9-cis,11-trans-octadecadienoic acid degradation requires the participation of DELTA3,DELTA2-enoyl-CoA isomerase
-
-
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
additional information
-
no requirement for metal ions
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2-trans-Dodecenoic acid
-
competitive inhibitor of 3-cis-dodecenoyl-CoA
3-Dodecynoic acid
-
competitive inhibitor of 3-cis-dodecenoyl-CoA
CoA
-
competitive inhibitor of 3-cis-dodecenoyl-CoA
diethyldicarbonate
-
-
long-chain acyl-CoA thioesters
-
-
Medium-chain acyl-CoA thioesters
-
-
-
PCMB
-
0.5 mM, 50% inhibition
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0044
-
2-trans,5-cis-octadienoyl-CoA
-
pH 8.0, 25C, MFE1
0.084
-
2-trans,5-cis-octadienoyl-CoA
-
pH 8.0, 25C, MECI
0.17
-
2-trans,5-cis-octadienoyl-CoA
-
pH 8.0, 25C, ECI
0.0096
-
2-trans,5-cis-tetradecadienoyl-CoA
-
pH 8.0, 25C, MFE1
0.02
-
2-trans,5-cis-tetradecadienoyl-CoA
-
pH 8.0, 25C, MECI
0.029
-
2-trans,5-cis-tetradecadienoyl-CoA
-
pH 8.0, 25C, ECI
0.032
-
3-cis-dodecenoyl-CoA
-
-
0.031
-
3-cis-Hexenoyl-CoA
-
pH 8.0, 25C, MFE1
0.14
-
3-cis-Hexenoyl-CoA
-
pI 7.01 enzyme
0.17
-
3-cis-Hexenoyl-CoA
-
-
0.24
-
3-cis-Hexenoyl-CoA
-
pH 8.0, 25C, MECI
0.27
-
3-cis-Hexenoyl-CoA
-
pI 6.83 enzyme
1.2
-
3-cis-Hexenoyl-CoA
-
pH 8.0, 25C, ECI
0.032
-
3-cis-octenoyl-CoA
-
pH 8.0, 25C, MFE1
0.1
-
3-cis-octenoyl-CoA
-
pH 8.0, 25C, ECI
0.15
-
3-cis-octenoyl-CoA
-
pH 8.0, 25C, MECI
0.006
-
3-cis-Tetradecenoyl-CoA
-
wild-type enzyme complex
0.021
-
3-cis-Tetradecenoyl-CoA
-
pH 8.0, 25C, ECI
0.045
-
3-cis-Tetradecenoyl-CoA
-
pH 8.0, 25C, MFE1
0.057
-
3-cis-Tetradecenoyl-CoA
-
pH 8.0, 25C, MECI
0.089
-
3-cis-Tetradecenoyl-CoA
-
mutant enzyme complex alpha/Glu139Gln
0.24
-
3-decynoyl-N-acetylcysteamine
-
pI 7.01 enzyme
0.52
-
3-decynoyl-N-acetylcysteamine
-
pI 6.83 enzyme
0.81
-
3-decynoyl-N-acetylcysteamine
-
pI 6.57 enzyme
0.28
-
3-dodecynoyl-N-acetylcysteamine
-
pI 7.01 enzyme
0.5
-
3-dodecynoyl-N-acetylcysteamine
-
pI 6.57 enzyme
0.97
-
3-dodecynoyl-N-acetylcysteamine
-
pI 6.83 enzyme
0.04
-
3-Hexenoyl-CoA
-
pI 7.01 enzyme
0.15
-
3-Hexenoyl-CoA
-
pI 6.83 enzyme
2.1
-
3-hexynoyl-N-acetylcysteamine
-
pI 7.01 enzyme
4
-
3-hexynoyl-N-acetylcysteamine
-
pI 6.57 enzyme
7.2
-
3-hexynoyl-N-acetylcysteamine
-
pI 6.83 enzyme
0.68
-
3-octynoyl-N-acetylcysteamine
-
pI 7.01 enzyme
1
-
3-octynoyl-N-acetylcysteamine
-
pI 6.57 enzyme
1.6
-
3-octynoyl-N-acetylcysteamine
-
pI 6.83 enzyme
0.021
-
3-trans-dodecenoyl-CoA
-
-
0.03
-
3-trans-Hexenoyl-CoA
P23965
mutant K242D, pH 8.0
0.038
-
3-trans-Hexenoyl-CoA
-
pH 8.0, 25C, MFE1
0.048
-
3-trans-Hexenoyl-CoA
P23965
wild-type, pH 8.0
0.076
-
3-trans-Hexenoyl-CoA
P23965
mutant K242T, pH 8.0
0.08
-
3-trans-Hexenoyl-CoA
P23965
mutant D149E, pH 8.0
0.081
-
3-trans-Hexenoyl-CoA
-
pH 7.5, 25C
0.089
-
3-trans-Hexenoyl-CoA
P23965
mutant K242R, pH 8.0
0.09
-
3-trans-Hexenoyl-CoA
-
pI 7.01 enzyme
0.1
-
3-trans-Hexenoyl-CoA
P23965
mutant K242F, pH 8.0
0.11
-
3-trans-Hexenoyl-CoA
-
pI 6.83 enzyme
0.12
-
3-trans-Hexenoyl-CoA
