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
4.2.1.17
-
RECOMMENDED NAME
GeneOntology No.
enoyl-CoA hydratase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl-CoA + H2O
show the reaction diagram
-
-
-
-
(3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl-CoA + H2O
show the reaction diagram
reaction mechanism, overview
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
elimination
-
-
-
-
hydration
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
2-methylbutyrate biosynthesis
-
-
4-coumarate degradation (anaerobic)
-
-
4-hydroxybenzoate biosynthesis V
-
-
adipate degradation
-
-
alanine metabolism
-
-
alpha-Linolenic acid metabolism
-
-
Aminobenzoate degradation
-
-
Benzoate degradation
-
-
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 (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
-
-
Microbial metabolism in diverse environments
-
-
phenylacetate degradation I (aerobic)
-
-
Phenylalanine metabolism
-
-
Propanoate metabolism
-
-
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.
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2-enoyl-CoA hydratase
-
-
-
-
2-octenoyl coenzyme A hydrase
-
-
-
-
acyl coenzyme A hydrase
-
-
-
-
beta-hydroxyacid dehydrase
-
-
-
-
beta-hydroxyacyl-CoA dehydrase
-
-
-
-
crotonase
-
-
-
-
crotonyl hydrase
-
-
-
-
D-3-hydroxyacyl-CoA dehydratase
-
-
-
-
ECH
-
-
-
-
enol-CoA hydratase
-
-
-
-
Enoyl coenzyme A hydrase (D)
-
-
-
-
enoyl coenzyme A hydrase (L)
-
-
-
-
enoyl coenzyme A hydratase
-
-
-
-
enoyl hydrase
-
-
-
-
hydratase, enoyl coenzyme A
-
-
-
-
SCEH
-
-
-
-
short chain enoyl coenzyme A hydratase
-
-
-
-
short-chain enoyl-CoA hydratase
-
-
-
-
trans-2-enoyl-CoA hydratase
-
-
-
-
unsaturated acyl-CoA hydratase
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
9027-13-8
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene fadB or ysiB
-
-
Manually annotated by BRENDA team
Bacillus subtilis 168
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
the classification is ambiguous because the stereochemistry of the reaction product is not exactly determined
-
-
Manually annotated by BRENDA team
gene paaF encoded in the paa gene cluster
UniProt
Manually annotated by BRENDA team
LS6749, enoyl-CoA hydratase and L-3-hydroxyacyl-CoA dehydrogenase are located on the same polypeptide, encoded by the fadB gene. 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
the classification is ambiguous because the stereochemistry is not exactly determined
-
-
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
Escherichia coli B.
strain B. The classification is ambiguous because the stereochemistry of the reaction product is not exactly determined
-
-
Manually annotated by BRENDA team
the classification is ambiguous because the stereochemistry is not exactly determined
SwissProt
Manually annotated by BRENDA team
Metallosphaera sedula DSMZ 5348
-
-
-
Manually annotated by BRENDA team
subsp. paratuberculosis, gene echA12 2 or MAP1197
-
-
Manually annotated by BRENDA team
Mycobacterium avium ATCC19698
subsp. paratuberculosis, gene echA12 2 or MAP1197
-
-
Manually annotated by BRENDA team
gene dspI or PA14_54640 (PA0745)
UniProt
Manually annotated by BRENDA team
gene paaF encoded in the paa gene cluster
-
-
Manually annotated by BRENDA team
strain KCTC1639, gene phaJ
-
-
Manually annotated by BRENDA team
Pseudomonas putida KCTC1639
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
recombinant
-
-
Manually annotated by BRENDA team
recombinant enzyme
-
-
Manually annotated by BRENDA team
the classification is ambiguous because the stereochemistry is not exactly determined
UniProt
Manually annotated by BRENDA team
the classification is ambiguous because the stereochemistry is not exactly determined
-
-
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
LITERATURE
malfunction
-
siRNA-mediated knockdown of ECHS1 in the murine hepatocyte cell line alpha mouse liver 12 demonstrate increased cellular lipid accumulation induced by free fatty acid overload. Administering ECHS1 siRNA specifically reduces the expression of ECHS1 protein in mice liver, which significantly exacerbates the hepatic steatosis induced by an high fat diet
malfunction
-
Ech1 shRNA interference decreases Hca-F cell proliferation and the in situ adhesive capacity of Hca-F cells to lymph nodes, phenotype, overview
malfunction
Q9I5I4
inactivation of dspI abolishes biofilm dispersion autoinduction in continuous cultures of Pseudommonas aeruginosa and results in biofilms that are significantly greater in thickness and biomass compared to the parental wild-type strain. But dispersion can be induced in dspI mutants by the exogenous addition of synthetic cis-2-decenoic acid or by complementation of DELTAdspI in trans under the control of an arabinose-inducible promoter
metabolism
-
