Information on EC 1.3.1.34 - 2,4-dienoyl-CoA reductase (NADPH)

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

EC NUMBER
COMMENTARY hide
1.3.1.34
-
RECOMMENDED NAME
GeneOntology No.
2,4-dienoyl-CoA reductase (NADPH)
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
trans-2,3-didehydroacyl-CoA + NADP+ = trans,trans-2,3,4,5-tetradehydroacyl-CoA + NADPH + H+
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
10-cis-heptadecenoyl-CoA degradation (yeast)
-
-
10-trans-heptadecenoyl-CoA degradation (reductase-dependent, yeast)
-
-
fatty acid beta-oxidation V (unsaturated, odd number, di-isomerase-dependent)
-
-
oleate beta-oxidation (reductase-dependent, yeast)
-
-
unsaturated, even numbered fatty acid beta-oxidation
-
-
lipid metabolism
-
-
SYSTEMATIC NAME
IUBMB Comments
trans-2,3-didehydroacyl-CoA:NADP+ 4-oxidoreductase
Best substrates for reduction contain a 2,4-diene structure with a chain-length of 8 or 10
CAS REGISTRY NUMBER
COMMENTARY hide
82869-38-3
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
strain B.
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
Wistar
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(2E,4E)-2,4-decadienoyl-CoA + NADPH
?
show the reaction diagram
-
-
-
-
?
(2E,4E)-2,4-hexadienoyl-CoA + NADPH
?
show the reaction diagram
-
-
-
-
?
(2E,4E)-hexa-2,4-dienoyl-CoA + NADPH + H+
(3E)-hex-3-enoyl-CoA + NADP+
show the reaction diagram
-
-
-
-
?
2,4,7,10,13,16,19-docosaheptaenoyl-CoA + NADPH
?
show the reaction diagram
2,4-cis-tetradecadienoyl-CoA + NADPH
2-cis-dehydroacyl-CoA + NADP+
show the reaction diagram
-
low activity
-
-
?
2,4-hexadienoyl-CoA + NADPH
3-hexadienoyl-CoA + NADP+
show the reaction diagram
2,4-trans-decadienoyl-CoA + NADPH
? + NADP+
show the reaction diagram
2,4-trans-hexadienoyl-CoA + NADPH
trans-3-hexenoyl-CoA + NADP+
show the reaction diagram
-
-
-
-
?
2,4-trans-tetradecadienoyl-CoA + NADPH
2-trans-dehydroacyl-CoA + NADP+
show the reaction diagram
-
-
-
-
?
2-cis,4-cis/trans-dienoyl-CoA + NADPH + H+
3-trans-enoyl-CoA + NADP+
show the reaction diagram
-
-
-
-
?
2-fluoro-trans-trans-2,4-octadienoyl-CoA + NADPH
2-fluoro-trans-3-octenoyl + NADP+
show the reaction diagram
-
substrate analogue, recombinant enzyme, reaction mechanism
-
-
?
2-trans,4-cis-decadienoyl-CoA + NADPH
2-decenoyl-CoA + NADP+
show the reaction diagram
-
-
initial reaction product
?
2-trans,4-cis-decadienoyl-CoA + NADPH
3-trans-decenoyl-CoA + NADP+
show the reaction diagram
2-trans,4-cis-decadienoylcarnitine + ?
?
show the reaction diagram
-
abnormal unsaturated fatty acid oxidation
-
-
-
2-trans,4-trans-decadienoyl-CoA + NADPH
2-trans-decenoyl-CoA + NADP+
show the reaction diagram
-
2-trans-decenoyl-CoA is the normal product of the wild type enzyme in bacteria
-
?
2-trans,4-trans-decadienoyl-CoA + NADPH
3-decenoyl-CoA + NADP+
show the reaction diagram
2-trans,4-trans-decadienoyl-CoA + NADPH
3-trans-decenoyl-CoA + NADP+
show the reaction diagram
-
3-trans-decenoyl-CoA is the product of the mutant enzymes Y166F, H252A, and H252A/Y166F
-
?
2-trans,4-trans-hexadienoyl-CoA + NADPH
?
show the reaction diagram
5-methyl-trans-trans-2,4-hexadienoyl-CoA + NADPH
5-methyl-trans-3-hexenoyl-CoA + NADP+
show the reaction diagram
-
substrate analogue, recombinant enzyme
-
-
?
