Information on EC 4.2.1.17 -

Information on EC 4.2.1.17 - enoyl-CoA hydratase:

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EC NUMBER	COMMENTARY
4.2.1.17	-

RECOMMENDED NAME	GeneOntology No.
enoyl-CoA hydratase	GO:0004300

REACTION	REACTION DIAGRAM	COMMENTARY	ORGANISM	UNIPROT ACCESSION NO.	LITERATURE
(3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl-CoA + H2O		-	-	-	-
(3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl-CoA + H2O		reaction mechanism, overview	Homo sapiens	-	715297

REACTION TYPE	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
addition	-	-	double bond; of H2O to carbon carbon double bond	-
elimination	-	-	-	-
hydration	-	-	-	-

PATHWAY	KEGG Link	MetaCyc Link
2-methylbutyrate biosynthesis	-	PWY-5109
4-coumarate degradation (anaerobic)	-	PWY-7046
4-hydroxybenzoate biosynthesis V	-	PWY-6435
fatty acid beta-oxidation I	-	FAO-PWY
fatty acid beta-oxidation II (peroxisome)	-	PWY-5136
fatty acid salvage	-	PWY-7094
isoleucine degradation I	-	ILEUDEG-PWY
jasmonic acid biosynthesis	-	PWY-735
methyl ketone biosynthesis	-	PWY-7007
phenylacetate degradation I (aerobic)	-	PWY0-321
unsaturated, even numbered fatty acid beta-oxidation	-	PWY-5138
valine degradation I	-	VALDEG-PWY

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 ACCESSION NO.	COMMENTARY	LITERATURE
(R)-specific 2-enoyl-CoA hydratase	Pseudomonas putida	-	-	693287
2,3-dehydroadipyl-CoA hydratase	Escherichia coli	P76082	-	716755
2,3-dehydroadipyl-CoA hydratase	Pseudomonas putida, Pseudomonas sp.	-	-	716755
2-enoyl-CoA hydratase	-	-	-	-
2-enoyl-CoA hydratase	Homo sapiens	-	-	714222
2-enoyl-CoA hydratase 1	Rattus norvegicus	-	-	684952
2-enoyl-CoA hydratase 1	Rattus norvegicus	-	is part of peroxisomal multifunctional enzyme perMFE-I together with L-specific 3-hydroxyacyl-CoA dehydrogenase (1.1.1.35)	696077
2-enoyl-CoA hydratase-1	Rattus norvegicus	-	-	649889
2-enoyl-hydratase 1	Rattus norvegicus	-	-	687485
2-octenoyl coenzyme A hydrase	-	-	-	-
4-hydroxybutyryl-CoA dehydratase	Clostridium aminobutyricum	-	-	695584
acyl coenzyme A hydrase	-	-	-	-
AIM1	Arabidopsis thaliana	Q9ZPJ5	-	715522
beta-hydroxyacid dehydrase	-	-	-	-
beta-hydroxyacyl-CoA dehydrase	-	-	-	-
classic 2-enoyl-CoA hydratase	Rattus norvegicus	-	-	687485
crotonase	-	-	-	-
crotonase	Sus scrofa	-	the classification is ambiguous because the stereochemistry of the reaction product is not exactly determined	33713, 5866
crotonase	Clostridium acetobutylicum	-	the classification is ambiguous because the stereochemistry of the reaction product is not exactly determined	33729
crotonase	Bos taurus	-	the classification is ambiguous because the stereochemistry is not exactly determined	33730
crotonase	Escherichia coli	-	the classification is ambiguous because the stereochemistry of the reaction product is not exactly determined	649591
crotonase	Rattus norvegicus	-	-	649889
crotonase	Escherichia coli	-	multienzyme of fatty acid oxidation contains in addition to enoyl-CoA hydratase, EC 1.1.1.35 (L-3-hydroxyacyl-CoA dehydrogenase), EC 2.3.1.16 (3-ketoacyl-CoA thiolase), EC 5.1.2.2 (3-hydroxyacyl-CoA epimerase) and EC 5.3.3.3 (DELTA3-cis-DELTA2-trans-enoyl-CoA isomerase)	700005
crotonyl hydrase	-	-	-	-
D-3-hydroxyacyl-CoA dehydratase	-	-	-	-
DELTA2-enoyl-CoA hydratase-1	Rattus norvegicus	P07896	-	704681
ECH	-	-	-	-
ECH	Rattus norvegicus	-	-	697212
ECH	Homo sapiens	-	-	714222
ECH1	Rattus norvegicus	-	-	689308
ECH1	Mus musculus	-	-	714400
ECH2	Rattus norvegicus	-	-	689308
ECHS1	Homo sapiens	-	-	702229, 715023
ECHS1	Mus musculus, Rattus norvegicus	-	-	702229
enol-CoA hydratase	-	-	-	-
Enoyl coenzyme A hydrase (D)	-	-	-	-
enoyl coenzyme A hydrase (L)	-	-	-	-
enoyl coenzyme A hydratase	-	-	-	-
enoyl coenzyme A hydratase (L)	Rhodospirillum rubrum	-	-	5792
enoyl coenzyme A hydratase 1	Mus musculus	-	-	714400
enoyl hydrase	-	-	-	-
enoyl-CoA hydratase	Rattus norvegicus	-	the classification is ambiguous because the stereochemistry is not exactly determined	33734, 699508
enoyl-CoA hydratase	Homo sapiens, Mus musculus, Rattus norvegicus	-	-	702229
enoyl-CoA hydratase	Pseudomonas aeruginosa, Pseudomonas citronellolis	-	-	717129
enoyl-CoA hydratase 1	Rattus norvegicus	-	-	689308
enoyl-CoA hydratase 2	Rattus norvegicus	-	-	689308
enoyl-CoA hydratase short chain 1	Homo sapiens	-	-	715023
FadRBs	Bacillus subtilis	-	-	713767
hydratase, enoyl coenzyme A	-	-	-	-
mECH-1	Rattus norvegicus	-	-	649889
MFP2	Arabidopsis thaliana	Q9ZPJ5	-	715522
mitochondrial enoyl coenzyme A hydratase	Rattus norvegicus	-	the classification is ambiguous because the stereochemistry is not exactly determined	697604
multifunctional enzyme type 1	Rattus norvegicus	-	-	649739
PaaF	Escherichia coli	P76082	-	716755
PaaF	Pseudomonas putida, Pseudomonas sp.	-	-	716755
perMFE-1	Rattus norvegicus	-	-	649739
perMFE-1	Rattus norvegicus	-	multifunctional enzyme, cf. 5.3.3.8 and EC 1.1.1.35, second multifunctional enzyme in rat liver peroxisome perMFE-2, cf. EC 4.2.1.107 and EC 4.2.1.119	684952
perMFE-I	Rattus norvegicus	-	peroxisomal multifunctional enzyme perMFE-I has 2-enoyl-CoA hydratase 1 activity (L-specific, EC 4.2.1.17) and L-specific 3-hydroxyacyl-CoA dehydrogenase (1.1.1.35) activity. Peroxisomal multifunctional enzyme perMFE-II has 2-enoyl-CoA hydratase 2 (D-specific) activity and D-specific 3-hydroxyacyl-CoA dehydrogenase (1.1.1.36) activity	696077
rat peroxisomal multifunctional enzyme type 1	Rattus norvegicus	P07896	-	704681
rpMFE1	Rattus norvegicus	P07896	-	704681
SCEH	-	-	-	-
SCEH	Homo sapiens	P30084	the classification is ambiguous because the stereochemistry is not exactly determined	697671
short chain enoyl coenzyme A hydratase	-	-	-	-
short-chain enoyl-CoA hydratase	-	-	-	-
trans-2-enoyl-CoA hydratase	-	-	-	-
unsaturated acyl-CoA hydratase	-	-	-	-
YsiA	Bacillus subtilis	-	-	713767
mitochondrial short-chain enoyl-CoA hydratase	Homo sapiens	P30084	the classification is ambiguous because the stereochemistry is not exactly determined	697671
additional information	Rattus norvegicus	-	crotonase superfamily enzyme	697212
additional information	Escherichia coli	P76082	PaaF is a member of the crotonase superfamily	716755
additional information	Pseudomonas putida, Pseudomonas sp.	-	PaaF is a member of the crotonase superfamily	716755