the human mitochondrial trifunctional protein enoyl-CoA hydratase is a multienzyme complex involved in fatty acid beta-oxidation. The pathway shows feed-back inhibition, overview
metabolism
Q9ZPJ5
two multifunctional peroxisomal isozymes, MFP2 and AIM1, both with 2-trans-enoyl-CoA hydratase and L-3-hydroxyacyl-CoA dehydrogenase activities, function in Arabidopsis thaliana peroxisomal beta-oxidation, where fatty acids are degraded by the sequential removal of two carbon units
metabolism
-
the enzyme catalyzes a reaction of the beta-oxidation, overview
metabolism
P76082
the enzyme catalyzes a reaction step of the beta-oxidation, as part of the catabolic gene cluster for phenylacetate degradation, overview
metabolism
-
the enzyme catalyzes a reaction step of the beta-oxidation, overview
physiological function
P07896
the multifunctional enzyme is involved in an alpha-methylacyl-CoAracemase-MFE2 independent synthesis pathway of bile acids from (24S)-hydroxyoxisterols, is involved in the beta-oxidation of long chain dicarboxylic acids
physiological function
-
FadRBs or YsiA is a transcriptional regulatory protein which negatively regulates the expression of beta-oxidation genes including those belonging to the lcfA operon, including fadRBs or ysiA. FadBBs is active in the hydratation of crotonyl-CoA, supporting the possibility of its direct involvement in the beta-oxidation pathway
physiological function
-
recombinant enoyl-CoA hydratase displays 2-enoyl-CoA hydratase, L-3-hydroxyacyl-CoA dehydrogenase, EC 1.1.1.35, and 3-ketoacyl-CoA thiolase, EC 2.3.1.16, activities
physiological function
Q9SE41
enoyl-CoA hydratase is one of the enzymes involved in the peroxisomal beta-oxidation cycle
physiological function
Q9I5I4
the enzyme is responsible for catalyzing the formation of alpha,beta-unsaturated fatty acids and dspI is essential for production of cis-2-decenoic acid, and it is required for synthesis of the biofilm dispersion autoinducer cis-2-decenoic acid in the human pathogen Pseudomonas aeruginosa. Expression of dspI is correlated with cell density during planktonic and biofilm growth
physiological function
Bacillus subtilis 168
-
FadRBs or YsiA is a transcriptional regulatory protein which negatively regulates the expression of beta-oxidation genes including those belonging to the lcfA operon, including fadRBs or ysiA. FadBBs is active in the hydratation of crotonyl-CoA, supporting the possibility of its direct involvement in the beta-oxidation pathway
-
metabolism
-
the enzyme catalyzes a reaction step of the beta-oxidation, overview
-
additional information
-
key role of ECHS1 and PRDX3 in regulation of 4-amino-5-(4-chlorophenyl)-7-(t-butyl)pyrazolo[3,4-d]pyrimidine, PP2, -induced apoptosis, downregulation of ECHS1 and PRDX3 potentiates PP2-induced apoptosis in MCF-7 cells, overview
additional information
Q9SE41
identification of residues involved in the ligand-enzyme interaction, homology modeling: the carbonyl group of hexadienoyl-CoA forms H-bonds with Ala32, Gly34, Val36 and Gly83. Phosphate groups of the substrate form two ionic bonds with Arg28. The enzyme shows few distinct structural changes which include structural variation in the mobile loop, formation and loss of certain interactions between the active site residues and substrates. AMECH is a monofunctional enzyme and has one catalytic glutamic acid Glu106, an essential catalytic residue. Asp114 might also be involved in the reaction mechanism, overview
additional information
Q9I5I4
transcript abundance of dspI correlates with cell density
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
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)-enoyl-CoA + H2O
(3S)-hydroxyacyl-CoA
show the reaction diagram
P07896
2E-enoyl-CoA is the product of the DELTA3,DELTA2-enoyl-CoA isomerase (EC 5.3.3.8) reaction, which subsequently is converted into (3S)-hydroxyacyl-CoA in the hydration step
-
-
?
(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
Q9ZPJ5
-
-
-
?
(S)-3-hydroxybutyryl-CoA
crotonoyl-CoA + H2O
show the reaction diagram
Metallosphaera sedula, Metallosphaera sedula DSMZ 5348
-
-
-
-
r
(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
-
-
-
-
r
2,3-dehydroadipyl-CoA + H2O
3-hydroxyadipyl-CoA
show the reaction diagram
P76082
-
-
-
r
2,3-dehydroadipyl-CoA + H2O
3-hydroxyadipyl-CoA
show the reaction diagram
-
substrate and product identification by mass spectrometry
-
-
r
2,3-dehydroadipyl-CoA + H2O
3-hydroxyadipyl-CoA
show the reaction diagram
P76082
substrate and product identification by mass spectrometry
-
-
r
2,3-dehydroadipyl-CoA + H2O
3-hydroxyadipyl-CoA
show the reaction diagram
-
substrate and product identification by mass spectrometry
-
-
r
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
-
2,3-octadienoyl-CoA is an intermediate. The classification is ambiguous because the stereochemistry is not exactly determined
-
-
?
