Information on EC 4.2.1.17 - enoyl-CoA hydratase

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

EC NUMBER
COMMENTARY hide
4.2.1.17
-
RECOMMENDED NAME
GeneOntology No.
enoyl-CoA hydratase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl-CoA + H2O
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
addition
-
-
double bond; of H2O to carbon carbon double bond
-
elimination
-
-
-
-
hydration
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
(4Z,7Z,10Z,13Z,16Z)-docosa-4,7,10,13,16-pentaenoate biosynthesis (6-desaturase)
-
-
(8E,10E)-dodeca-8,10-dienol biosynthesis
-
-
2-methylbutanoate biosynthesis
-
-
4-coumarate degradation (anaerobic)
-
-
4-hydroxybenzoate biosynthesis V
-
-
adipate degradation
-
-
alanine metabolism
-
-
alpha-Linolenic acid metabolism
-
-
Aminobenzoate degradation
-
-
Benzoate degradation
-
-
benzoyl-CoA degradation I (aerobic)
-
-
beta-Alanine metabolism
-
-
Biosynthesis of antibiotics
-
-
Biosynthesis of secondary metabolites
-
-
Biosynthesis of unsaturated fatty acids
-
-
Butanoate metabolism
-
-
Caprolactam degradation
-
-
Carbon fixation pathways in prokaryotes
-
-
docosahexaenoate biosynthesis III (6-desaturase, mammals)
-
-
fatty acid beta-oxidation I
-
-
fatty acid beta-oxidation II (peroxisome)
-
-
fatty acid beta-oxidation VI (peroxisome)
-
-
Fatty acid degradation
-
-
Fatty acid elongation
-
-
fatty acid salvage
-
-
Geraniol degradation
-
-
jasmonic acid biosynthesis
-
-
L-isoleucine degradation I
-
-
L-valine degradation I
-
-
Limonene and pinene degradation
-
-
lipid metabolism
-
-
Lysine degradation
-
-
Metabolic pathways
-
-
methyl ketone biosynthesis (engineered)
-
-
Microbial metabolism in diverse environments
-
-
oleate beta-oxidation
-
-
phenylacetate degradation I (aerobic)
-
-
Phenylalanine metabolism
-
-
Propanoate metabolism
-
-
pyruvate fermentation to hexanol (engineered)
-
-
Spodoptera littoralis pheromone biosynthesis
-
-
toluene degradation to benzoyl-CoA (anaerobic)
-
-
Tryptophan metabolism
-
-
unsaturated, even numbered fatty acid beta-oxidation
-
-
valine metabolism
-
-
Valine, leucine and isoleucine degradation
-
-
SYSTEMATIC NAME
IUBMB Comments
(3S)-3-hydroxyacyl-CoA hydro-lyase
Acts in the reverse direction. With cis-compounds, yields (3R)-3-hydroxyacyl-CoA. cf. EC 4.2.1.74 long-chain-enoyl-CoA hydratase.
CAS REGISTRY NUMBER
COMMENTARY hide
9027-13-8
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
gene fadB or ysiB
-
-
Manually annotated by BRENDA team
gene fadB or ysiB
-
-
Manually annotated by BRENDA team
the classification is ambiguous because the stereochemistry of the reaction product is not exactly determined
-
-
Manually annotated by BRENDA team
strain B. The classification is ambiguous because the stereochemistry of the reaction product is not exactly determined
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
subsp. paratuberculosis, gene echA12 2 or MAP1197
-
-
Manually annotated by BRENDA team
subsp. paratuberculosis, gene echA12 2 or MAP1197
-
-
Manually annotated by BRENDA team
strain KCTC1639, gene phaJ
-
-
Manually annotated by BRENDA team
gene paaF encoded in the paa gene cluster
-
-
Manually annotated by BRENDA team
gene paaF encoded in the paa gene cluster
-
-
Manually annotated by BRENDA team
the classification is ambiguous because the stereochemistry of the reaction product is not exactly determined
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(2E)-5-methylhexa-2,4-dienoyl-CoA + H2O
3-hydroxy-5-methylhex-4-enoyl-CoA
show the reaction diagram
(2E)-enoyl-CoA + H2O
(3S)-hydroxyacyl-CoA
show the reaction diagram
(2E)-octenoyl-CoA + H2O
?
show the reaction diagram
-
36% of the activity with crotonyl-CoA. The classification is ambiguous because the stereochemistry is not exactly determined
-
-
?