CAS REGISTRY NUMBER	COMMENTARY
9027-13-8	-

ORGANISM	COMMENTARY	LITERATURE	SEQUENCE CODE	SEQUENCE DB	SOURCE
Arabidopsis thaliana	-	715522	Q9ZPJ5	UniProt
Bacillus subtilis	gene fadB or ysiB	713767	-	-
Bos taurus	-	33718, 696477	-	-
Bos taurus	the classification is ambiguous because the stereochemistry of the reaction product is not exactly determined	33730	-	-
Clostridium acetobutylicum	the classification is ambiguous because the stereochemistry of the reaction product is not exactly determined	33729	-	-
Clostridium aminobutyricum	-	695584	-	-
Escherichia coli	gene paaF encoded in the paa gene cluster	716755	P76082	UniProt
Escherichia coli	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	2210	-	-
Escherichia coli	strain B. The classification is ambiguous because the stereochemistry of the reaction product is not exactly determined	2207	-	-
Escherichia coli	the classification is ambiguous because the stereochemistry is not exactly determined	649591	-	-
Escherichia coli	the classification is ambiguous because the stereochemistry of the reaction product is not exactly determined	700005	-	-
Escherichia coli B.	strain B. The classification is ambiguous because the stereochemistry of the reaction product is not exactly determined	2207	-	-
Homo sapiens	-	702229, 714222, 715023, 715297	-	-
Homo sapiens	the classification is ambiguous because the stereochemistry is not exactly determined	697671	P30084	SwissProt
Mus musculus	-	702229, 714400	-	-
Pseudomonas aeruginosa	-	717129	-	-
Pseudomonas citronellolis	-	717129	-	-
Pseudomonas putida	gene paaF encoded in the paa gene cluster	716755	-	-
Pseudomonas putida	strain KCTC1639, gene phaJ	693287	-	-
Pseudomonas putida KCTC1639	strain KCTC1639, gene phaJ	693287	-	-
Pseudomonas sp.	gene paaF encoded in the paa gene cluster	716755	-	-
Pseudomonas sp. Y2	gene paaF encoded in the paa gene cluster	716755	-	-
Rattus norvegicus	-	649739, 697212, 697690	P14604	UniProt
Rattus norvegicus	-	649889, 684952, 687485, 689308, 696077, 702229	-	-
Rattus norvegicus	-	704681	P07896	UniProt
Rattus norvegicus	recombinant	650113	-	-
Rattus norvegicus	recombinant enzyme	651567	-	-
Rattus norvegicus	the classification is ambiguous because the stereochemistry is not exactly determined	33734, 697604	P14604	UniProt
Rattus norvegicus	the classification is ambiguous because the stereochemistry is not exactly determined	699508	-	-
Rhodospirillum rubrum	-	5792	-	-
Sus scrofa	the classification is ambiguous because the stereochemistry of the reaction product is not exactly determined	33713, 5866	-	-

GENERAL INFORMATION	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
malfunction	Mus musculus	-	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	702229
malfunction	Mus musculus	-	Ech1 shRNA interference decreases Hca-F cell proliferation and the in situ adhesive capacity of Hca-F cells to lymph nodes, phenotype, overview	714400
metabolism	Homo sapiens	-	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	714222
metabolism	Arabidopsis thaliana	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	715522
metabolism	Escherichia coli	P76082	the enzyme catalyzes a reaction step of the beta-oxidation, as part of the catabolic gene cluster for phenylacetate degradation, overview	716755
metabolism	Pseudomonas putida, Pseudomonas sp.	-	the enzyme catalyzes a reaction step of the beta-oxidation, overview	716755
physiological function	Rattus norvegicus	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	704681
physiological function	Bacillus subtilis	-	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	713767
physiological function	Homo sapiens	-	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	714222
metabolism	Pseudomonas aeruginosa, Pseudomonas citronellolis	-	the enzyme catalyzes a reaction of the beta-oxidation, overview	717129
additional information	Homo sapiens	-	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	715023