3-octynoyl-CoA + H2O
3-ketooctanoyl-CoA
show the reaction diagram
-
reaction of ECH1, ECH2 is inactivated by the compound, it is possible that 3-octynoyl-CoA is isomerized to reactive 2,3-octadienoyl-CoA, overview
-
-
?
crotonoyl-CoA + H2O
(S)-3-hydroxybutyryl-CoA
show the reaction diagram
Metallosphaera sedula, Metallosphaera sedula DSMZ 5348
-
-
-
-
r
crotonyl-CoA + H2O
(3S)-3-hydroxybutanoyl-CoA
show the reaction diagram
-
-
-
-
?
crotonyl-CoA + H2O
(3S)-3-hydroxybutanoyl-CoA
show the reaction diagram
-
-
-
-
?
crotonyl-CoA + H2O
(3S)-3-hydroxybutanoyl-CoA
show the reaction diagram
-
-
-
-
r
crotonyl-CoA + H2O
(3S)-3-hydroxybutanoyl-CoA
show the reaction diagram
-
i.e. (E)-2-butenoyl-CoA. The reaction proceeds via the syn addition of water and thus the pro-2R proton of (3S)-hydroxybutyryl-CoA is derived from solvent. The equilibrium constant for the hydration of trans-2-crotonyl-CoA to (3S)-hydroxybutyryl-CoA is 7.5. The rate of 3(R)-hydroxybutyryl-CoA formation is 400000fold slower than the normal hydration reaction (of crotonyl-CoA to (3S)-3-hydroxybutanoyl-CoA) but at least 1600000fold faster than the non-enzyme-catalyzed reaction. Formation of the incorrect stereoisomer likely occurs via syn addition of water to the incorrect face of the trans-2-crotonyl-CoA double bond. The absolute stereospecificity for the enzyme-catalyzed reaction is 1 in 400000. To account for the exchange of the hydroxybutyryl pro-2S proton, the enzyme must also catalyze the dehydration of 3(R)-hydroxybutyryl-CoA to cis-2-crotonyl-CoA. Thus, the enzyme is capable of catalyzing the epimerization of hydroxybutyryl-CoA
-
-
r
crotonyl-CoA + H2O
(3S)-3-hydroxybutanoyl-CoA
show the reaction diagram
-
two enoyl coenzyme A hydrases ocur in Rhodospirillum rubrum extracts whose combined activity results in the racemization of (3S)-3-hydroxybutanoyl-CoA to (3R)-3-hydroxybutanoyl-CoA. Both hydrases catalyze the reversible hydration of crotonyl coenzyme A to 3-hydroxybutanoyl coenzyme A. One of the hydrases is specific for the synthesis of the (3S)-isomer (enoyl coenzyme A hydrase (D)) while the other catalyzes the synthesis of the (3R)-isomer (enoyl coenzyme A hydratase (L))
-
-
r
crotonyl-CoA + H2O
(3S)-3-hydroxybutanoyl-CoA
show the reaction diagram
-
as active as trans-decenoyl-CoA
-
-
?
crotonyl-CoA + H2O
(3S)-3-hydroxybutanoyl-CoA
show the reaction diagram
-
i.e. (E)-2-butenoyl-CoA. Reaction is catalyzed with a stereospecificity of 1 in 400000. The enzyme catalyzes the rapid interconversion of substrate and the (3S)-3-hydroxybutanoyl-CoA product relative to the rate of (3R)-3-hydroxybutanoyl-CoA formation. Formation of the correct product enantiomer requires an intact oxyanion hole and optimal positioning of the substrate with respect to two catalytic glutamates (E144 and E164) in the active site
-
-
r
crotonyl-CoA + H2O
(3S)-3-hydroxybutanoyl-CoA
show the reaction diagram
-
i.e. (E)-2-butenoyl-CoA. The reaction proceeds via the syn addition of water and thus the pro-2R proton of (3S)-hydroxybutyryl-CoA is derived from solvent. The equilibrium constant for the hydration of trans-2-crotonyl-CoA to (3S)-hydroxybutyryl-CoA is 7.5. The rate of 3(R)-hydroxybutyryl-CoA formation is 400000fold slower than the normal hydration reaction (of crotonyl-CoA to (3S)-3-hydroxybutanoyl-CoA) but at least 1600000fold faster than the non-enzyme-catalyzed reaction. Formation of the incorrect stereoisomer likely occurs via syn addition of water to the incorrect face of the trans-2-crotonyl-CoA double bond. The absolute stereospecificity for the enzyme-catalyzed reaction is 1 in 400000
-
-
r
crotonyl-CoA + H2O
(3S)-3-hydroxybutanoyl-CoA
show the reaction diagram
-
ratio of hydration rates trans-2-decenoyl-CoA/crotonyl-CoA is 0.29
-
-
r
crotonyl-CoA + H2O
(3S)-3-hydroxybutanoyl-CoA
show the reaction diagram
-
two enoyl coenzyme A hydrases occur in Rhodospirillum rubrum extracts whose combined activity results in the racemization of (3S)-3-hydroxybutanoyl-CoA to (3R)-3-hydroxybutanoyl-CoA. Both hydrases catalyze the reversible hydration of crotonyl-CoA to 3-hydroxybutanoyl-CoA. One of the hydrases is specific for the synthesis of the (3S)-isomer (enoyl coenzyme A hydrase (D)) while the other catalyzes the synthesis of the (3R)-isomer (enoyl coenzyme A hydratase (L))
-
-
r
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
?