5-phenyl-2,4-pentadienoyl-CoA + NADPH
?
show the reaction diagram
-
-
-
-
?
pent-2,4-dienoyl-CoA + NADPH
?
show the reaction diagram
-
-
-
-
?
trans-trans-2,4-hexadecadienoyl-CoA + NADPH
trans-2-hexadecenoyl-CoA + NADP+
show the reaction diagram
-
step in the beta-oxidation of oleoyl-CoA via 2-trans-5-cis-tetradecadienoyl-CoA in mitochondria via the reductase-dependent pathway, enzyme is not involved in the isomerase-dependent pathway, overview
-
-
?
trans-trans-2,4-hexadienoyl-CoA + NADPH
trans-3-hexenoyl-CoA + NADP+
show the reaction diagram
additional information
?
-
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
2-cis,4-cis/trans-dienoyl-CoA + NADPH + H+
3-trans-enoyl-CoA + NADP+
show the reaction diagram
-
-
-
-
?
2-trans,4-cis-decadienoylcarnitine + ?
?
show the reaction diagram
-
abnormal unsaturated fatty acid oxidation
-
-
-
trans-trans-2,4-hexadecadienoyl-CoA + NADPH
trans-2-hexadecenoyl-CoA + NADP+
show the reaction diagram
-
step in the beta-oxidation of oleoyl-CoA via 2-trans-5-cis-tetradecadienoyl-CoA in mitochondria via the reductase-dependent pathway, enzyme is not involved in the isomerase-dependent pathway, overview
-
-
?
trans-trans-2,4-hexadienoyl-CoA + NADPH
trans-3-hexenoyl-CoA + NADP+
show the reaction diagram
-
-
-
-
r
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4Fe-4S-center
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FAD
-
determined by HPLC or fluorometrically, molar ratio of cofactor to enzyme: 1
flavin
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enzyme is a iron-sulfur flavoenzyme
FMN
-
determined by HPLC or fluorometrically, molar ratio of cofactor to enzyme: 1
NAD(P)H
-
-
NADP+
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binding mechanism and structure
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Fe2+
-
enzyme is a iron-sulfur flavoenzyme
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3-furan-2-yl-acrylyl-CoA
-
competitive, substrate analogue
albumin
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-
-
iodoacetic acid
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inhibition of 70-80% at concentration of 1 mM
lysine
-
slight inhibition
N-ethylmaleimide
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inhibition of 70-80% at concentration of 1 mM
pent-4-enoate
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inhibitory effect alleviated by clofibrate
additional information
-
NADH inhibits mitochondrial beta-oxidation, while acetyl-CoA has no effect
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Clofibrate
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0127
(2E,4E)-2,4-decadienoyl-CoA
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pH 7.4, 20C
0.0716
(2E,4E)-2,4-hexadienoyl-CoA
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pH 7.4, 20C
0.102 - 0.155
2,4,7,10,13,16,19-docosaheptaenoyl-CoA
0.006
2,4-decadienoyl-CoA
0.059 - 0.108
2,4-hexadienoyl-CoA
0.0062
2,4-trans-decadienoyl-CoA
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recombinant His-tagged truncated enzyme, pH 6.0, 22C
0.0265
2,4-trans-hexadienoyl-CoA
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recombinant His-tagged truncated enzyme, pH 6.0, 22C
0.0065
2-fluoro-trans-trans-2,4-octadienoyl-CoA
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recombinant His-tagged truncated wild-type enzyme, pH 6.0, 22C
0.0023
2-trans,4-trans-decadienoyl-CoA
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-
0.00046
2-trans,4-trans-hexadienoyl-CoA
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-
0.016
5-methyl-trans-trans-2,4-hexadienoyl-CoA
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recombinant His-tagged truncated wild-type enzyme, pH 6.0, 22C
0.00044 - 0.215
NADPH
0.0045 - 0.154
trans-trans-2,4-hexadienoyl-CoA
additional information
additional information
-
kinetics of oleoyl-CoA degradation in mitochondrial protein extract
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
16
2-trans,4-trans-decadienoyl-CoA
Escherichia coli
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-
2.1
2-trans,4-trans-hexadienoyl-CoA
Rattus norvegicus
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0.008 - 9.5
NADPH
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0015