SUBSTRATE	PRODUCT	REACTION DIAGRAM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY/ Substrate	LITERATURE/ Substrate	COMMENTARY/ Product	LITERATURE/ Product	Reversibility r=reversible ir=irreversible ?=not specified
(1S,3S)-3-hydroxycyclohexane carboxylate	cyclohex-1-ene carboxylate + H2O		Clostridium aminobutyricum	-	-	695584	-	-	?
(2E)-5-methylhexa-2,4-dienoyl-CoA + H2O	3-hydroxy-5-methylhex-4-enoyl-CoA		Pseudomonas aeruginosa, Pseudomonas citronellolis	-	-	717129	-	-	?
(2E)-enoyl-CoA + H2O	(3S)-hydroxyacyl-CoA		Rattus norvegicus	-	-	684952	-	-	?
(2E)-enoyl-CoA + H2O	(3S)-hydroxyacyl-CoA		Rattus norvegicus	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	704681	-	-	?
(3S)-3-hydroxyacyl-CoA	(E)-2(or 3)-enoyl-CoA + H2O		Arabidopsis thaliana	Q9ZPJ5	-	715522	-	-	?
(Z)-2-butenoyl-CoA + H2O	(3R)-3-hydroxybutanoyl-CoA		Rattus norvegicus	-	kcat is 12fold slower than with the trans-iosmer crotonyl-CoA	651567	-	-	?
2,3-dehydroadipyl-CoA + H2O	3-hydroxyadipyl-CoA		Pseudomonas sp., Pseudomonas putida	-	-	716755	-	-	r
2,3-dehydroadipyl-CoA + H2O	3-hydroxyadipyl-CoA		Escherichia coli	P76082	-	716755	-	-	r
2,3-dehydroadipyl-CoA + H2O	3-hydroxyadipyl-CoA		Pseudomonas sp., Pseudomonas putida	-	substrate and product identification by mass spectrometry	716755	-	-	r
2,3-dehydroadipyl-CoA + H2O	3-hydroxyadipyl-CoA		Escherichia coli	P76082	substrate and product identification by mass spectrometry	716755	-	-	r
2,3-octadienoyl-CoA + H2O	3-ketooctanoyl-CoA		Escherichia coli	-	the classification is ambiguous because the stereochemistry is not exactly determined	649591	-	-	?
2-trans-octenoyl-CoA + H2O	3-hydroxyoctanoyl-CoA		Escherichia coli	-	the classification is ambiguous because the stereochemistry is not exactly determined	649591	-	-	?
3'-dephosphocrotonyl-CoA + H2O	?		Rattus norvegicus	-	-	650113	-	-	?
3-octynoyl-CoA + H2O	3-ketooctanoyl-CoA		Escherichia coli	-	2,3-octadienoyl-CoA is an intermediate. The classification is ambiguous because the stereochemistry is not exactly determined	649591	-	-	?
3-octynoyl-CoA + H2O	3-ketooctanoyl-CoA		Rattus norvegicus	-	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	689308	-	-	?
4-hydroxybutyryl-CoA	crotonyl-CoA + H2O		Clostridium aminobutyricum	-	the 4-hydroxybutyryl-CoA dehydratase catalyzes the gamma-elimination of water and is also involved in the fifth CO2 fixation cycle, overview, mechanism for the dehydration of 4-hydroxybutyryl-CoA to crotonyl-CoA, overview	695584	-	-	?
crotonyl-CoA + H2O	(3S)-3-hydroxybutanoyl-CoA		Rattus norvegicus	-	-	649889	-	-	?
crotonyl-CoA + H2O	(3S)-3-hydroxybutanoyl-CoA		Bos taurus	-	-	33718	-	-	?
crotonyl-CoA + H2O	(3S)-3-hydroxybutanoyl-CoA		Bos taurus	-	-	696477	-	-	r
crotonyl-CoA + H2O	(3S)-3-hydroxybutanoyl-CoA		Rattus norvegicus	-	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	651567	-	-	r
crotonyl-CoA + H2O	(3S)-3-hydroxybutanoyl-CoA		Rhodospirillum rubrum	-	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))	5792	-	-	r
crotonyl-CoA + H2O	(3S)-3-hydroxybutanoyl-CoA		Rattus norvegicus	-	as active as trans-decenoyl-CoA	696077	-	-	?
crotonyl-CoA + H2O	(3S)-3-hydroxybutanoyl-CoA		Rattus norvegicus	-	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	650113	-	-	r
crotonyl-CoA + H2O	(3S)-3-hydroxybutanoyl-CoA		Rattus norvegicus	-	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	651567	-	-	r
crotonyl-CoA + H2O	(3S)-3-hydroxybutanoyl-CoA		Rattus norvegicus	-	ratio of hydration rates trans-2-decenoyl-CoA/crotonyl-CoA is 0.29	687485	-	-	r
crotonyl-CoA + H2O	(3S)-3-hydroxybutanoyl-CoA		Rhodospirillum rubrum	-	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))	5792	-	-	r
crotonyl-CoA + H2O	(3S)-3-hydroxyacyl-CoA		Rattus norvegicus	-	stereoselective reaction mechanism, Glu144 and Glu164 are essential for ECH catalysis, overview	697212	-	-	?
crotonyl-CoA + H2O	?		Sus scrofa	-	best substrate. The classification is ambiguous because the stereochemistry is not exactly determined	5866	-	-	?
crotonyl-CoA + H2O	?		Bos taurus	-	best substrate. The classification is ambiguous because the stereochemistry is not exactly determined	33730	-	-	?
crotonyl-CoA + H2O	?		Escherichia coli	-	the classification is ambiguous because the stereochemistry is not exactly determined	2207, 700005	-	-	?
crotonyl-CoA + H2O	?		Clostridium acetobutylicum	-	the classification is ambiguous because the stereochemistry is not exactly determined	33729	-	-	?
crotonyl-CoA + H2O	?		Sus scrofa	-	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)	33713	-	-	?
dec-2-enoyl-CoA + H2O	?		Sus scrofa	-	32% of the activity with crotonyl-CoA. The classification is ambiguous because the stereochemistry is not exactly determined	5866	-	-	?
decenoyl-CoA + H2O	?		Bos taurus	-	17% of the activity with crotonyl-CoA. The classification is ambiguous because the stereochemistry is not exactly determined	33730	-	-	?
decenoyl-CoA + H2O	?		Escherichia coli	-	the classification is ambiguous because the stereochemistry is not exactly determined	700005	-	-	?
dodec-2-enoyl-CoA + H2O	?		Sus scrofa	-	9.6% of the activity with crotonyl-CoA. The classification is ambiguous because the stereochemistry is not exactly determined	5866	-	-	?
dodecenoyl-CoA + H2O	?		Bos taurus	-	7% of the activity with crotonyl-CoA. The classification is ambiguous because the stereochemistry is not exactly determined	33730	-	-	?
hex-2-enoyl-CoA + H2O	?		Sus scrofa	-	77% of the activity with crotonyl-CoA. The classification is ambiguous because the stereochemistry is not exactly determined	5866	-	-	?
hexadec-2-enoyl-CoA + H2O	?		Sus scrofa	-	2.4% of the activity with crotonyl-CoA. The classification is ambiguous because the stereochemistry is not exactly determined	5866	-	-	?
hexadecenoyl-CoA + H2O	?		Bos taurus	-	1% of the activity with crotonyl-CoA. The classification is ambiguous because the stereochemistry is not exactly determined	33730	-	-	?
hexenoyl-CoA + H2O	?		Clostridium acetobutylicum	-	-	33729	-	-	?
oct-2-enoyl-CoA + H2O	?		Sus scrofa	-	54% of the activity with crotonyl-CoA. The classification is ambiguous because the stereochemistry is not exactly determined	5866	-	-	?
octenoyl-CoA + H2O	?		Bos taurus	-	36% of the activity with crotonyl-CoA. The classification is ambiguous because the stereochemistry is not exactly determined	33730	-	-	?
tetradecenoyl-CoA + H2O	?		Bos taurus	-	2% of the activity with crotonyl-CoA. The classification is ambiguous because the stereochemistry is not exactly determined	33730	-	-	?
trans-2-decenoyl-CoA + H2O	(3S)-hydroxydecanoyl-CoA		Rattus norvegicus	P14604	-	649739	-	-	?
trans-2-decenoyl-CoA + H2O	(3S)-hydroxydecanoyl-CoA		Rattus norvegicus	-	-	649889	-	-	?
trans-2-decenoyl-CoA + H2O	(3S)-hydroxydecanoyl-CoA		Rattus norvegicus	-	ratio of hydration rates trans-2-decenoyl-CoA/crotonyl-CoA is 0.29	687485	-	-	r
trans-2-decenoyl-CoA + H2O	(3S)-hydroxydecanoyl-CoA		Bos taurus	-	Vmax is 8fold lower than with crotonyl-CoA	33718	-	-	?
trans-2-hexadecanoyl-CoA + H2O	(3S)-hydroxyhexadecanoyl-CoA		Bos taurus	-	Vmax is 82fold lower than with crotonyl-CoA	33718	-	-	?
trans-2-hexenoyl-CoA + H2O	(3S)-hydroxyhexanoyl-CoA		Rattus norvegicus	P14604	-	649739	-	-	?
trans-2-hexenoyl-CoA + H2O	(3S)-hydroxyhexanoyl-CoA		Rattus norvegicus	-	-	649889	-	-	?
trans-decenoyl-CoA + H2O	?		Rattus norvegicus	-	as active as crotonyl-CoA	696077	-	-	?
hexenoyl-CoA + H2O	?		Bos taurus	-	67% of the activity with crotonyl-CoA. The classification is ambiguous because the stereochemistry is not exactly determined	33730	-	-	?
additional information	?	-	Pseudomonas putida	-	biosynthetic pathway of medium-chain-length polyhydroxyalkanoates	693287	-	-	-
additional information	?	-	Rattus norvegicus	-	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	697212	-	-	-
additional information	?	-	Rattus norvegicus	-	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	689308	-	-	-
additional information	?	-	Homo sapiens	P30084	the enzyme catalyzes the second step of the mitochondrial fatty acid beta-oxidation spiral	697671	-	-	-
additional information	?	-	Rattus norvegicus	-	ECH (XI) also has enoyl-CoA isomerase activity at approximately 1/5000 the level of its hydratase activity, overview	697212	-	-	-
additional information	?	-	Rattus norvegicus	-	the enzyme also catalyzes DELTA3-DELTA2-isomerization of trans-3-hexenoyl-CoA	649889	-	-	-
additional information	?	-	Clostridium aminobutyricum	-	the stereochemically similar reactions of 4-hydroxybutyryl-CoA dehydratase and acyl-CoA dehydrogenase suggest a common mechanism for both enzymes, overview	695584	-	-	-
additional information	?	-	Homo sapiens	-	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	715297	-	-	-
additional information	?	-	Bacillus subtilis	-	stereoselectivity of 2-enoyl-CoA dehydratase	713767	-	-	-
additional information	?	-	Homo sapiens	-	recombinant TFP interacts strongly with cardiolipin and phosphatidylcholine	714222	-	-	-
additional information	?	-	Arabidopsis thaliana	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	715522	-	-	-