show the reaction diagram
-
best substrate. The classification is ambiguous because the stereochemistry is not exactly determined
-
-
?
crotonyl-CoA + H2O
?
show the reaction diagram
-
best substrate. The classification is ambiguous because the stereochemistry is not exactly determined
-
-
?
crotonyl-CoA + H2O
?
show the reaction diagram
-
the classification is ambiguous because the stereochemistry is not exactly determined
-
-
?
crotonyl-CoA + H2O
?
show the reaction diagram
-
the classification is ambiguous because the stereochemistry is not exactly determined
-
-
?
crotonyl-CoA + H2O
?
show the reaction diagram
-
the classification is ambiguous because the stereochemistry is not exactly determined, The binding shows a moderate dependence on ionic strength (2-200 mM) and pH (6.5-8)
-
-
?
crotonyl-CoA + H2O
?
show the reaction diagram
Escherichia coli B.
-
the classification is ambiguous because the stereochemistry is not exactly determined
-
-
?
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
-
17% of the activity with crotonyl-CoA. The classification is ambiguous because the stereochemistry is not exactly determined
-
-
?
decenoyl-CoA + H2O
?
show the reaction diagram
-
the classification is ambiguous because the stereochemistry is not exactly determined
-
-
?
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
(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
P14604
-
-
-
?
trans-2-decenoyl-CoA + H2O
(3S)-hydroxydecanoyl-CoA
show the reaction diagram
-
-
-
-
?
trans-2-decenoyl-CoA + H2O
(3S)-hydroxydecanoyl-CoA
show the reaction diagram
-
ratio of hydration rates trans-2-decenoyl-CoA/crotonyl-CoA is 0.29
-
-
r
trans-2-decenoyl-CoA + H2O
(3S)-hydroxydecanoyl-CoA
show the reaction diagram
-
Vmax is 8fold lower than with crotonyl-CoA
-
-
?
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-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
P14604
-
-
-
?
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
-
-
?
hexenoyl-CoA + H2O
?
show the reaction diagram
-
67% of the activity with crotonyl-CoA. The classification is ambiguous because the stereochemistry is not exactly determined
-
-
?
additional information
?
-
-
biosynthetic pathway of medium-chain-length polyhydroxyalkanoates
-
-
-
additional information
?
-
-
ECH catalyzes the reversible syn-addition of a water molecule across the double bond of a trans-2-enoyl-CoA, e.g. crotonyl-CoA, thioester to give a beta-hydroxyacyl-CoA thioester. The enzyme binds the substrates at the interface between monomers within the same trimer
-
-
-
additional information
?
-
-
In eukaryotes, ECH2 is a 31 kDa integral part of multifunctional protein-2, MFP-2, also called multifunctional enzyme 2, D-bifunctional enzyme, or 17-beta-estradiol dehydrogenase type IV. The MFP-2 plays a central role in peroxisomal beta-oxidation as it handles most peroxisomal beta-oxidation substrates, the beta-oxidation in mitochondria involves a (3S)-hydroxyacyl-CoA intermediate, while the beta-oxidation in peroxisomes has a (3R)-hydroxyacyl-CoA intermediate. The enzymes responsible for the formation of these two different intermediates are enoyl-CoA hydratase 1 (ECH1) in mitochondria and enoyl-CoA hydratase 2 (ECH2) in peroxisomes
-
-
-
additional information
?
-
P30084
the enzyme catalyzes the second step of the mitochondrial fatty acid beta-oxidation spiral
-
-
-
additional information
?
-
-
ECH (XI) also has enoyl-CoA isomerase activity at approximately 1/5000 the level of its hydratase activity, overview
-
-
-
additional information
?
-
-
the enzyme also catalyzes DELTA3-DELTA2-isomerization of trans-3-hexenoyl-CoA
-
-
-
additional information
?
-
-
catalysis by enoyl-CoA hydratase involves two glutamic acid residues at the active site, which are part of a hydrogen bonding network with the molecule of water that is added to the CdC.17 The C-2 deuteron is transferred by a glutamic acid residue acting as a Bronsted general acid. Buffer effect on the stereoselectivity of protonation of an enolate anion with a Bronsted acid that, overview
-
-
-
additional information
?
-
-
stereoselectivity of 2-enoyl-CoA dehydratase
-
-
-
additional information
?
-
-
recombinant TFP interacts strongly with cardiolipin and phosphatidylcholine
-
-
-
additional information
?
-
Q9ZPJ5
substrates are enoyl-CoA chains of C4-C14, neither AtMFP2 nor AtAIM1 efficiently degrade enoyl chains longer than C14-CoA, substrate specificity in vitro with 2-trans-enoyl-CoA substrates, AIM perfers th C4 substrate, while MFE2 prefers the C8 substrate, overview
-
-
-
additional information
?
-
-
(3R)-3-hydroxyacyl-CoA is a peroxisomal specific intermediate, development and evaluation of a quantitative product separation method by a chiral column chromatography, overview
-
-
-
additional information
?