mutant enzyme C334A/C337A, with 2-trans,4-trans-decadienoyl-CoA as substrate
0.00281
-
4-cis-decenoyl-CoA, NADPH, protein fraction virtually free of 2-enoyl-CoA reductase activity
0.003
-
2-trans,4-trans-decadienoyl-CoA, NADPH, muscle
0.0046
-
2-trans,4-cis-decadienoyl-CoA, NADPH, muscle
0.0067
mutant enzyme C337A, with 2-trans,4-trans-decadienoyl-CoA as substrate
0.007
mutant enzyme H252A, with 2-trans,4-trans-decadienoyl-CoA as substrate
0.0084
-
2-trans,4-trans-decadienoyl-CoA, NADPH, liver
0.00882
-
2-trans,4-trans-hexadienoyl-CoA, NADPH, protein fraction virtually free of 2-enoyl-CoA reductase activity
0.0124
-
trans-2-trans-4-hexedienoyl-CoA as a substrate
0.013
-
2-trans,4-cis-decadienoyl-CoA, NADPH, liver
0.0274
-
hexa-2,4-dienoyl-CoA, NADPH, normally fed
0.0331
-
trans-2-trans-4-hexedienoyl-CoA as a substrate, clofibrate-treated
0.0394
-
hexa-2,4-dienoyl-CoA, NADPH, fed soy-bean oil
0.0461
-
pent-2,4-dienoyl-CoA, NADPH, fed partially hydrogenated marine oils
0.0605
-
hexa-2,4-dienoyl-CoA, NADPH, fed partially hydrogenated marine oils
0.0895
-
pent-2,4-dienoyl-CoA, NADPH, fed partially hydrogenated marine oils
0.095
mutant enzyme E164A, with 2-trans,4-trans-decadienoyl-CoA as substrate
0.33
mutant enzyme H252A/Y166F, with 2-trans,4-trans-decadienoyl-CoA as substrate
0.5
-
reductase activity for wild-type and Decr-/- mice, the observed residual activity represents the activity of mitochondrial 2-enoyl thioester reductase, which functions in mitochondrial fatty acid synthesis and can also reduce 2,4-hexadienoyl-CoA in vitro
1.79
-
2,4-hexadienoyl-CoA, NADPH
2.02
mutant enzyme Y166F, with 2-trans,4-trans-decadienoyl-CoA as substrate
2.2
-
reductase activity measured in liver mitochondrial extract
2.6
-
reductase activity measured in muscle mitochondrial extract
3.9
-
2-trans,4-trans-decadienoyl-CoA, NADPH
4.1
-
2-trans,4-trans-decadienoyl-CoA, NADPH
7.21
-
purified recombinant truncated His-tagged enzyme, substrate 2,4-trans-hexadienoyl-CoA
7.54
wild type enzyme, with 2-trans,4-trans-decadienoyl-CoA as substrate
10.9
-
2-trans,4-trans-decadienoyl-CoA, NADPH
20
-
2-trans,4-trans-decadienoyl-CoA, NADPH
additional information
-
analysis of liver fatty acids after the mice are fasted for 24 h indicates that fasting has a minor effect on the lipid content of wild type liver, with an overall increase of 29% in the concentration of fatty acids, in Decr-/- mice, the overall concentration of fatty acids increases by 108% after fasting; Decr-/- mice show decreased blood glucose and elevated non-esterified fatty acids concentrations after fasting in comparison to wild type mice; fasting increases the total concentration of acylcarnitines by 2fold in wild type mice (567 nM), in Decr-/- mice, a markedly higher 9fold increase is observed (2150 nM); immunoblotting of mitochondrial extracts from liver, muscle and heart with an antibody against human DECR reveals a detectable signal from wild type mice, whereas no signal can be detected for homozygous null mutant mice; in Decr-/- mice, the overall concentration of fatty acids increases by 108% after fasting, the most profound changes between fasted wild type and Decr-/- mice are observed for the levels of palmitoleic acid (C16:1), oleic acid, linolenic acid (C18:3) and linoleic acid, which are 2.5- to 3.8fold higher in Decr-/- mice, in comparison to the fed state, the concentrations of monounsaturated fatty acids and polyunsaturated fatty acids increase by 288% and 254%, respectively; mitochondrial 2,4-dienoyl-CoA reductase activity in mice is indispensable for the complete oxidation of (poly)unsaturated fatty acids and for adaptation to metabolic stress; mitochondrial 2,4-dienoyl-CoA reductase deficiency in mice results in severe hypoglycemia with stress intolerance and unimpaired ketogenesis
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4
-
recombinant mutants E227A, E276A, D300A, and D117A
5
-
recombinant mutant E154A
7.4
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trans,trans-2,4-hexadienoyl-CoA + NADPH
8
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22
-
assay at room temperature
37
-
enzyme assay
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
source of the natural substrate 2-trans,4cis-decadienoylcarnitine