NATURAL SUBSTRATES	NATURAL PRODUCTS	REACTION DIAGRAM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY SUBSTRATE	LITERATURE (Substrate)	COMMENTARY PRODUCT	LITERATURE (Product)
(2E)-5-methylhexa-2,4-dienoyl-CoA + H2O	3-hydroxy-5-methylhex-4-enoyl-CoA		Pseudomonas aeruginosa, Pseudomonas citronellolis	-	-	717129	-	-
(3S)-3-hydroxyacyl-CoA	(E)-2(or 3)-enoyl-CoA + H2O		Arabidopsis thaliana	Q9ZPJ5	-	715522	-	-
(Z)-2-butenoyl-CoA + H2O	(3R)-3-hydroxybutanoyl-CoA		Rattus norvegicus	-	kcat is 12fold slower than with the trans-iosmer crotonyl-CoA	651567	-	-
2,3-dehydroadipyl-CoA + H2O	3-hydroxyadipyl-CoA		Pseudomonas sp., Pseudomonas putida	-	-	716755	-	-
2,3-dehydroadipyl-CoA + H2O	3-hydroxyadipyl-CoA		Escherichia coli	P76082	-	716755	-	-
4-hydroxybutyryl-CoA	crotonyl-CoA + H2O		Clostridium aminobutyricum	-	the 4-hydroxybutyryl-CoA dehydratase catalyzes the gamma-elimination of water and is also involved in the fifth CO2 fixation cycle, overview	695584	-	-
crotonyl-CoA + H2O	(3S)-3-hydroxybutanoyl-CoA		Rattus norvegicus	-	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	651567	-	-
crotonyl-CoA + H2O	(3S)-3-hydroxybutanoyl-CoA		Rhodospirillum rubrum	-	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))	5792	-	-
additional information	?	-	Pseudomonas putida	-	biosynthetic pathway of medium-chain-length polyhydroxyalkanoates	693287	-	-
additional information	?	-	Rattus norvegicus	-	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	697212	-	-
additional information	?	-	Rattus norvegicus	-	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	689308	-	-
additional information	?	-	Homo sapiens	P30084	the enzyme catalyzes the second step of the mitochondrial fatty acid beta-oxidation spiral	697671	-	-
additional information	?	-	Homo sapiens	-	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	715297	-	-
additional information	?	-	Bacillus subtilis	-	stereoselectivity of 2-enoyl-CoA dehydratase	713767	-	-

COFACTOR	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	IMAGE
FAD	Clostridium aminobutyricum	-	each 56 kDa subunit of the homotetrameric enzyme contains one FAD and a [Fe4S4]2+ cluster	695584	2D-image

METALS and IONS	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
Fe2+	Clostridium aminobutyricum	-	each 56 kDa subunit of the homotetrameric enzyme contains one FAD and a [Fe4S4]2+ cluster	695584