-
-
development of a chiral high-performance liquid chromatography-tandem mass spectrometry method for analysis of stereospecificity of enoyl-coenzyme A hydratases/isomerases, including reaction of the 3-hydroxyl group on the chiral carbon with 3,5-dimethylphenyl isocyanate, resolving of the resulting urethane derivatives, and monitoring of the liberated free hydroxy fatty acid fragment ion, detailed overview
-
-
-
additional information
?
-
Bacillus subtilis 168
-
stereoselectivity of 2-enoyl-CoA dehydratase
-
-
-
additional information
?
-
Pseudomonas putida KCTC1639
-
biosynthetic pathway of medium-chain-length polyhydroxyalkanoates
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
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
Metallosphaera sedula, Metallosphaera sedula DSMZ 5348
-
-
-
-
r
(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
-
-
-
-
r
2,3-dehydroadipyl-CoA + H2O
3-hydroxyadipyl-CoA
show the reaction diagram
P76082
-
-
-
r
2,3-dehydroadipyl-CoA + H2O
3-hydroxyadipyl-CoA
show the reaction diagram
-
-
-
-
r
crotonoyl-CoA + H2O
(S)-3-hydroxybutyryl-CoA
show the reaction diagram
Metallosphaera sedula, Metallosphaera sedula DSMZ 5348
-
-
-
-
r
crotonyl-CoA + H2O
(3S)-3-hydroxybutanoyl-CoA
show the reaction diagram
-
i.e. (E)-2-butenoyl-CoA. The reaction proceeds via the syn addition of water and thus the pro-2R proton of (3S)-hydroxybutyryl-CoA is derived from solvent. The equilibrium constant for the hydration of trans-2-crotonyl-CoA to (3S)-hydroxybutyryl-CoA is 7.5. The rate of 3(R)-hydroxybutyryl-CoA formation is 400000fold slower than the normal hydration reaction (of crotonyl-CoA to (3S)-3-hydroxybutanoyl-CoA) but at least 1600000fold faster than the non-enzyme-catalyzed reaction. Formation of the incorrect stereoisomer likely occurs via syn addition of water to the incorrect face of the trans-2-crotonyl-CoA double bond. The absolute stereospecificity for the enzyme-catalyzed reaction is 1 in 400000. To account for the exchange of the hydroxybutyryl pro-2S proton, the enzyme must also catalyze the dehydration of 3(R)-hydroxybutyryl-CoA to cis-2-crotonyl-CoA. Thus, the enzyme is capable of catalyzing the epimerization of hydroxybutyryl-CoA
-
-
r
crotonyl-CoA + H2O
(3S)-3-hydroxybutanoyl-CoA
show the reaction diagram
-
two enoyl coenzyme A hydrases ocur in Rhodospirillum rubrum extracts whose combined activity results in the racemization of (3S)-3-hydroxybutanoyl-CoA to (3R)-3-hydroxybutanoyl-CoA. Both hydrases catalyze the reversible hydration of crotonyl coenzyme A to 3-hydroxybutanoyl coenzyme A. One of the hydrases is specific for the synthesis of the (3S)-isomer (enoyl coenzyme A hydrase (D)) while the other catalyzes the synthesis of the (3R)-isomer (enoyl coenzyme A hydratase (L))
-
-
r
additional information
?
-
-
biosynthetic pathway of medium-chain-length polyhydroxyalkanoates
-
-
-
additional information
?
-
-
ECH catalyzes the reversible syn-addition of a water molecule across the double bond of a trans-2-enoyl-CoA, e.g. crotonyl-CoA, thioester to give a beta-hydroxyacyl-CoA thioester. The enzyme binds the substrates at the interface between monomers within the same trimer
-
-
-
additional information
?
-
-
In eukaryotes, ECH2 is a 31 kDa integral part of multifunctional protein-2, MFP-2, also called multifunctional enzyme 2, D-bifunctional enzyme, or 17-beta-estradiol dehydrogenase type IV. The MFP-2 plays a central role in peroxisomal beta-oxidation as it handles most peroxisomal beta-oxidation substrates, the beta-oxidation in mitochondria involves a (3S)-hydroxyacyl-CoA intermediate, while the beta-oxidation in peroxisomes has a (3R)-hydroxyacyl-CoA intermediate. The enzymes responsible for the formation of these two different intermediates are enoyl-CoA hydratase 1 (ECH1) in mitochondria and enoyl-CoA hydratase 2 (ECH2) in peroxisomes
-
-
-
additional information
?
-
P30084
the enzyme catalyzes the second step of the mitochondrial fatty acid beta-oxidation spiral
-
-
-
additional information
?
-
-
catalysis by enoyl-CoA hydratase involves two glutamic acid residues at the active site, which are part of a hydrogen bonding network with the molecule of water that is added to the CdC.17 The C-2 deuteron is transferred by a glutamic acid residue acting as a Bronsted general acid. Buffer effect on the stereoselectivity of protonation of an enolate anion with a Bronsted acid that, overview
-
-
-
additional information
?
-
-
stereoselectivity of 2-enoyl-CoA dehydratase
-
-
-
additional information
?
-
-
(3R)-3-hydroxyacyl-CoA is a peroxisomal specific intermediate
-
-
-
additional information
?