P23965
mutant K242C, pH 8.0
0.47
-
3-trans-Hexenoyl-CoA
-
pH 8.0, 25C, MECI
1.6
-
3-trans-Hexenoyl-CoA
-
pH 8.0, 25C, ECI
0.028
-
3-trans-Octenoyl-CoA
-
pH 8.0, 25C, MFE1
0.12
-
3-trans-Octenoyl-CoA
-
pH 8.0, 25C, ECI
0.19
-
3-trans-Octenoyl-CoA
-
pH 8.0, 25C, MECI
0.029
-
3-trans-tetradecenoyl-CoA
-
pH 8.0, 25C, ECI
0.032
-
3-trans-tetradecenoyl-CoA
-
pH 8.0, 25C, MFE1
0.00062
-
trans-2-Hexenoyl-CoA
P23965
pH 8, hydratase activity, mutant enzyme K242T
0.0026
-
trans-2-Hexenoyl-CoA
P23965
pH 8, hydratase activity, mutant enzyme K242D
0.31
-
trans-2-Hexenoyl-CoA
P23965
pH 8, hydratase activity, mutant enzyme K242C
0.03
-
trans-3-hexenoyl-CoA
P23965
25C, pH 7.5, mutant enzyme K242D
0.048
-
trans-3-hexenoyl-CoA
P23965
25C, pH 7.5, wild-type enzyme
0.076
-
trans-3-hexenoyl-CoA
P23965
25C, pH 7.5, mutant enzyme K242T
0.08
-
trans-3-hexenoyl-CoA
P23965
25C, pH 7.5, mutant enzyme D149E
0.089
-
trans-3-hexenoyl-CoA
P23965
25C, pH 7.5, mutant enzyme K242R
0.1
-
trans-3-hexenoyl-CoA
P23965
25C, pH 7.5, mutant enzyme K242F
0.12
-
trans-3-hexenoyl-CoA
P23965
25C, pH 7.5, mutant enzyme K242C
0.048
-
3-trans-tetradecenoyl-CoA
-
pH 8.0, 25C, MECI
additional information
-
additional information
-
-
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
11
-
2-trans,5-cis-octadienoyl-CoA
-
pH 8.0, 25C, MFE1
26
-
2-trans,5-cis-octadienoyl-CoA
-
pH 8.0, 25C, ECI
45
-
2-trans,5-cis-octadienoyl-CoA
-
pH 8.0, 25C, MECI
8.3
-
2-trans,5-cis-tetradecadienoyl-CoA
-
pH 8.0, 25C, MECI
12
-
2-trans,5-cis-tetradecadienoyl-CoA
-
pH 8.0, 25C, MFE1
15
-
2-trans,5-cis-tetradecadienoyl-CoA
-
pH 8.0, 25C, ECI
128
-
3-cis-dodecenoyl-CoA
-
-
1.6
-
3-cis-Hexenoyl-CoA
-
pH 8.0, 25C, MFE1
4
-
3-cis-Hexenoyl-CoA
-
pI 6.83 enzyme
9.4
-
3-cis-Hexenoyl-CoA
-
pI 7.01 enzyme
58
-
3-cis-Hexenoyl-CoA
-
pH 8.0, 25C, ECI
200
-
3-cis-Hexenoyl-CoA
-
pH 8.0, 25C, MECI
2.4
-
3-cis-octenoyl-CoA
-
pH 8.0, 25C, MFE1
47
-
3-cis-octenoyl-CoA
-
pH 8.0, 25C, ECI
180
-
3-cis-octenoyl-CoA
-
pH 8.0, 25C, MECI
2.7
-
3-cis-Tetradecenoyl-CoA
-
pH 8.0, 25C, MFE1
25
-
3-cis-Tetradecenoyl-CoA
-
mutant enzyme complex alpha/Glu139Gln
63
-
3-cis-Tetradecenoyl-CoA
-
wild-type enzyme complex
98
-
3-cis-Tetradecenoyl-CoA
-
pH 8.0, 25C, MECI
210
-
3-cis-Tetradecenoyl-CoA
-
pH 8.0, 25C, ECI
50
-
3-decynoyl-N-acetylcysteamine
-
pI 6.57 enzyme
68
-
3-decynoyl-N-acetylcysteamine
-
pI 6.57 enzyme
128
-
3-decynoyl-N-acetylcysteamine
-
pI 7.01 enzyme
190
-
3-decynoyl-N-acetylcysteamine
-
pI 6.83 enzyme
284
-
3-decynoyl-N-acetylcysteamine
-
pI 6.83 enzyme
59
-
3-dodecynoyl-N-acetylcysteamine
-
pI 6.83 enzyme
160
-
3-dodecynoyl-N-acetylcysteamine
-
pI 7.01 enzyme
500
-
3-dodecynoyl-N-acetylcysteamine
-
pI 6.83 enzyme
12.1
-
3-Hexynoyl-CoA
-
pI 7.01 enzyme
25
-
3-Hexynoyl-CoA
-
pI 6.83 enzyme
33
-
3-hexynoyl-N-acetylcysteamine
-
pI 6.57 enzyme
61
-
3-hexynoyl-N-acetylcysteamine
-
pI 6.83 enzyme
130
-
3-hexynoyl-N-acetylcysteamine
-
pI 6.83 enzyme
105
-
3-octynoyl-N-acetylcysteamine
-
pI 7.01 enzyme
0.06
-
3-trans-Hexenoyl-CoA
P23965