INHIBITORS	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	IMAGE
(3S)-hydroxybutanoyl-CoA	Bos taurus	-	competitive	33718	-
(3S)-hydroxyhexadecanoyl-CoA	Bos taurus	-	competitive, 50% inhibition at 0.00075 mM, 90% inhibition by 0.004 mM	33718	-
(R)-methylenecyclopropylformyl-CoA	Rattus norvegicus	-	methylenecyclopropylformyl-CoA is a better inhibitor for enoyl-CoA hydratase 2 than for enoyl-CoA hydratase 1	689308	2D-image
(S)-methylenecyclopropylformyl-CoA	Rattus norvegicus	-	methylenecyclopropylformyl-CoA is a better inhibitor for enoyl-CoA hydratase 2 than for enoyl-CoA hydratase 1	689308	2D-image
3-ketohexadecanoyl-CoA	Bos taurus	-	0.008 mM, 40% inhibition	33718	2D-image
3-octynoyl-CoA	Rattus norvegicus	-	irreversibly inactivates only enoyl-CoA hydratase 2, the catalytic residue Glu47 is covalently labeled by the inhibitor	689308	2D-image
acetoacetyl-CoA	Bos taurus	-	enolate form of acetoacetyl-CoA acts as a competitive inhibitor. 6 molecules of inhibitor are bound per molecule of enzyme	33730	2D-image
acetoacetyl-CoA	Sus scrofa	-	-	5866	2D-image
acetoacetyl-CoA	Rattus norvegicus	-	-	697604	2D-image
crotonyl-CoA	Clostridium acetobutylicum	-	-	33729	2D-image
decenoyl-CoA	Bos taurus	-	-	33730	2D-image
hexadecenoyl-CoA	Bos taurus	-	-	33730	2D-image
hexenoyl-CoA	Bos taurus	-	-	33730	2D-image
iodoacetamide	Sus scrofa	-	10 mM, 20 min, 20% inhibition	5866	2D-image
NEM	Sus scrofa	-	10 mM, 19% inhibition. 5 mM, 13% inhibition	5866	2D-image
Octanoyl-CoA	Rattus norvegicus	-	-	33734, 699508	2D-image
p-chloromercuribenzoate	Sus scrofa	-	1 mM, complete inhibition. 0.1 mM, 11% inhibition	5866	2D-image
methylenecyclopropylformyl-CoA	Rattus norvegicus	-	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	689308	2D-image
additional information	Clostridium acetobutylicum	-	no inhibition by hexenoyl-CoA	33729	-
additional information	Bos taurus	-	no inhibition: ethyl acetoacetate, acetoacetate	33730	-
additional information	Rattus norvegicus	-	3-octynoyl-CoA is not an inhibitor of enoyl-CoA hydratase 1	689308	-
additional information	Homo sapiens	-	the enzyme is controlled by feed-back inhibition, overview	714222	-

ACTIVATING COMPOUND	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	IMAGE
CoA	Rattus norvegicus	-	the enzyme is dependent on CoA	697212	2D-image

KM VALUE [mM]	KM VALUE [mM] Maximum	SUBSTRATE	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	IMAGE
0.05	-	(Z)-2-butenoyl-CoA	Rattus norvegicus	-	pH 7.4, 25�C	651567	-
0.008	-	2-decenoyl-CoA	Escherichia coli	-	-	700005	2D-image
0.118	-	3'-dephosphocrotonyl-CoA	Rattus norvegicus	-	pH 7.4, 25�C, mutant enzyme E144D	650113	2D-image
0.003	-	crotonyl-CoA	Rattus norvegicus	-	pH 7.4, 25�C, mutant enzyme G141P	650113	2D-image
0.013	-	crotonyl-CoA	Sus scrofa	-	pH 9.0	5866	2D-image
0.015	-	crotonyl-CoA	Rattus norvegicus	-	pH 7.4, 25�C, wild-type enzyme	650113	2D-image
0.022	-	crotonyl-CoA	Bos taurus	-	pH 8, 25�C	33718	2D-image
0.025	-	crotonyl-CoA	Rattus norvegicus	-	pH 7.4, 25�C, mutant enzyme E144Q	650113	2D-image
0.03	-	crotonyl-CoA	Clostridium acetobutylicum	-	25�C	33729	2D-image
0.032	-	crotonyl-CoA	Rattus norvegicus	-	pH 7.4, 25�C, mutant enzyme E164D	650113	2D-image
0.041	-	crotonyl-CoA	Rattus norvegicus	-	pH 7.4, 25�C, mutant enzyme E164Q	650113	2D-image
0.0499	-	crotonyl-CoA	Rattus norvegicus	-	pH 8.0, 22�C, wild-type enzyme	649889	2D-image
0.05	-	crotonyl-CoA	Rattus norvegicus	-	-	651567	2D-image
0.05	-	crotonyl-CoA	Escherichia coli	-	-	700005	2D-image
0.195	-	crotonyl-CoA	Rattus norvegicus	-	pH 7.4, 25�C, mutant enzyme A98P	650113	2D-image
0.029	-	dec-2-enoyl-CoA	Sus scrofa	-	pH 9.0	5866	2D-image
0.03	-	dodec-2-enoyl-CoA	Sus scrofa	-	pH 9.0	5866	2D-image
0.029	-	hex-2-enoyl-CoA	Sus scrofa	-	pH 9.0	5866	2D-image
0.03	-	hexadec-2-enoyl-CoA	Sus scrofa	-	pH 9.0	5866	-
0.13	-	hexenoyl-CoA	Clostridium acetobutylicum	-	25�C	33729	2D-image
0.029	-	oct-2-enoyl-CoA	Sus scrofa	-	pH 9.0	5866	2D-image
0.0025	-	trans-2-decenoyl-CoA	Rattus norvegicus	-	pH 8.0, 22�C, mutant enzyme E144A/Q162L	649889	2D-image
0.0029	-	trans-2-decenoyl-CoA	Rattus norvegicus	-	pH 8.0, 22�C, mutant enzyme Q162A	649889	2D-image
0.003	-	trans-2-decenoyl-CoA	Rattus norvegicus	-	pH 8.0, 22�C, mutant enzyme E144A	649889	2D-image
0.0039	-	trans-2-decenoyl-CoA	Rattus norvegicus	-	pH 8.0, 22�C, wild-type enzyme	649889	2D-image
0.005	-	trans-2-decenoyl-CoA	Rattus norvegicus	-	pH 8.0, 22�C, mutant enzyme Q162L	649889	2D-image
0.0052	-	trans-2-decenoyl-CoA	Rattus norvegicus	-	pH 8.0, 22�C, mutant enzyme E164A	649889	2D-image
0.0063	-	trans-2-decenoyl-CoA	Rattus norvegicus	-	pH 8.0, 22�C, mutant enzyme Q162M	649889	2D-image
0.009	-	trans-2-hexadecanoyl-CoA	Bos taurus	-	pH 8, 25�C	33718	-
0.0143	-	trans-2-Hexenoyl-CoA	Rattus norvegicus	-	pH 8.0, 22�C, mutant enzyme Q162A	649889	2D-image
0.0152	-	trans-2-Hexenoyl-CoA	Rattus norvegicus	-	pH 8.0, 22�C, mutant enzyme E144A	649889	2D-image
0.021	-	trans-2-Hexenoyl-CoA	Rattus norvegicus	-	pH 8.0, 22�C, mutant enzyme E144A/Q162L	649889	2D-image
0.0229	-	trans-2-Hexenoyl-CoA	Rattus norvegicus	-	pH 8.0, 22�C, mutant enzyme Q162M	649889	2D-image
0.024	-	trans-2-Hexenoyl-CoA	Rattus norvegicus	-	pH 8.0, 22�C, mutant enzyme E164A	649889	2D-image
0.025	-	trans-2-Hexenoyl-CoA	Rattus norvegicus	-	pH 8.0, 22�C, wild-type enzyme	649889	2D-image
0.027	-	trans-2-Hexenoyl-CoA	Rattus norvegicus	-	pH 8.0, 22�C, mutant enzyme Q162L	649889	2D-image