(3S)-3-hydroxyacyl-CoA
(E)-2(or 3)-enoyl-CoA + H2O
show the reaction diagram
-
-
-
?
(S)-3-hydroxybutyryl-CoA
crotonoyl-CoA + H2O
show the reaction diagram
(Z)-2-butenoyl-CoA + H2O
(3R)-3-hydroxybutanoyl-CoA
show the reaction diagram
-
kcat is 12fold slower than with the trans-iosmer crotonyl-CoA
-
-
?
2 trans-2-decenoyl-CoA + 2 H2O
(3S)-3-hydroxydecanoyl-CoA + (3R)-3-hydroxydecanoyl-CoA
show the reaction diagram
-
Pseudomonas aeruginosa enzyme activity is of both the ECH-1 and ECH-2 type
R- and S-enantiomers of produced 3-hydroxydecanoate are nearly equally abundant in case of Pseudomonas aeruginosa
-
?
2,3-dehydroadipyl-CoA + H2O
3-hydroxyadipyl-CoA
show the reaction diagram
2,3-octadienoyl-CoA + H2O
3-ketooctanoyl-CoA
show the reaction diagram
-
the classification is ambiguous because the stereochemistry is not exactly determined
-
-
?
2-trans-octenoyl-CoA + H2O
3-hydroxyoctanoyl-CoA
show the reaction diagram
-
the classification is ambiguous because the stereochemistry is not exactly determined
-
-
?
3'-dephosphocrotonyl-CoA + H2O
?
show the reaction diagram
-
-
-
-
?
3-octynoyl-CoA + H2O
3-ketooctanoyl-CoA
show the reaction diagram
crotonoyl-CoA + H2O
(S)-3-hydroxybutyryl-CoA
show the reaction diagram
crotonyl-CoA + H2O
(3S)-3-hydroxyacyl-CoA
show the reaction diagram
-
stereoselective reaction mechanism, Glu144 and Glu164 are essential for ECH catalysis, overview
-
-
?
crotonyl-CoA + H2O
(3S)-3-hydroxybutanoyl-CoA
show the reaction diagram
crotonyl-CoA + H2O
?
show the reaction diagram
dec-2-enoyl-CoA + H2O
?
show the reaction diagram
-
32% of the activity with crotonyl-CoA. The classification is ambiguous because the stereochemistry is not exactly determined
-
-
?
decenoyl-CoA + H2O
?
show the reaction diagram
dodec-2-enoyl-CoA + H2O
?
show the reaction diagram
-
9.6% of the activity with crotonyl-CoA. The classification is ambiguous because the stereochemistry is not exactly determined
-
-
?
dodecenoyl-CoA + H2O
?
show the reaction diagram
-
7% of the activity with crotonyl-CoA. The classification is ambiguous because the stereochemistry is not exactly determined
-
-
?
hex-2-enoyl-CoA + H2O
?
show the reaction diagram
-
77% of the activity with crotonyl-CoA. The classification is ambiguous because the stereochemistry is not exactly determined
-
-
?
hexadec-2-enoyl-CoA + H2O
?
show the reaction diagram
-
2.4% of the activity with crotonyl-CoA. The classification is ambiguous because the stereochemistry is not exactly determined
-
-
?
hexadecenoyl-CoA + H2O
?
show the reaction diagram
-
1% of the activity with crotonyl-CoA. The classification is ambiguous because the stereochemistry is not exactly determined
-
-
?
hexenoyl-CoA + H2O
?
show the reaction diagram
oct-2-enoyl-CoA + H2O
?
show the reaction diagram
-
54% of the activity with crotonyl-CoA. The classification is ambiguous because the stereochemistry is not exactly determined
-
-
?