mutant K242D, pH 8.0
0.14
-
3-trans-Hexenoyl-CoA
P23965
mutant K242F, pH 8.0
0.19
-
3-trans-Hexenoyl-CoA
P23965
mutant K242T, pH 8.0
1.8
-
3-trans-Hexenoyl-CoA
-
pH 8.0, 25C, MFE1
3
-
3-trans-Hexenoyl-CoA
-
pI 6.83 enzyme
5
-
3-trans-Hexenoyl-CoA
-
pI 7.01 enzyme
11
-
3-trans-Hexenoyl-CoA
P23965
mutant K242C, pH 8.0
50
-
3-trans-Hexenoyl-CoA
P23965
mutant K242R, pH 8.0
70
-
3-trans-Hexenoyl-CoA
P23965
mutant D149E, pH 8.0
100
-
3-trans-Hexenoyl-CoA
-
pH 8.0, 25C, ECI
160
-
3-trans-Hexenoyl-CoA
P23965
wild-type, pH 8.0
270
-
3-trans-Hexenoyl-CoA
-
pH 8.0, 25C, MECI
2
-
3-trans-Octenoyl-CoA
-
pH 8.0, 25C, MFE1
25
-
3-trans-Octenoyl-CoA
-
pH 8.0, 25C, MECI
210
-
3-trans-Octenoyl-CoA
-
pH 8.0, 25C, ECI
1.4
-
3-trans-tetradecenoyl-CoA
-
pH 8.0, 25C, MFE1
20
-
3-trans-tetradecenoyl-CoA
-
pH 8.0, 25C, MECI
0.013
-
trans-2-Hexenoyl-CoA
P23965
pH 8, hydratase activity, mutant enzyme K242D
0.021
-
trans-2-Hexenoyl-CoA
P23965
pH 8, hydratase activity, mutant enzyme K242T
1
-
trans-2-Hexenoyl-CoA
P23965
pH 8, hydratase activity, mutant enzyme K242C
0.06
-
trans-3-hexenoyl-CoA
P23965
25C, pH 7.5, mutant enzyme K242D
0.11
-
trans-3-hexenoyl-CoA
-
pH 7
0.14
-
trans-3-hexenoyl-CoA
P23965
25C, pH 7.5, mutant enzyme K242F
0.19
-
trans-3-hexenoyl-CoA
P23965
25C, pH 7.5, mutant enzyme K242T
6.5
-
trans-3-hexenoyl-CoA
-
pH 9.0
11
-
trans-3-hexenoyl-CoA
P23965
25C, pH 7.5, mutant enzyme K242C
50
-
trans-3-hexenoyl-CoA
P23965
25C, pH 7.5, mutant enzyme K242R
70
-
trans-3-hexenoyl-CoA
P23965
25C, pH 7.5, mutant enzyme D149E
160
-
trans-3-hexenoyl-CoA
P23965
25C, pH 7.5, wild-type enzyme
540
-
3-trans-tetradecenoyl-CoA
-
pH 8.0, 25C, ECI
additional information
-
additional information
-
-
-
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
21
-
-
human mitochondrial DELTA3,DELTA2-enoyl-CoA-isomerase
46.9
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
catalytic activity of E136A variant below detection limit
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7
-
-
-
7.5
8
-
phosphate buffer
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5
9
-
pH 5: about 50% of maximal activity, pH 7-9: maximal activity
6
8.5
-
at least 60% of maximal activity over the pH range 6 to 8.5
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
37
-
-
-
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6
-
-
theoretical
6
-
-
estimated from amino acid sequence
6.3
-
-
determined by 2-D gel electrophoresis
6.3
-
-
isoelectric focusing
6.7
-
-
AtECI1
7.3
-
-
AtECI3
8.6
-
-
AtECI2
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
weakly expressed
Manually annotated by BRENDA team
-
fat-degrading
Manually annotated by BRENDA team
-
proximal tubules
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
at least 2 isoforms in liver: 1. monofunctional mitochondrial enzyme, 2. peroxisomal enzyme forming a part of a multifunctional enzyme
Manually annotated by BRENDA team
-
short chain DELTA3,DELTA2-enoyl-CoA isomerase
Manually annotated by BRENDA team
-
most strongly expressed
