Information on EC 5.3.3.8 - dodecenoyl-CoA isomerase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
5.3.3.8
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RECOMMENDED NAME
GeneOntology No.
dodecenoyl-CoA isomerase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(3Z)-dodec-3-enoyl-CoA = (2E)-dodec-2-enoyl-CoA
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
intramolecular oxidoreduction
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isomerization
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
fatty acid beta-oxidation I
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fatty acid beta-oxidation III (unsaturated, odd number)
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fatty acid beta-oxidation V (unsaturated, odd number, di-isomerase-dependent)
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Fatty acid degradation
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lipid metabolism
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oleate beta-oxidation (isomerase-dependent, yeast)
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unsaturated, even numbered fatty acid beta-oxidation
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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.
CAS REGISTRY NUMBER
COMMENTARY hide
62213-29-0
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
genes AtECI1, AtECI2, AtECI3
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
rat mitochondrial enoyl-CoA isomerase
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Manually annotated by BRENDA team
strain BJ1991
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
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enzyme knockdown of inhibits hepatitis C virus RNA replication in cultured hepatoma cells. Enzyme deficiency causes alterations in the cellular metabolome
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(3E)-undecenoyl CoA
(2E)-undecenoyl CoA
show the reaction diagram
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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
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-
?
(3E,7Z)-tridecedienoyl CoA
(2E,7Z)-tridecedienoyl CoA
show the reaction diagram
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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
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-
?
(3Z)-nonenoyl CoA
(2Z)-nonenoyl CoA
show the reaction diagram
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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
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-
?
2-trans,5-cis-octadienoyl-CoA
3-cis,5-cis-octadienoyl-CoA
show the reaction diagram
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?
2-trans,5-cis-tetradecadienoyl-CoA
3,5-cis-tetradecadienoyl-CoA
show the reaction diagram
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?
2-trans,5-cis-tetradecadienoyl-CoA
3-cis,5-cis-octadienoyl-CoA
show the reaction diagram
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?
3-cis-dodecenoyl-CoA
2-trans-dodecenoyl-CoA
show the reaction diagram
3-cis-hexenoyl-CoA
2-trans-hexenoyl-CoA
show the reaction diagram
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-
?
3-cis-Hexenoyl-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-Decenoyl-pantetheine
?
show the reaction diagram
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3-Decynoyl-CoA
?
show the reaction diagram
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3-decynoyl-N-acetylcysteamine
2,3-decadienoyl-N-acetylcysteamine
show the reaction diagram
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3-dodecynoyl-N-acetylcysteamine
?
show the reaction diagram
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r
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3-Hexynoyl-CoA
?
show the reaction diagram
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3-hexynoyl-N-acetylcysteamine
?
show the reaction diagram
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3-octynoyl-N-acetylcysteamine
?
show the reaction diagram
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3-trans-Decenoyl-CoA
2-trans-Decenoyl-CoA
show the reaction diagram
3-trans-dodecenoyl-CoA
2-trans-dodecenoyl-CoA
show the reaction diagram
3-trans-Hexadecenoyl-CoA
2-trans-Hexadecenoyl-CoA
show the reaction diagram
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3-trans-Hexenoyl-CoA
2-trans-Hexenoyl-CoA
show the reaction diagram
3-trans-octenoyl-CoA
2-trans-octenoyl-CoA
show the reaction diagram
3-trans-tetradecenoyl-CoA
2-trans-tetradecenoyl-CoA
show the reaction diagram
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-
?
trans-2-hexenoyl-CoA + H2O
3-hydroxyhexanoyl-CoA
show the reaction diagram
K242C mutation allows Delta3-Delta2-enoyl-CoA isomerase to acquire enoyl-CoA hydratase activity
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?