-
Bacillus subtilis 168
-
stereoselectivity of 2-enoyl-CoA dehydratase
-
-
-
additional information
?
-
Pseudomonas putida KCTC1639
-
biosynthetic pathway of medium-chain-length polyhydroxyalkanoates
-
-
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
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
-
enolate form of acetoacetyl-CoA acts as a competitive inhibitor. 6 molecules of inhibitor are bound per molecule of enzyme
acetoacetyl-CoA
-
-
acetoacetyl-CoA
-
-
acetoacetyl-CoA
Q9SE41
competitive inhibitor, binding structure, overview
decenoyl-CoA
-
-
hexadecenoyl-CoA
-
-
hexenoyl-CoA
-
-
iodoacetamide
-
10 mM, 20 min, 20% inhibition
NEM
-
10 mM, 19% inhibition. 5 mM, 13% inhibition
Octanoyl-CoA
-
-
Octanoyl-CoA
Q9SE41
competitive inhibitor, binding structure, overview
p-chloromercuribenzoate
-
1 mM, complete inhibition. 0.1 mM, 11% 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
additional information
-
no inhibition by hexenoyl-CoA
-
additional information
-
no inhibition: ethyl acetoacetate, acetoacetate
-
additional information
-
3-octynoyl-CoA is not an inhibitor of enoyl-CoA hydratase 1
-
additional information
-
the enzyme is controlled by feed-back inhibition, overview
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
CoA
-
the enzyme is dependent on CoA
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.06
(S)-3-hydroxybutyryl-CoA
-
at pH 7.0 and 70C
0.05
(Z)-2-butenoyl-CoA
-
pH 7.4, 25C
-
0.008
2-decenoyl-CoA
-
-
0.118
3'-dephosphocrotonyl-CoA
-
pH 7.4, 25C, mutant enzyme E144D
0.07
crotonoyl-CoA
-
at pH 7.0 and 70C
0.003
crotonyl-CoA
-
pH 7.4, 25C, mutant enzyme G141P
0.013
crotonyl-CoA
-
pH 9.0
0.015
crotonyl-CoA
-
pH 7.4, 25C, wild-type enzyme
0.022
crotonyl-CoA
-
pH 8, 25C
0.025
crotonyl-CoA
-
pH 7.4, 25C, mutant enzyme E144Q
0.03
crotonyl-CoA
-
25C
0.032
crotonyl-CoA
-
pH 7.4, 25C, mutant enzyme E164D
0.041
crotonyl-CoA
-
pH 7.4, 25C, mutant enzyme E164Q
0.0499
crotonyl-CoA
-
pH 8.0, 22C, wild-type enzyme
0.05
crotonyl-CoA
-
-
0.05
crotonyl-CoA
-
-
0.195
crotonyl-CoA
-
pH 7.4, 25C, mutant enzyme A98P
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
-
25C
0.029
oct-2-enoyl-CoA
-
pH 9.0
0.0025
trans-2-decenoyl-CoA
-
pH 8.0, 22C, mutant enzyme E144A/Q162L
0.0029
trans-2-decenoyl-CoA
-
pH 8.0, 22C, mutant enzyme Q162A
0.003
trans-2-decenoyl-CoA
-
pH 8.0, 22C, mutant enzyme E144A
0.0039
trans-2-decenoyl-CoA
-
pH 8.0, 22C, wild-type enzyme
0.005
trans-2-decenoyl-CoA
-
pH 8.0, 22C, mutant enzyme Q162L
0.0052
trans-2-decenoyl-CoA
-
pH 8.0, 22C, mutant enzyme E164A
0.0063
trans-2-decenoyl-CoA
-
pH 8.0, 22C, mutant enzyme Q162M
0.009
trans-2-hexadecanoyl-CoA
-
pH 8, 25C
-
0.0143
trans-2-Hexenoyl-CoA
-
pH 8.0, 22C, mutant enzyme Q162A
0.0152
trans-2-Hexenoyl-CoA
-
pH 8.0, 22C, mutant enzyme E144A
0.021
trans-2-Hexenoyl-CoA
-
pH 8.0, 22C, mutant enzyme E144A/Q162L
0.0229
trans-2-Hexenoyl-CoA
-
pH 8.0, 22C, mutant enzyme Q162M
0.024
trans-2-Hexenoyl-CoA
-
pH 8.0, 22C, mutant enzyme E164A
0.025
trans-2-Hexenoyl-CoA
-
pH 8.0, 22C, wild-type enzyme
0.027
trans-2-Hexenoyl-CoA
-
pH 8.0, 22C, mutant enzyme Q162L
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
15
(S)-3-hydroxybutyryl-CoA
-
at pH 7.0 and 70C
152
(Z)-2-butenoyl-CoA
-
pH 7.4, 25C
-
26
3'-dephosphocrotonyl-CoA
-
pH 7.4, 25C, mutant enzyme E144D
19
crotonoyl-CoA
-
at pH 7.0 and 70C
0.0011
crotonyl-CoA
-
pH 7.4, 25C, mutant enzyme G141P
0.0053
crotonyl-CoA
-
pH 7.4, 25C, mutant enzyme E164Q
0.53
crotonyl-CoA
-
pH 7.4, 25C, mutant enzyme A98P
0.6
crotonyl-CoA
-
pH 7.4, 25C, mutant enzyme E144Q
1.5
crotonyl-CoA
-
pH 7.4, 25C, mutant enzyme E164D
1790
crotonyl-CoA
-
pH 7.4, 25C, wild-type enzyme
1790
crotonyl-CoA
-
-
2238
crotonyl-CoA
-
pH 8.0, 22C, wild-type enzyme
5667
crotonyl-CoA
-
pH 7.5, 25C