Manually annotated by BRENDA team
-
weakly expressed
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
determined by producing constructs between enhanced yellow fluorescent protein (EYFP) at the N-terminus and the AtECI proteins at the C-terminus. The localization of EYFP-AtECI1 and EYFP-AtECI2 indicate that AtECI1 and AtECI2 are peroxisomal proteins. The EYFP-AtECI3 construct results in diffuse fluorescence throughout the cytosol and nucleus, indicating the absence of peroxisomal targeting. AtECI1, AtECI2, and AtECI3 show high overall homology to peroximal mammalian isomerases, but have only one coserved glutamate reisdue in an position similar to that in the mitochondrial isoemrases
Manually annotated by BRENDA team
-
tightly membrane-associated, sole site of enzyme activity
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
short chain DELTA3,DELTA2-enoyl-CoA isomerase
Manually annotated by BRENDA team
-
main intracellular site
Manually annotated by BRENDA team
-
enzyme is synthesized with a N-terminal mitochondrial targeting sequence which is cleaved during mitochondrial import
Manually annotated by BRENDA team
-
determined by producing constructs between enhanced yellow fluorescent protein (EYFP) at the N-terminus and the AtECI proteins at the C-terminus. The localization of EYFP-AtECI1 and EYFP-AtECI2 indicate that AtECI1 and AtECI2 are peroxisomal proteins. The EYFP-AtECI3 construct results in diffuse fluorescence throughout the cytosol and nucleus, indicating the absence of peroxisomal targeting. AtECI1, AtECI2, and AtECI3 show high overall homology to peroximal mammalian isomerases, but have only one conserved glutamate reisdue in an position similar to that in the mitochondrial isoemrases
Manually annotated by BRENDA team
-
trifunctional enzyme which exhibits the activities of EC5.3.3.8, EC 4.2.1.17 and EC 1.1.1.35
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
exclusively localized in
Manually annotated by BRENDA team
-
minor intracellular site
Manually annotated by BRENDA team
-
determined by producing constructs between enhanced yellow fluorescent protein (EYFP) at the N-terminus and the AtECI proteins at the C-terminus. The localization of EYFP-AtECI1 and EYFP-AtECI2 indicate that AtECI1 and AtECI2 are peroxisomal proteins. The EYFP-AtECI3 construct results in diffuse fluorescence throughout the cytosol and nucleus, indicating the absence of peroxisomal targeting. AtECI1, AtECI2, and AtECI3 show high overall homology to peroximal mammalian isomerases, but have only one coserved glutamate reisdue in an position similar to that in the mitochondrial isoemrases
Manually annotated by BRENDA team
Saccharomyces cerevisiae BJ1991
-
;
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Mycobacterium paratuberculosis (strain ATCC BAA-968 / K-10)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
26000
-
-
AtECI1, AtECI2, AtECI3, all three proteins consist of 240 amino acids, predicted mass. AtECI2 and AtECI3 share 77% identity over the whole protein, and both are located in tandem on chromosome 4, separated by 1314 bp