TURNOVER NUMBER [1/s]	TURNOVER NUMBER MAXIMUM[1/s]	SUBSTRATE	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	IMAGE
152	-	(Z)-2-butenoyl-CoA	Rattus norvegicus	-	pH 7.4, 25�C	651567	-
26	-	3'-dephosphocrotonyl-CoA	Rattus norvegicus	-	pH 7.4, 25�C, mutant enzyme E144D	650113	2D-image
0.0011	-	crotonyl-CoA	Rattus norvegicus	-	pH 7.4, 25�C, mutant enzyme G141P	650113	2D-image
0.0053	-	crotonyl-CoA	Rattus norvegicus	-	pH 7.4, 25�C, mutant enzyme E164Q	650113	2D-image
0.53	-	crotonyl-CoA	Rattus norvegicus	-	pH 7.4, 25�C, mutant enzyme A98P	650113	2D-image
0.6	-	crotonyl-CoA	Rattus norvegicus	-	pH 7.4, 25�C, mutant enzyme E144Q	650113	2D-image
1.5	-	crotonyl-CoA	Rattus norvegicus	-	pH 7.4, 25�C, mutant enzyme E164D	650113	2D-image
1790	-	crotonyl-CoA	Rattus norvegicus	-	pH 7.4, 25�C, wild-type enzyme	650113	2D-image
1790	-	crotonyl-CoA	Rattus norvegicus	-	-	651567	2D-image
2238	-	crotonyl-CoA	Rattus norvegicus	-	pH 8.0, 22�C, wild-type enzyme	649889	2D-image
5667	-	crotonyl-CoA	Bos taurus	-	pH 7.5, 25�C	33730	2D-image
0.0121	-	trans-2-decenoyl-CoA	Rattus norvegicus	-	pH 8.0, 22�C, mutant enzyme E144A/Q162L	649889	2D-image
0.085	-	trans-2-decenoyl-CoA	Rattus norvegicus	-	pH 8.0, 22�C, mutant enzyme E144A	649889	2D-image
0.095	-	trans-2-decenoyl-CoA	Rattus norvegicus	-	pH 8.0, 22�C, mutant enzyme E164A	649889	2D-image
104	-	trans-2-decenoyl-CoA	Rattus norvegicus	-	pH 8.0, 22�C, mutant enzyme Q162A	649889	2D-image
164	-	trans-2-decenoyl-CoA	Rattus norvegicus	-	pH 8.0, 22�C, mutant enzyme Q162M	649889	2D-image
174	-	trans-2-decenoyl-CoA	Rattus norvegicus	-	pH 8.0, 22�C, mutant enzyme Q162L	649889	2D-image
203	-	trans-2-decenoyl-CoA	Rattus norvegicus	-	pH 8.0, 22�C, wild-type enzyme	649889	2D-image
0.06	-	trans-2-Hexenoyl-CoA	Rattus norvegicus	-	pH 8.0, 22�C, mutant enzyme E144A/Q162L	649889	2D-image
0.43	-	trans-2-Hexenoyl-CoA	Rattus norvegicus	-	pH 8.0, 22�C, mutant enzyme E144A	649889	2D-image
0.44	-	trans-2-Hexenoyl-CoA	Rattus norvegicus	-	pH 8.0, 22�C, mutant enzyme E164A	649889	2D-image
180	-	trans-2-Hexenoyl-CoA	Bos taurus	-	pH 8	678385	2D-image
561	-	trans-2-Hexenoyl-CoA	Rattus norvegicus	-	pH 8.0, 22�C, mutant enzyme Q162L	649889	2D-image
601	-	trans-2-Hexenoyl-CoA	Rattus norvegicus	-	pH 8.0, 22�C, mutant enzyme Q162M	649889	2D-image
607	-	trans-2-Hexenoyl-CoA	Rattus norvegicus	-	pH 8.0, 22�C, mutant enzyme Q162A	649889	2D-image
745	-	trans-2-Hexenoyl-CoA	Rattus norvegicus	-	pH 8.0, 22�C, wild-type enzyme	649889	2D-image

kcat/KM VALUE [1/mMs^-1]	kcat/KM VALUE [1/mMs^-1] Maximum	SUBSTRATE	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	IMAGE
No entries in this field

Ki VALUE [mM]	Ki VALUE [mM] Maximum	INHIBITOR	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	IMAGE
0.037	-	(3S)-hydroxybutanoyl-CoA	Bos taurus	-	pH 8, 25�C	33718	-
0.00035	-	(3S)-hydroxyhexadecanoyl-CoA	Bos taurus	-	pH 8, 25�C	33718	-
0.041	-	(R)-methylenecyclopropylformyl-CoA	Rattus norvegicus	-	25�C, ECH2	689308	2D-image
0.047	-	(R)-methylenecyclopropylformyl-CoA	Rattus norvegicus	-	25�C, ECH1	689308	2D-image
0.049	-	(R)-methylenecyclopropylformyl-CoA	Rattus norvegicus	-	25�C, ECH1	689308	2D-image
0.0492	-	(R)-methylenecyclopropylformyl-CoA	Rattus norvegicus	-	25�C	689308	2D-image
0.053	-	(S)-methylenecyclopropylformyl-CoA	Rattus norvegicus	-	25�C, ECH2	689308	2D-image
0.0571	-	(S)-methylenecyclopropylformyl-CoA	Rattus norvegicus	-	25�C	689308	2D-image
0.065	-	3-octynoyl-CoA	Rattus norvegicus	-	ECH2	689308	2D-image
0.0016	-	acetoacetyl-CoA	Bos taurus	-	pH 7.5, 25�C	33730	2D-image
0.014	-	acetoacetyl-CoA	Sus scrofa	-	pH 8.0, due to the binding of the enolate form of acetoacetyl-CoA the Ki-value should be highly pH-dependent	5866	2D-image
0.0003	-	decenoyl-CoA	Bos taurus	-	pH 7.5, 25�C	33730	2D-image
0.0004	-	dodecenoyl-CoA	Bos taurus	-	pH 7.5, 25�C	33730	-
0.0005	-	hexadecenoyl-CoA	Bos taurus	-	pH 7.5, 25�C	33730	2D-image
0.00024	-	hexenoyl-CoA	Bos taurus	-	pH 7.5, 25�C	33730	2D-image
0.00028	-	Octenoyl-CoA	Bos taurus	-	pH 7.5, 25�C	33730	-
0.00042	-	tetradecenoyl-CoA	Bos taurus	-	pH 7.5, 25�C	33730	-

IC50 VALUE [mM]	IC50 VALUE [mM] Maximum	INHIBITOR	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	IMAGE
No entries in this field