0.0121
trans-2-decenoyl-CoA
-
pH 8.0, 22C, mutant enzyme E144A/Q162L
0.085
trans-2-decenoyl-CoA
-
pH 8.0, 22C, mutant enzyme E144A
0.095
trans-2-decenoyl-CoA
-
pH 8.0, 22C, mutant enzyme E164A
104
trans-2-decenoyl-CoA
-
pH 8.0, 22C, mutant enzyme Q162A
164
trans-2-decenoyl-CoA
-
pH 8.0, 22C, mutant enzyme Q162M
174
trans-2-decenoyl-CoA
-
pH 8.0, 22C, mutant enzyme Q162L
203
trans-2-decenoyl-CoA
-
pH 8.0, 22C, wild-type enzyme
0.06
trans-2-Hexenoyl-CoA
-
pH 8.0, 22C, mutant enzyme E144A/Q162L
0.43
trans-2-Hexenoyl-CoA
-
pH 8.0, 22C, mutant enzyme E144A
0.44
trans-2-Hexenoyl-CoA
-
pH 8.0, 22C, mutant enzyme E164A
180
trans-2-Hexenoyl-CoA
-
pH 8
561
trans-2-Hexenoyl-CoA
-
pH 8.0, 22C, mutant enzyme Q162L
601
trans-2-Hexenoyl-CoA
-
pH 8.0, 22C, mutant enzyme Q162M
607
trans-2-Hexenoyl-CoA
-
pH 8.0, 22C, mutant enzyme Q162A
745
trans-2-Hexenoyl-CoA
-
pH 8.0, 22C, wild-type enzyme
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
260
(S)-3-hydroxybutyryl-CoA
-
at pH 7.0 and 70C
4305
260
crotonoyl-CoA
-
at pH 7.0 and 70C
3806
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.037
(3S)-hydroxybutanoyl-CoA
-
pH 8, 25C
0.00035
(3S)-hydroxyhexadecanoyl-CoA
-
pH 8, 25C
0.041
(R)-methylenecyclopropylformyl-CoA
-
25C, ECH2
0.047
(R)-methylenecyclopropylformyl-CoA
-
25C, ECH1
0.049
(R)-methylenecyclopropylformyl-CoA
-
25C, ECH1
0.0492
(R)-methylenecyclopropylformyl-CoA
-
25C
0.053
(S)-methylenecyclopropylformyl-CoA
-
25C, ECH2
0.0571
(S)-methylenecyclopropylformyl-CoA
-
25C
0.065
3-octynoyl-CoA
-
ECH2
0.0016
acetoacetyl-CoA
-
pH 7.5, 25C
0.014
acetoacetyl-CoA
-
pH 8.0, due to the binding of the enolate form of acetoacetyl-CoA the Ki-value should be highly pH-dependent
0.0003
decenoyl-CoA
-
pH 7.5, 25C
0.0004
dodecenoyl-CoA
-
pH 7.5, 25C
0.0005
hexadecenoyl-CoA
-
pH 7.5, 25C
0.00024
hexenoyl-CoA
-
pH 7.5, 25C
0.00028
octenoyl-CoA
-
pH 7.5, 25C
0.00042
tetradecenoyl-CoA
-
pH 7.5, 25C
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
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
-
intrinsic activity compared to overexpressing strain activity, overview
additional information
Q9ZPJ5
2-enoyl-CoA substrate specificity of MFE2 and AIM, overview
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.4
-
assay at
7.5
-
assay at
8
-
assay at
8.5
-
-
8.5
Q9ZPJ5
assay at
9
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
22
-
assay at
25
-
assay at
27
Q9ZPJ5
assay at
37
-
assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
a hepatocarcinoma cell line. Expression of Ech1 is upregulated in the Hca-F cell line
Manually annotated by BRENDA team
additional information
Q9I5I4
high expression levels of dspI in planktonic and biofilm cells
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Bacillus subtilis (strain 168)
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)
Mycobacterium abscessus (strain ATCC 19977 / DSM 44196)
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)
Novosphingobium aromaticivorans (strain DSM 12444 / F199)
Novosphingobium aromaticivorans (strain DSM 12444 / F199)
Polaromonas sp. (strain JS666 / ATCC BAA-500)
Ralstonia metallidurans (strain CH34 / ATCC 43123 / DSM 2839)
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
LITERATURE
155000
-
non-denaturing PAGE
5866
158000
-
equilibrium sedimentation analysis, gel filtration
33729
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
2207
460000
-
about, enoyl-CoA hydratase complex, gel filtration
714222
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
700005
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 420000, + x * 78000, two subunits are present in equimolar amounts, multienzyme complex of fatty acid oxidation: EC 4.2.1.17/EC1.1.1.35/EC 2.3.1.16/EC 5.1.2.3/EC 5.3.3.3, SDS-PAGE
?