trans-3-hexenoyl-CoA
trans-2-hexenoyl-CoA
show the reaction diagram
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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no requirement for metal ions
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-trans-Dodecenoic acid
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competitive inhibitor of 3-cis-dodecenoyl-CoA
3-Dodecynoic acid
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competitive inhibitor of 3-cis-dodecenoyl-CoA
CoA
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competitive inhibitor of 3-cis-dodecenoyl-CoA
diethyldicarbonate
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long-chain acyl-CoA thioesters
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Medium-chain acyl-CoA thioesters
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0044 - 0.17
2-trans,5-cis-octadienoyl-CoA
0.0096 - 0.029
2-trans,5-cis-tetradecadienoyl-CoA
0.032
3-cis-dodecenoyl-CoA
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0.031 - 1.2
3-cis-hexenoyl-CoA
0.032 - 0.15
3-cis-octenoyl-CoA
0.006 - 0.089
3-cis-Tetradecenoyl-CoA
0.24 - 0.81
3-decynoyl-N-acetylcysteamine
0.28 - 0.97
3-dodecynoyl-N-acetylcysteamine
0.04 - 0.15
3-hexenoyl-CoA
2.1 - 7.2
3-hexynoyl-N-acetylcysteamine
0.68 - 1.6
3-octynoyl-N-acetylcysteamine
0.021
3-trans-dodecenoyl-CoA
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0.03 - 1.6
3-trans-hexenoyl-CoA
0.028 - 0.19
3-trans-Octenoyl-CoA
0.029 - 0.048
3-trans-tetradecenoyl-CoA
0.00062 - 0.31
trans-2-hexenoyl-CoA
0.03 - 0.12
trans-3-hexenoyl-CoA
additional information
additional information
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
11 - 45
2-trans,5-cis-octadienoyl-CoA
8.3 - 15
2-trans,5-cis-tetradecadienoyl-CoA
128
3-cis-dodecenoyl-CoA
Bos taurus
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1.6 - 200
3-cis-hexenoyl-CoA
2.4 - 180
3-cis-octenoyl-CoA
2.7 - 210
3-cis-Tetradecenoyl-CoA
50 - 284
3-decynoyl-N-acetylcysteamine
59 - 500
3-dodecynoyl-N-acetylcysteamine
12.1 - 25
3-Hexynoyl-CoA
33 - 130
3-hexynoyl-N-acetylcysteamine
105
3-octynoyl-N-acetylcysteamine
Sus scrofa
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pI 7.01 enzyme
0.06 - 270
3-trans-hexenoyl-CoA
2 - 210
3-trans-Octenoyl-CoA
1.4 - 540
3-trans-tetradecenoyl-CoA
0.013 - 1
trans-2-hexenoyl-CoA
0.06 - 160
trans-3-hexenoyl-CoA
additional information
additional information
Sus scrofa
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.5
PCMB
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
21
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human mitochondrial DELTA3,DELTA2-enoyl-CoA-isomerase
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5 - 8
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phosphate buffer
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 9
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pH 5: about 50% of maximal activity, pH 7-9: maximal activity
6 - 8.5
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at least 60% of maximal activity over the pH range 6 to 8.5
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6
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estimated from amino acid sequence; theoretical
6.3
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determined by 2-D gel electrophoresis; isoelectric focusing
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
weakly expressed
Manually annotated by BRENDA team
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most strongly expressed
Manually annotated by BRENDA team
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weakly expressed
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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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
PDB
SCOP
CATH
ORGANISM
UNIPROT
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)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
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
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
26000
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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
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determined by 2-D gel electrophoresis
28000
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theoretical
50000
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gel filtration
70000
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liver, monomeric enzyme, gel filtration; myocardium, dimeric enzyme, gel filtration
73000
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liver, sucrose density gradient centrifugation
75000
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multifunctional enzyme with activity of EC 5.3.3.8, EC 4.2.1.17 and EC 1.1.1.35, gel filtration
80000
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heart, gel filtration
81000
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liver, gel filtration
83000
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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
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equilibrium ultracentrifugation
170000
200000
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long-chain isomerase, gel filtration
260000
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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
COMMENTARY hide
LITERATURE
hexamer
monomer
tetramer
trimer
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
lipoprotein
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystal structure of DELTA3,DELTA2-enoyl-CoA isomerase complexed with the substrate analogue octanoyl-CoA has been refined a 1.3 angstrom resolution
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hanging drop vapor diffusion method, 2.1 A structure of a tight hexameric crystal form of the enzyme
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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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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0 - 4
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slow loss of activity
23
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8 h, stable at room temperature
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
loss of activity by photooxidation of His residue at neutral pH in presence of rose bengal
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3010
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, stable for more than 3 years
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-80C, stable for at least 6 months
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0-4C, slow loss of activity
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4C, stable for 2 days
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
4 enzyme forms: pI 7.27 enzyme, pI 7.01 enzyme, pI 6.83 enzyme, pI 6.57 enzyme
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ECI, MECI and MFE1
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enzyme consistently copurifies with glutathione S-transferase
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gel filtration
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partial, multienzyme complex of fatty acid oxidation
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recombinant enzyme
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trifunctional enzyme which exhibits the activities of EC 5.3.3.8, EC 4.2.1.17 and EC 1.1.1.35
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
; expression in Escherichia coli
expressed in Escherichia coli DH5alpha cells
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expression in Escherichia coli
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
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multienzyme complex
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overexpression in Escherichia coli
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wild type and mutant enzymes expressed in Escherichia coli
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
dodecenoyl-coenzyme A DELTA isomerase mRNA in omental fat depots from normal and obese individuals demonstrates a 1.6fold underexpression in obese patients
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expression of 2,3-trans-enoyl-CoA isomerase is decreased in metastatic tumor tissue; the level of 2,3-trans-enoyl-CoA isomerase is decreased in metastatic breast cancer
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E134Q
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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
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The replacement of Glu165 by Gln leads to a strongly reduced enzymatic activity. Tyr150 is not involved in isomerase catalysis
E136A
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variant to study the importance of Glu136 for catalysis
D149E
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
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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
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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
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
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
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
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
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
COMMENTARY hide
LITERATURE
medicine
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decreased levels of 2,3-trans-enoyl-CoA isomerase might have impact on the aberrant behaviour of cancer cells
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