tetradecenoyl-CoA + H2O
?
show the reaction diagram
-
2% of the activity with crotonyl-CoA. The classification is ambiguous because the stereochemistry is not exactly determined
-
-
?
trans-2-decenoyl-CoA + H2O
(3R)-3-hydroxydecanoyl-CoA
show the reaction diagram
-
Escherichia coli enzyme activity is of the S-specific ECH-1 type
the distribution of R- and S-enantiomers of produced 3-hydroxydecanoate is in favour of the S-enantiomer in case of Escherichia coli
-
?
trans-2-decenoyl-CoA + H2O
(3S)-3-hydroxydecanoyl-CoA
show the reaction diagram
-
Escherichia coli enzyme activity is of the S-specific ECH-1 type
the distribution of R- and S-enantiomers of produced 3-hydroxydecanoate is in favour of the S-enantiomer in case of Escherichia coli
-
?
trans-2-decenoyl-CoA + H2O
(3S)-hydroxydecanoyl-CoA
show the reaction diagram
trans-2-hexadecanoyl-CoA + H2O
(3S)-hydroxyhexadecanoyl-CoA
show the reaction diagram
-
Vmax is 82fold lower than with crotonyl-CoA
-
-
?
trans-2-hexadecenoyl-CoA + H2O
(3S)-3-hydroxyhexadecanoyl-CoA + (3R)-3-hydroxyhexadecanoyl-CoA
show the reaction diagram
-
rat liver homogenate enzyme activity is (S)-specific
(3S)-3-hydroxyhexadecanoyl-CoA is the dominant product
-
?
trans-2-hexenoyl-CoA + H2O
(3S)-3-hydroxyhexanoyl-CoA
show the reaction diagram
trans-decenoyl-CoA + H2O
?
show the reaction diagram
-
as active as crotonyl-CoA
-
-
?
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
(2E)-5-methylhexa-2,4-dienoyl-CoA + H2O
3-hydroxy-5-methylhex-4-enoyl-CoA
show the reaction diagram
(3S)-3-hydroxyacyl-CoA
(E)-2(or 3)-enoyl-CoA + H2O
show the reaction diagram
Q9ZPJ5
-
-
-
?
(S)-3-hydroxybutyryl-CoA
crotonoyl-CoA + H2O
show the reaction diagram
(Z)-2-butenoyl-CoA + H2O
(3R)-3-hydroxybutanoyl-CoA
show the reaction diagram
-
kcat is 12fold slower than with the trans-iosmer crotonyl-CoA
-
-
?
2,3-dehydroadipyl-CoA + H2O
3-hydroxyadipyl-CoA
show the reaction diagram
crotonoyl-CoA + H2O
(S)-3-hydroxybutyryl-CoA
show the reaction diagram
crotonyl-CoA + H2O
(3S)-3-hydroxybutanoyl-CoA
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(3S)-hydroxybutanoyl-CoA
-
competitive
(3S)-hydroxyhexadecanoyl-CoA
-
competitive, 50% inhibition at 0.00075 mM, 90% inhibition by 0.004 mM
(R)-methylenecyclopropylformyl-CoA
-
methylenecyclopropylformyl-CoA is a better inhibitor for enoyl-CoA hydratase 2 than for enoyl-CoA hydratase 1
(S)-methylenecyclopropylformyl-CoA
-
methylenecyclopropylformyl-CoA is a better inhibitor for enoyl-CoA hydratase 2 than for enoyl-CoA hydratase 1
3-ketohexadecanoyl-CoA
-
0.008 mM, 40% inhibition
3-octynoyl-CoA
-
irreversibly inactivates only enoyl-CoA hydratase 2, the catalytic residue Glu47 is covalently labeled by the inhibitor
acetoacetyl-CoA
decenoyl-CoA
-
-
hexadecenoyl-CoA
-
-
hexenoyl-CoA
-
-
iodoacetamide
-
10 mM, 20 min, 20% inhibition
methylenecyclopropylformyl-CoA
-
a metabolite derived from a natural amino acid, (methylenecyclopropyl)glycine, that inactivates enoyl-CoA hydratase 1 and enoyl-CoA hydratase 2. Competence of (R)- and (S)-MCPF-CoA to inactivate the ECH2 and kinetic analysis, enzye-inhibitor complex structures, mass spectrometric analysis, inhbition mechanism, overview
NEM
-
10 mM, 19% inhibition. 5 mM, 13% inhibition
Octanoyl-CoA
p-chloromercuribenzoate
-
1 mM, complete inhibition. 0.1 mM, 11% inhibition
additional information
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
CoA
-
the enzyme is dependent on CoA
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.06
(S)-3-hydroxybutyryl-CoA
-
at pH 7.0 and 70°C
0.05
(Z)-2-butenoyl-CoA
-
pH 7.4, 25°C
-
0.008
2-decenoyl-CoA
-
-
0.118
3'-dephosphocrotonyl-CoA
-