27000
-
-
determined by 2-D gel electrophoresis
28000
-
-
theoretical
50000
-
-
gel filtration
60000
-
-
gel filtration
60000
-
-
gel filtration
60000
-
-
gel filtration
70000
-
-
liver, monomeric enzyme, gel filtration; myocardium, dimeric enzyme, gel filtration
73000
-
-
liver, sucrose density gradient centrifugation
75000
-
-
multifunctional enzyme with activity of EC 5.3.3.8, EC 4.2.1.17 and EC 1.1.1.35, gel filtration
80000
-
-
heart, gel filtration
81000
-
-
liver, gel filtration
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
91000
-
-
equilibrium ultracentrifugation
170000
-
-
gel filtration, dynamic light-scattering
170000
-
-
gel filtration
200000
-
-
long-chain isomerase, gel filtration
260000
-
-
multienzyme complex which exhibits activity of EC 4.2.1.17, EC 1.1.1.35, EC 2.3.1.16, EC 5.1.2.3 and EC 5.3.3.8, gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
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 * 31000, SDS-PAGE in presence of 6 M urea
?
-
x * 30000, SDS-PAGE in presence of 6 M urea
?
-
x * 29000, SDS-PAGE in presence of 6 M urea
?
-
x * 28735, calculation from nucleotide sequence
?
-
x * 29300, short chain preferring DELTA3,DELTA2-enoyl-CoA isomerase, calculation from cDNA-derived nucleotide sequence
?
-
x * 39600, calculation from nucleotide sequence
?
-
x * 39400, calculation from nucleotide sequence
?
-
x * 27000, SDS-PAGE; x * 28000, estimated from amino acid sequence
dimer
-
2 * 47000, SDS-PAGE
dimer
-
2 * 30000, SDS-PAGE, enzyme has a strong tendency to form a dimer, monomeric form is also active
dimer
-
x * 32254, calculation from nucleotide sequence
dimer
-
2 * 30000, SDS-PAGE
dimer
-
2 * 30000, liver and heart enzyme, SDS-PAGE in presence of 6 M urea
dimer
-
-
dimer
-
2 * 30000, myocardium, SDS-PAGE
dimer
-
2 * 24000, SDS-PAGE
dimer
-
2 * 29300, mitochondrial clofibrate-inducible short-chain isomerase
dimer
-
2 * 30000, SDS-PAGE
hexamer
-
6 * 32000, SDS-PAGE
monomer
-
1 * 75000, multifunctional enzyme with activity of EC 5.3.3.8, EC 4.2.1.17 and EC 1.1.1.35, SDS-PAGE
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 * 78000, liver, SDS-PAGE
monomer
-
1 * 78511, peroxisomal isoenzyme, which is a part of a multifunctional protein
tetramer
-
2 * 42000 + 2 * 78000, multienzyme complex which exhibits activity of EC 4.2.1.17, EC 1.1.1.35, EC 2.3.1.16, EC 5.1.2.3 and EC 5.3.3.8, SDS-PAGE
tetramer
Escherichia coli B.
-
2 * 42000 + 2 * 78000, multienzyme complex which exhibits activity of EC 4.2.1.17, EC 1.1.1.35, EC 2.3.1.16, EC 5.1.2.3 and EC 5.3.3.8, SDS-PAGE
-
trimer
-
crystallographic analysis
trimer
-
crystallographic analysis
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
lipoprotein
-
multienzyme complex which exhibits activity of EC 4.2.1.17, EC 1.1.1.35, EC 2.3.1.16, EC 5.1.2.3 and EC 5.3.3.8, contains 63 nmol of lipid per mg of protein: phosphatidylethanolamine, phosphatidylglycerol, and cardiolipin
lipoprotein
Escherichia coli B.