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30780
-
encoded by the gene pDCR, calculated from sequence of cDNA
31300
-
purified recombinant enzyme, encoded by the gene PDCR, calculated from sequence of cDNA, SDS-PAGE
32410
-
purified recombinant enzyme, electrospray ionization-mass spectrometry
69000
-
encoded by the oleate inducible gene SPS19, gel filtration
72550
-
purified recombinant enzyme, encoded by the gene fadH, SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 34000, recombinant truncated His-tagged enzyme, SDS-PAGE
homodimer
-
2 * 34000, SDS-PAGE
homotetramer
-
4 * 36066, immature monomer of the 120 kDa isoform, RT-PCR, PCR-fragment subcloned to pUC18, sequenced
tetramer
-
crystal structure
additional information
-
analytical ultracentrifugation analysis of purified pDCR reveals that the protein exists as a mixture of monomers, dimers, and tetramers in solution
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
the crystal structure of the ternary complex 2,4-dienoyl-CoA reductase-trans-2,trans-4-hexadienoyl-CoA-NADP+ reveals that the carbonyl oxygen of the substrate accepts a hydrogen bond from general acid Y199 and also N148
-
15 mg/ml purified recombinant enzyme, hanging drop vapour diffusion method, reservoir solution: 30% PEG 5000 monomethyl ether, 0.2 M sodium acetate, 0.1 M ammonium sulfate, 0.1 M 3-(N-morpholino)ethane sulfonic acid, pH 6.5, precipitant solution: 18% PEG 5000 monomethyl ether, 180 mM sodium acetate, 90 mM ammonium sulfate, 90 mM 3-(N-morpholino)ethane sulfonic acid, mixture in a ratio 1:1.5, 1 week, no cryoprotection, X-ray diffraction structure determination and analysis at 2.2 A resolution, heavy atom derivatives
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the crystal structure of a ternary complex of peroxisomal 2,4-dienoyl CoA reductases (pDCR) with hexadienoyl CoA and NADP is described. The structure of pDCR refined to 1.84 A resolution reveals the absence of the tyrosine-serine pair seen in the active site of mitochondrial DCR. Instead, aspartate hydrogen-bonded to the Calpha hydroxyl via a water molecule perturbs the water molecule for protonation of the substrate
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wild-type and selenomethionine enzyme, 0.001 ml of protein and of reservoir solution, the latter containing 16% PEG 4000 w/v, 0.18 M ammonium sulfate, 80 mM sodium acetate, pH 4.6, 20% glycerol, addition of 30% ethylene glycol and 4 mM NADP+ for the binary complex of enzyme with NADP+, and 120 mM substrate for the ternary complex of enzyme with NADP+ and substrate trans-trans-2,4-dienoyl-CoA, X-ray diffraction structure determination and analysis at 2.1 A and 1.75 A resolution, respectively
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 7.5
-
stable at 40C for 10 min
390708
8
-
activity loss about 50%
390708
9
-
total loss of activity
390708
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22
-
purified recombinant truncated enzyme is highly stable at room temperature
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80C, purified recombinant truncated enzyme, completely stable for at least 6 months
-
22C, room temperature, purified recombinant truncated enzyme, 70% remaining activity after 1 week
-
4C, purified recombinant truncated enzyme, completely stable for 1 week
-
sensitive to freezing, activity loss upon storage on ice
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
affinity chromatography
-
dye-ligand chromatography, general ligand affinity-chromatography
-
gel filtration
-
gel filtration, DEAE-cellulose column chromatography, affinity chromatography
-
ion-exchange and affinity chromatography
-
ion-exchange chromatography
-
ion-exchange chromatography or dye-ligand chromatography, affinity chromatography
-
metal ion affinity chromatography
-
Ni-NTA chromatography
-
NTA-Ni2+ agarose column chromatography
partial, solubilization of enzyme using Triton X-100 from heart mitochondria
-
recombinant enzyme from strain BL21(DE3) via DEAE ion exchange and affinity chromatography
-
recombinant His-tagged truncated enzyme from Escherichia coli strain BL21(DE3) by one-step nickel affinity chromatography, to over 95% purity
-