pH 7.4, 25°C, mutant enzyme E144D
0.07
crotonoyl-CoA
-
at pH 7.0 and 70°C
0.003 - 0.195
crotonyl-CoA
0.029
dec-2-enoyl-CoA
-
pH 9.0
0.03
dodec-2-enoyl-CoA
-
pH 9.0
0.029
hex-2-enoyl-CoA
-
pH 9.0
0.03
hexadec-2-enoyl-CoA
-
pH 9.0
-
0.13
hexenoyl-CoA
-
25°C
0.029
oct-2-enoyl-CoA
-
pH 9.0
0.0025 - 0.0063
trans-2-decenoyl-CoA
0.009
trans-2-hexadecanoyl-CoA
-
pH 8, 25°C
-
0.0143 - 0.027
trans-2-hexenoyl-CoA
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
15
(S)-3-hydroxybutyryl-CoA
Metallosphaera sedula
-
at pH 7.0 and 70°C
152
(Z)-2-butenoyl-CoA
Rattus norvegicus
-
pH 7.4, 25°C
-
26
3'-dephosphocrotonyl-CoA
Rattus norvegicus
-
pH 7.4, 25°C, mutant enzyme E144D
19
crotonoyl-CoA
Metallosphaera sedula
-
at pH 7.0 and 70°C
0.0011 - 5667
crotonyl-CoA
0.0121 - 203
trans-2-decenoyl-CoA
0.06 - 745
trans-2-hexenoyl-CoA
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
260
(S)-3-hydroxybutyryl-CoA
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.037
(3S)-hydroxybutanoyl-CoA
-
pH 8, 25°C
0.00035
(3S)-hydroxyhexadecanoyl-CoA
-
pH 8, 25°C
0.041 - 0.0492
(R)-methylenecyclopropylformyl-CoA
0.053 - 0.0571
(S)-methylenecyclopropylformyl-CoA
0.065
3-octynoyl-CoA
-
ECH2
0.0016 - 0.014
acetoacetyl-CoA
0.0003
decenoyl-CoA
-
pH 7.5, 25°C
0.0004
dodecenoyl-CoA
-
pH 7.5, 25°C
0.0005
hexadecenoyl-CoA
-
pH 7.5, 25°C
0.00024
hexenoyl-CoA
-
pH 7.5, 25°C
0.00028
octenoyl-CoA
-
pH 7.5, 25°C
0.00042
tetradecenoyl-CoA
-
pH 7.5, 25°C
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
64
-
homogenate of cells transformed with the pET3aECH1 expression vector
420
-
hydration of 3-octynoyl-CoA
650
-
hydration of 2,3-octadienoyl-CoA
973
-
hydration of 2-trans-octenoyl-CoA
1334
-
-
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.4
-
assay at
7.5
-
assay at
9
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22
-
assay at
37
-
assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
a hepatocarcinoma cell line. Expression of Ech1 is upregulated in the Hca-F cell line
Manually annotated by BRENDA team
additional information
high expression levels of dspI in planktonic and biofilm cells
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
UNIPROT
Bacillus subtilis (strain 168)
Cupriavidus metallidurans (strain ATCC 43123 / DSM 2839 / NBRC 102507 / CH34)
Escherichia coli (strain K12)
Geobacillus kaustophilus (strain HTA426)
Geobacillus kaustophilus (strain HTA426)
Hyphomonas neptunium (strain ATCC 15444)
Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC 33152 / DSM 7513)
Mycobacterium abscessus (strain ATCC 19977 / DSM 44196 / CIP 104536 / JCM 13569 / NCTC 13031 / TMC 1543)
Mycobacterium abscessus (strain ATCC 19977 / DSM 44196 / CIP 104536 / JCM 13569 / NCTC 13031 / TMC 1543)
Mycobacterium marinum (strain ATCC BAA-535 / M)
Mycobacterium paratuberculosis (strain ATCC BAA-968 / K-10)
Mycobacterium paratuberculosis (strain ATCC BAA-968 / K-10)
Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155)
Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155)
Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155)
Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155)
Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155)
Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Novosphingobium aromaticivorans (strain DSM 12444 / F199)
Novosphingobium aromaticivorans (strain DSM 12444 / F199)
Polaromonas sp. (strain JS666 / ATCC BAA-500)
Rhodobacter sphaeroides (strain ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158)
Thermobifida fusca (strain YX)
Thermobifida fusca (strain YX)
Thermobifida fusca (strain YX)
Thermoplasma volcanium (strain ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