SPECIFIC ACTIVITY [µmol/min/mg]	SPECIFIC ACTIVITY MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
64	-	Rattus norvegicus	-	homogenate of cells transformed with the pET3aECH1 expression vector	649889
420	-	Escherichia coli	-	hydration of 3-octynoyl-CoA	649591
650	-	Escherichia coli	-	hydration of 2,3-octadienoyl-CoA	649591
973	-	Escherichia coli	-	hydration of 2-trans-octenoyl-CoA	649591
1334	-	Sus scrofa	-	-	5866
6155	-	Clostridium acetobutylicum	-	-	33729
additional information	-	Pseudomonas putida	-	intrinsic activity compared to overexpressing strain activity, overview	693287
additional information	-	Arabidopsis thaliana	Q9ZPJ5	2-enoyl-CoA substrate specificity of MFE2 and AIM, overview	715522

pH OPTIMUM	pH MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
7.4	-	Rattus norvegicus	-	assay at	650113
7.5	-	Bacillus subtilis	-	assay at	713767
8	-	Rattus norvegicus	-	assay at	649889
8.5	-	Sus scrofa	-	-	5866
8.5	-	Arabidopsis thaliana	Q9ZPJ5	assay at	715522
9	-	Homo sapiens	-	assay at	714222

pH RANGE	pH RANGE MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
No entries in this field

TEMPERATURE OPTIMUM	TEMPERATURE OPTIMUM MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
22	-	Rattus norvegicus	-	assay at	649889
25	-	Clostridium acetobutylicum	-	assay at	33729
25	-	Rattus norvegicus	-	assay at	650113, 689308
25	-	Bacillus subtilis	-	assay at	713767
27	-	Arabidopsis thaliana	Q9ZPJ5	assay at	715522
37	-	Homo sapiens	-	assay at	714222

TEMPERATURE RANGE	TEMPERATURE MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
No entries in this field

pI VALUE	pI VALUE MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
No entries in this field

SOURCE TISSUE	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	SOURCE
AML-12 cell	Mus musculus	-	-	702229
Hca-F cell	Mus musculus	-	a hepatocarcinoma cell line. Expression of Ech1 is upregulated in the Hca-F cell line	714400
heart	Sus scrofa	-	-	33713, 5866
liver	Bos taurus	-	-	33718, 33730, 696477
liver	Rattus norvegicus	-	-	649889, 684952, 687485, 696077, 697604, 697690, 702229, 704681
liver	Homo sapiens, Mus musculus	-	-	702229
MCF-7 cell	Homo sapiens	-	-	715023

LOCALIZATION	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	GeneOntology No.	LITERATURE	SOURCE
mitochondrial inner membrane	Homo sapiens	-	-	5743	714222
mitochondrion	Bos taurus	-	-	5739	33730
mitochondrion	Rattus norvegicus	-	-	5739	33734, 649889, 650113, 651567, 689308, 697212, 697604, 697690, 699508
mitochondrion	Sus scrofa	-	-	5739	5866
mitochondrion	Homo sapiens	P30084	-	5739	697671
peroxisome	Rattus norvegicus	-	-	5777	649739, 684952, 696077, 704681
peroxisome	Arabidopsis thaliana	Q9ZPJ5	-	5777	715522

PDB	SCOP	CATH	ORGANISM
1iq6, download	SCOP (1iq6)	CATH (1iq6)	Aeromonas punctata
3kqf, download	SCOP (3kqf)	CATH (3kqf)	Bacillus anthracis
3hp0, download	SCOP (3hp0)	CATH (3hp0)	Bacillus subtilis (strain 168)
4fzw, download	SCOP (4fzw)	CATH (4fzw)	Escherichia coli (strain K12)
2pbp, download	SCOP (2pbp)	CATH (2pbp)	Geobacillus kaustophilus (strain HTA426)
2ppy, download	SCOP (2ppy)	CATH (2ppy)	Geobacillus kaustophilus (strain HTA426)
1hzd, download	SCOP (1hzd)	CATH (1hzd)	Homo sapiens
2hw5, download	SCOP (2hw5)	CATH (2hw5)	Homo sapiens
3i47, download	SCOP (3i47)	CATH (3i47)	Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC 33152 / DSM 7513)
3qxz, download	SCOP (3qxz)	CATH (3qxz)	Mycobacterium abscessus (strain ATCC 19977 / DSM 44196)
3r9q, download	SCOP (3r9q)	CATH (3r9q)	Mycobacterium abscessus (strain ATCC 19977 / DSM 44196)
3qxi, download	SCOP (3qxi)	CATH (3qxi)	Mycobacterium marinum (strain ATCC BAA-535 / M)
3qyr, download	SCOP (3qyr)	CATH (3qyr)	Mycobacterium paratuberculosis (strain ATCC BAA-968 / K-10)
3r9t, download	SCOP (3r9t)	CATH (3r9t)	Mycobacterium paratuberculosis (strain ATCC BAA-968 / K-10)
3moy, download	SCOP (3moy)	CATH (3moy)	Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155)
3njb, download	SCOP (3njb)	CATH (3njb)	Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155)
3njd, download	SCOP (3njd)	CATH (3njd)	Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155)
3ome, download	SCOP (3ome)	CATH (3ome)	Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155)
3pe8, download	SCOP (3pe8)	CATH (3pe8)	Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155)
2c2i, download	SCOP (2c2i)	CATH (2c2i)	Mycobacterium tuberculosis
3h81, download	SCOP (3h81)	CATH (3h81)	Mycobacterium tuberculosis
3he2, download	SCOP (3he2)	CATH (3he2)	Mycobacterium tuberculosis
3pzk, download	SCOP (3pzk)	CATH (3pzk)	Mycobacterium tuberculosis
3q0g, download	SCOP (3q0g)	CATH (3q0g)	Mycobacterium tuberculosis
3q0j, download	SCOP (3q0j)	CATH (3q0j)	Mycobacterium tuberculosis
4hc8, download	SCOP (4hc8)	CATH (4hc8)	Mycobacterium tuberculosis
1wdk, download	SCOP (1wdk)	CATH (1wdk)	Pseudomonas fragi
1wdl, download	SCOP (1wdl)	CATH (1wdl)	Pseudomonas fragi
1wdm, download	SCOP (1wdm)	CATH (1wdm)	Pseudomonas fragi
2d3t, download	SCOP (2d3t)	CATH (2d3t)	Pseudomonas fragi
1dci, download	SCOP (1dci)	CATH (1dci)	Rattus norvegicus
1dub, download	SCOP (1dub)	CATH (1dub)	Rattus norvegicus
1ey3, download	SCOP (1ey3)	CATH (1ey3)	Rattus norvegicus
1mj3, download	SCOP (1mj3)	CATH (1mj3)	Rattus norvegicus
2dub, download	SCOP (2dub)	CATH (2dub)	Rattus norvegicus
2x58, download	SCOP (2x58)	CATH (2x58)	Rattus norvegicus
3zw8, download	SCOP (3zw8)	CATH (3zw8)	Rattus norvegicus
3zw9, download	SCOP (3zw9)	CATH (3zw9)	Rattus norvegicus
3zwa, download	SCOP (3zwa)	CATH (3zwa)	Rattus norvegicus
3zwb, download	SCOP (3zwb)	CATH (3zwb)	Rattus norvegicus
3zwc, download	SCOP (3zwc)	CATH (3zwc)	Rattus norvegicus
1uiy, download	SCOP (1uiy)	CATH (1uiy)	Thermus thermophilus
1wz8, download	SCOP (1wz8)	CATH (1wz8)	Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
3hrx, download	SCOP (3hrx)	CATH (3hrx)	Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)