recombinant His-tagged truncated wild-type and of mutant enzymes from Escherichia coli strain BL21(DE3) by one-step nickel affinity chromatography, to over 95% purity
-
recombinant wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, to homogeneity
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
creation of a DECR-deficient mouse line, fasted Decr-/- mice display increased serum acylcarnitines, especially decadienoylcarnitine, a product of the incomplete oxidation of linoleic acid (C18:2), urinary excretion of unsaturated dicarboxylic acids, and hepatic steatosis, wherein unsaturated fatty acids accumulate in liver triacylglycerols, metabolically challenged Decr-/- mice turn on ketogenesis, but unexpectedly develop hypoglycemia
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expressed in Escehrichia coli as a His-tagged fusion protein
-
expressed in Escherichia coli
expressed in Escherichia coli BL21 cells
expression in strain BL21(DE3)
-
functional overexpression of truncated His-tagged enzyme in Escherichia coli strain BL21(DE3)
-
overexpression of His-tagged truncated wild-type and of mutant enzymes in Escherichia coli strain BL21(DE3), expression as soluble protein, except for mutant D117A
-
overexpression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3), expression of selenomethionine enzyme in Escherichia coli strain B834(DE3)
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression of 2,4-dienoyl-CoA reductase is up-regulated in pancreas of alcohol-fed rats
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C334A/C337A
the mutation exhibits 0.02% of wild type activity
C337A
the mutation results in the loss of most of the iron and acid-labile sulfur and exhibits 0.09% of wild type activity
E164A
mutant exhibits 1.5% of the wild type activity
H252A
the mutation exhibits 0.09% of wild type activity
H252F
mutant is inactive
Y166F
mutant exhibits 27% of the wild type activity, however, the product of the reduction is 3-enoyl-CoA instead of 2-enoyl-CoA
Y166F/E164Q
double mutant is inactive
Y166F/H252A
the double mutation exhibits 4.4% of the wild type activity
D117A
-
site-directed mutagenesis, mutant is expressed in inclusion bodies and cannot be refolded to a functional enzyme after extraction from inclusion bodies with 8 M urea as denatured protein
D137A
-
relative activity: 3.32% (substrate: 2,4-decadienoyl CoA), 1.27% (substrate: 2,4-hexadienoyl CoA) (wild-type: 100%)
D155A
-
relative activity: 36.3% (substrate: 2,4-decadienoyl CoA), 59.6% (substrate: 2,4-hexadienoyl CoA) (wild-type: 100%)
D186A
-
relative activity: 6.21% (substrate: 2,4-decadienoyl CoA), 1.86% (substrate: 2,4-hexadienoyl CoA) (wild-type: 100%)
D268A
-
relative activity: 2.75% (substrate: 2,4-decadienoyl CoA), 1.14% (substrate: 2,4-hexadienoyl CoA) (wild-type: 100%)
D300A
-
site-directed mutagenesis, reduced activity and altered kinetics compared to the wild-type enzyme
D86A
-
relative activity: 1.70% (substrate: 2,4-decadienoyl CoA), 1.76% (substrate: 2,4-hexadienoyl CoA) (wild-type: 100%)
E154A
-
site-directed mutagenesis, reduced activity and altered kinetics compared to the wild-type enzyme
E215A
-
relative activity: 28.9% (substrate: 2,4-decadienoyl CoA), 7.59% (substrate: 2,4-hexadienoyl CoA) (wild-type: 100%)
E227A
-
site-directed mutagenesis, reduced activity and altered kinetics compared to the wild-type enzyme
E276A
-
site-directed mutagenesis, reduced activity and altered kinetics compared to the wild-type enzyme
E310A
-
site-directed mutagenesis, effects on reaction mechanism
E310Q
-
site-directed mutagenesis, effects on reaction mechanism
K214A
-
site-directed mutagenesis, effects on reaction mechanism
N148A
-
site-directed mutagenesis, effects on reaction mechanism
S210A
-
site-directed mutagenesis, effects on reaction mechanism
T197A
-
site-directed mutagenesis, effects on reaction mechanism
Y199A
-
site-directed mutagenesis, effects on reaction mechanism
additional information
Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
mutant D117A is expressed in inclusion bodies and cannot be refolded to a functional enzyme after extraction from inclusion bodies with 8 M urea as denatured protein
-
Show AA Sequence (2348 entries)
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