155000
-
non-denaturing PAGE
158000
-
equilibrium sedimentation analysis, gel filtration
160000
-
multienzyme complex of fatty acid oxidation: EC 4.2.1.17/EC 1.1.1.35/EC2.3.1.16/EC 5.1.2.3/EC 5.3.3.3, gel filtration, non-denaturing PAGE
460000
-
about, enoyl-CoA hydratase complex, gel filtration
additional information
-
MW of multienzyme complex of fatty acid oxidation, EC 4.2.1.17/EC 1.1.1.35/EC 2.3.1.16/EC 5.1.2.3/EC 5.3.3.3: 270000-300000 Da
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexamer
homodimer
-
ECH2 exists as a homodimer in its crystal structure
oligomer
-
x * 79014, alpha-subunit, + x * 49291, beta-subunit, mass spectrometry and gel filtration
tetramer
-
4 * 40000, SDS-PAGE
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
lipoprotein
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
purified recombinant His-tagged wild-type and SeMet-labeled AtMFP2, X-ray diffraction structure determination and analysis at 2.5-2.7 A resolution
at 2.8 A resolution, multidomain protein having 5 domains: A, B, C, D, and E. The N-terminal part has a crotonase fold, which builds the active site for the DELTA3,DELTA2-enoyl-CoA isomerase (EC 5.3.3.8) and DELTA2-enoyl-CoA hydratase-1
hanging drop method, crystal structure of the enzyme complexed with the potent inhibitor acetoacetyl-CoA, refined at 2.5 A resolution. The active site architecture confirms the importance of Glu164 as the catalytic acid for providing the alpha-proton during the hydratase reaction. It also shows the importance of Glu144 as the catalytic base for the activation of a water molecule in the hydratase reaction
-
hanging drop method, structure of the mitochondrial enoyl-CoA hydratase, co-crystallised with the inhibitor octanoyl-CoA, refined at a resolution of 2.4 A
-
structure of enoyl-Coenzyme A (CoA) hydratase, co-crystallised with the inhibitor octanoyl-CoA, refined at a resolution of 2.4 A
-
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60
-
liver cell homogenate, 2 min, production of (3R)-3-hydroxyhexadecanoyl-CoA is remarkably decreased after heat treatment, while production of (3S)-3-hydroxyhexadecanoyl-CoA remains stable
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
multienzyme complex of fatty acid oxidation: EC4.2.1.17/EC1.1.1.35/EC2.3.1.16/EC5.1.2.3/EC5.3.3.3
-
purified from rat liver
Q-Sepharose column chromatography and Superdex 200 gel filtration
-
recombinant
-
recombinant alpha- and His-tagged beta-subunits from Escherichia coli by nickel affinity chromatography to homogeneity
-
recombinant enzyme
-
recombinant His-tagged wild-type and SeMet-labeled AtMFP2 from Escherichia coli strains BL21(DE3) and B834(DE3), respectively, by nickel affinity chromatography and gel filtration
recombinant His6-tagged truncated ECH2 mutant enzyme
-
recombinant, wild-type and mutant enzymes
-
refolded recombinant N-terminally His-tagged enzyme expresssed in Escherichia coli by nickel affinity chromatography
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
co-expression of His-tagged alpha- and beta-subunits in Escherichia coli strain Rosetta-2(DE3)
-
expressed in Escherichia coli BL21
-
expressed in Escherichia coli Rosetta 2 (DE3) cells
-
expressed in Escherichis coli BL21(DE3)
expression in Pichia pastoris
-
expression of a His6-tagged truncated ECH2 mutant enzyme
-
expression of recombinant His6-tagged FadB from pET21b-fadBBs in Escherichia coli strain BL21(DE3)
-
gene dspI, quantitative reverse transcriptase PCR expression analysis. Gene dspI is co-transcribed with the upstream genes PA14_54620 and PA14_54630