-
multienzyme complex which exhibits activity of EC 4.2.1.17, EC 1.1.1.35, EC 2.3.1.16, EC 5.1.2.3 and EC 5.3.3.8, contains 63 nmol of lipid per mg of protein: phosphatidylethanolamine, phosphatidylglycerol, and cardiolipin
-
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
crystal structure of DELTA3,DELTA2-enoyl-CoA isomerase complexed with the substrate analogue octanoyl-CoA has been refined a 1.3 angstrom resolution
-
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
-
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0
4
-
slow loss of activity
23
-
-
8 h, stable at room temperature
OXIDATION STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
loss of activity by photooxidation of His residue at neutral pH in presence of rose bengal
-
3010
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-20C, stable for more than 3 years
-
-80C, stable for at least 6 months
-
0-4C, slow loss of activity
-
4C, stable for 2 days
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
partial, multienzyme complex of fatty acid oxidation
-
enzyme consistently copurifies with glutathione S-transferase
-
gel filtration
-
recombinant enzyme
-
ECI, MECI and MFE1
-
trifunctional enzyme which exhibits the activities of EC 5.3.3.8, EC 4.2.1.17 and EC 1.1.1.35
-
4 enzyme forms: pI 7.27 enzyme, pI 7.01 enzyme, pI 6.83 enzyme, pI 6.57 enzyme
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
heterologously expressed in Sacchcaromyces cerevisiae. In vivo enzyme activity tests of the proteins encoded by AtECI1, AtECI2, and AtECI3 by complementation of the Saccharomyces cerevisiae double mutant eciDELTAdci1DELTA with deletions of the genes, DELTA2,DELTA3-enoyl-CoA isomerase and DELTA3,4,DELTA2,4-dienoyl CoA isomerase
-
multienzyme complex
-
expression in Escherichia coli
-
; expression in Escherichia coli
P23965
overexpression in Escherichia coli
-
wild type and mutant enzymes expressed in Escherichia coli
-
expression in Escherichia coli
-
expression in Escherichia coli
-
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expression of 2,3-trans-enoyl-CoA isomerase is decreased in metastatic tumor tissue
-
dodecenoyl-coenzyme A DELTA isomerase mRNA in omental fat depots from normal and obese individuals demonstrates a 1.6fold underexpression in obese patients
-
the level of 2,3-trans-enoyl-CoA isomerase is decreased in metastatic breast cancer
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
E134Q
-
catalytic properties of the five different component enzyme activities of the alpha/Arg134Gln mutant complex show no significant changes as compared with those of the wild-type complex. In the alpha/Glu139Gln mutant complex DELTA3-cis-DELTA2-trans-enoyl-CoA isomerase shows 60% decreased turnover number and a significant increase in Km for 3-cis-tetradecenoyl-CoA
E139Q
-
The replacement of Glu165 by Gln leads to a strongly reduced enzymatic activity. Tyr150 is not involved in isomerase catalysis
E136A
-
variant to study the importance of Glu136 for catalysis
D149E
P23965
decrease in catalytic activity; 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
P23965
decrease in catalytic activity, mutants shows additional hydratase activity on 2-hexenoyl-CoA with Vmax of 1.9 micromol per min and mg; 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; 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
P23965
decrease in catalytic activity, mutants shows slight additional hydratase activity on 2-hexenoyl-CoA with Vmax of 0.026 micromol per min and mg; 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; 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
K242F
P23965
decrease in catalytic activity; 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
P23965
decrease in catalytic activity; 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
P23965
decrease in catalytic activity, mutants shows additional hydratase activity on 2-hexenoyl-CoA with Vmax of 0.041 micromol per min and mg; 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; 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
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
additional information
-
in the absence of DELTA3,DELTA2-enoyl CoA isomerase, complete beta-oxidation of (10Z)-heptadecanoic acid is blocked. In vivo enzyme activity tests of the proteins encoded by AtECI1, AtECI2, and AtECI3 by complementation of the Saccharomyces cerevisiae double mutant eciDELTAdci1DELTA with deletions of the genes, DELTA2,DELTA3-enoyl-CoA isomerase and DELTA3,4,DELTA2,4-dienoyl CoA isomerase
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
medicine
-
decreased levels of 2,3-trans-enoyl-CoA isomerase might have impact on the aberrant behaviour of cancer cells