Escherichia coli B.
-
x * 420000, + x * 78000, two subunits are present in equimolar amounts, multienzyme complex of fatty acid oxidation: EC 4.2.1.17/EC1.1.1.35/EC 2.3.1.16/EC 5.1.2.3/EC 5.3.3.3, SDS-PAGE
-
hexamer
-
-
hexamer
-
6 * 27300, SDS-PAGE
hexamer
-
6 * 161000, the hexamer is a dimer of trimers
hexamer
-
mitochondrial ECH1 that exists as a hexamer
oligomer
-
x * 79014, alpha-subunit, + x * 49291, beta-subunit, mass spectrometry and gel filtration
tetramer
-
4 * 40000, SDS-PAGE
homodimer
-
ECH2 exists as a homodimer in its crystal structure
additional information
-
perMFE-1 can be divided into ve separate domains or parts
additional information
-
the enzyme binds the substrates at the interface between monomers within the same trimer, monomer structure, modelling in comparison to other crotonase superfamily enzymes, overview
additional information
-
the alpha and beta subunits of the human mitochondrial trifunctional protein enoyl-CoA hydratase are part of the multienzyme complex, with predominance of alpha2beta2 and alpha4beta4 complexes, with higher order oligomers
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
lipoprotein
-
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 contains phospholipid
lipoprotein
-
63 nmol of lipid phosphate per mg of protein, phosphatidylethanolamine, phosphatidylglycerol, cardiolipin. 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 contains phospholipid
lipoprotein
Escherichia coli B.
-
63 nmol of lipid phosphate per mg of protein, phosphatidylethanolamine, phosphatidylglycerol, cardiolipin. 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 contains phospholipid
-
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
Q9ZPJ5
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
P07896
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
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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
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structure of enoyl-Coenzyme A (CoA) hydratase, co-crystallised with the inhibitor octanoyl-CoA, refined at a resolution of 2.4 A
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
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
730242
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
Q9ZPJ5
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
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recombinant alpha- and His-tagged beta-subunits from Escherichia coli by nickel affinity chromatography to homogeneity
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Q-Sepharose column chromatography and Superdex 200 gel filtration
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refolded recombinant N-terminally His-tagged enzyme expresssed in Escherichia coli by nickel affinity chromatography
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purified from rat liver
P07896
recombinant
-
recombinant enzyme
-
recombinant His6-tagged truncated ECH2 mutant enzyme
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recombinant, wild-type and mutant enzymes
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
Q9ZPJ5
expression of recombinant His6-tagged FadB from pET21b-fadBBs in Escherichia coli strain BL21(DE3)
-
-
P30084
co-expression of His-tagged alpha- and beta-subunits in Escherichia coli strain Rosetta-2(DE3)
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expressed in Escherichia coli Rosetta 2 (DE3) cells
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gene echA12 2, DNA and amino acid sequence determination and analysis, overexpression of N-terminally His-tagged enzyme in Escherichia coli in inclusion bodies
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gene dspI, quantitative reverse transcriptase PCR expression analysis. Gene dspI is co-transcribed with the upstream genes PA14_54620 and PA14_54630
Q9I5I4
gene phaJ, overexpression in strain KCTC1639 leads to oversupplementation with (R)-3-hydroxyalkanoate monomers and increased biosynthesis of medium-chain-length polyhydroxyalkanoate
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expressed in Escherichia coli BL21
-
expressed in Escherichis coli BL21(DE3)
P07896
expression in Pichia pastoris
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expression of a His6-tagged truncated ECH2 mutant enzyme
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
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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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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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A98P
-
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
-
kcat for trans-2-hexenoyl-CoA is 1733fold lower than wild-type value
E144A
-
site-directed mutagenesis, the mutant shows a 1000fold reduced activity compared to the wild-type enzyme
E144A/Q162L
-
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
-
60fold decreases in kcat with little change in KM
E144Q
-
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
E164A
-
kcat for trans-2-hexenoyl-CoA is 1709fold lower than wild-type value
E164A
-
site-directed mutagenesis, the mutant shows a 1000fold reduced activity compared to the wild-type enzyme
E164D
-
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
-
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
Q162A
-
kcat for trans-2-hexenoyl-CoA is nearly identical to wild-type value
Q162L
-
kcat for trans-2-hexenoyl-CoA is nearly identical to wild-type value
Q162M
-
kcat for trans-2-hexenoyl-CoA is nearly identical to wild-type value
additional information
Q9I5I4
generation of a deletion mutant strain DELTAdspI, functional complementation of DELTAdspI, overview
G141P
-
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
additional information
-
experiments with engineered perMFE-1 variants demonstrate that the H1/I competence of domain A requires stabilizing interactions with domains D and E. The variant His-perMFE (residues 288-79)DELTA, in which the domain C is deleted, is stable and has hydratase-1 activity
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
LITERATURE
medicine
-
ECHS1 down-regulation contributes to high-fat diet-induced hepatic steatosis