gene echA12 2, DNA and amino acid sequence determination and analysis, overexpression of N-terminally His-tagged enzyme in Escherichia coli in inclusion bodies
-
gene phaJ, overexpression in strain KCTC1639 leads to oversupplementation with (R)-3-hydroxyalkanoate monomers and increased biosynthesis of medium-chain-length polyhydroxyalkanoate
-
recombinant expression of His-tagged AtMFP2 in Escherichia coli strain BL21(DE3) for the wild-type enzyme, and in Escherichia coli strain B834(DE3) for the selenomethionine-labeled variant
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
a proteomic approach is applied to examine the effect of high fat diet on the liver proteome during the progression of nonalcoholic fatty liver disease. Male rats fed an high-fat diet for 4, 12, and 24 weeks show a reduced protein level of ECHS1
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ECHS1 expression level in patients with simple steatosis is reduced
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ECHS1 is downregulated by 4-amino-5-(4-chlorophenyl)-7-(t-butyl)pyrazolo[3,4-d]pyrimidine, i.e. PP2, that induces apoptosis in breast cancer MCF-7 cells
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A98P
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kcat is decreased 3400fold compared to wild type and KM is increased 13fold, mutant enzyme has a severely compromised ability for catalyzing the formation of (3R)-3-hydroxybutanoyl-CoA
E144A/Q162L
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kcat for trans-2-hexenoyl-CoA is 12417fold lower than wild-type value. The point mutations E144A and Q162L by themselves apparently do not cause structural rearrangements of the active site helix, but when both residues are changed, the active site geometry changes
E144D
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60fold decreases in kcat with little change in KM
E144Q
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3000fold decreases in kcat with little change in KM. The mutant is unable to catalyze the formation of (3R)-3-hydroxybutanoyl-CoA even when the incubation is extended to 4 days
E164D
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1200fold decreases in kcat with little change in KM. First-order rate constant for the formation of (3R)-3-hydroxybutanoyl-CoA is similar to wild-type value
E164Q
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340000fold decreases in kcat with little change in KM. While wild-type enoyl-CoA hydratase catalyzes the rapid interconversion of substrate and the (3S)-3-hydroxybutanoyl-CoA product relative to the rate of (3R)-3-hydroxybutanoyl-CoA formation, E164Q catalyzes the formation of both product enantiomers at similar rates
G141P
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1600000fold decrease in kcat with no change in KM, mutant enzyme has a severely compromised ability for catalyzing the formation of (3R)-3-hydroxybutanoyl-CoA
Q162A
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kcat for trans-2-hexenoyl-CoA is nearly identical to wild-type value
Q162L
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kcat for trans-2-hexenoyl-CoA is nearly identical to wild-type value
Q162M
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kcat for trans-2-hexenoyl-CoA is nearly identical to wild-type value
additional information
Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant N-terminally His-tagged enzyme from Escherichia coli inclusion bodies in 20 mM Tris-HCl, 500 mM NaCl, pH 7.5, by addition of 8 M urea and protease inhibitors
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
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