MOLECULAR WEIGHT	MOLECULAR WEIGHT MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
155000	-	Sus scrofa	-	non-denaturing PAGE	5866
158000	-	Clostridium acetobutylicum	-	equilibrium sedimentation analysis, gel filtration	33729
160000	-	Escherichia coli	-	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	-	Homo sapiens	-	about, enoyl-CoA hydratase complex, gel filtration	714222
additional information	-	Escherichia coli	-	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 ACCESSION NO.	COMMENTARY	LITERATURE
?	Escherichia coli	-	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	2207
hexamer	Bos taurus	-	-	33730
hexamer	Sus scrofa	-	6 * 27300, SDS-PAGE	5866
hexamer	Rattus norvegicus	-	mitochondrial ECH1 that exists as a hexamer	689308
hexamer	Rattus norvegicus	-	6 * 161000, the hexamer is a dimer of trimers	697604
homodimer	Rattus norvegicus	-	ECH2 exists as a homodimer in its crystal structure	689308
oligomer	Homo sapiens	-	x * 79014, alpha-subunit, + x * 49291, beta-subunit, mass spectrometry and gel filtration	714222
tetramer	Clostridium acetobutylicum	-	4 * 40000, SDS-PAGE	33729
homotetramer	Clostridium aminobutyricum	-	4 * 56000	695584
additional information	Rattus norvegicus	-	perMFE-1 can be divided into �ve separate domains or parts	649739
additional information	Clostridium aminobutyricum	-	each 56 kDa subunit of the homotetrameric enzyme contains one FAD and a [Fe4S4]2+ cluster	695584
additional information	Rattus norvegicus	-	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	697212
additional information	Homo sapiens	-	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	714222

POSTTRANSLATIONAL MODIFICATION	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
lipoprotein	Escherichia coli	-	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	2207
lipoprotein	Escherichia coli	-	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	700005

Crystallization/COMMENTARY	ORGANISM	UNIPROT ACCESSION NO.	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	Arabidopsis thaliana	Q9ZPJ5	715522
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	Rattus norvegicus	P07896	704681
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	Rattus norvegicus	-	697604
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	Rattus norvegicus	-	33734
structure of enoyl-Coenzyme A (CoA) hydratase, co-crystallised with the inhibitor octanoyl-CoA, refined at a resolution of 2.4 A	Rattus norvegicus	-	699508

pH STABILITY	pH STABILITY MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
No entries in this field

TEMPERATURE STABILITY	TEMPERATURE STABILITY MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
No entries in this field

GENERAL STABILITY	ORGANISM	UNIPROT ACCESSION NO.	LITERATURE
No entries in this field

ORGANIC SOLVENT	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
No entries in this field

OXIDATION STABILITY	ORGANISM	UNIPROT ACCESSION NO.	LITERATURE
No entries in this field

STORAGE STABILITY	ORGANISM	UNIPROT ACCESSION NO.	LITERATURE
No entries in this field

Purification/COMMENTARY	ORGANISM	UNIPROT ACCESSION NO.	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	Arabidopsis thaliana	Q9ZPJ5	715522
-	Clostridium acetobutylicum	-	33729
-	Escherichia coli	-	2207
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	Escherichia coli	-	700005
recombinant alpha- and His-tagged beta-subunits from Escherichia coli by nickel affinity chromatography to homogeneity	Homo sapiens	-	714222
-	Rattus norvegicus	-	699508
purified from rat liver	Rattus norvegicus	P07896	704681
recombinant	Rattus norvegicus	-	651567
recombinant enzyme	Rattus norvegicus	-	649739, 649889
recombinant His6-tagged truncated ECH2 mutant enzyme	Rattus norvegicus	-	689308
recombinant, wild-type and mutant enzymes	Rattus norvegicus	-	650113
-	Sus scrofa	-	5866

Cloned/COMMENTARY	ORGANISM	UNIPROT ACCESSION NO.	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	Arabidopsis thaliana	Q9ZPJ5	715522
expression of recombinant His6-tagged FadB from pET21b-fadBBs in Escherichia coli strain BL21(DE3)	Bacillus subtilis	-	713767
-	Homo sapiens	P30084	697671
co-expression of His-tagged alpha- and beta-subunits in Escherichia coli strain Rosetta-2(DE3)	Homo sapiens	-	714222
gene phaJ, overexpression in strain KCTC1639 leads to oversupplementation with (R)-3-hydroxyalkanoate monomers and increased biosynthesis of medium-chain-length polyhydroxyalkanoate	Pseudomonas putida	-	693287
-	Rattus norvegicus	-	697690
expressed in Escherichia coli BL21	Rattus norvegicus	-	649889
expressed in Escherichis coli BL21(DE3)	Rattus norvegicus	P07896	704681
expression in Pichia pastoris	Rattus norvegicus	-	649739, 696077
expression of a His6-tagged truncated ECH2 mutant enzyme	Rattus norvegicus	-	689308

EXPRESSION	ORGANISM	UNIPROT ACCESSION NO.	LITERATURE
ECHS1 expression level in patients with simple steatosis is reduced	Homo sapiens	-	702229
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	Homo sapiens	-	715023
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	Rattus norvegicus	-	702229

ENGINEERING	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
A98P	Rattus norvegicus	-	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	650113
E144A	Rattus norvegicus	-	kcat for trans-2-hexenoyl-CoA is 1733fold lower than wild-type value	649889
E144A	Rattus norvegicus	-	site-directed mutagenesis, the mutant shows a 1000fold reduced activity compared to the wild-type enzyme	697212
E144A/Q162L	Rattus norvegicus	-	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	649889
E144D	Rattus norvegicus	-	60fold decreases in kcat with little change in KM	650113
E144Q	Rattus norvegicus	-	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	650113
E164A	Rattus norvegicus	-	kcat for trans-2-hexenoyl-CoA is 1709fold lower than wild-type value	649889
E164A	Rattus norvegicus	-	site-directed mutagenesis, the mutant shows a 1000fold reduced activity compared to the wild-type enzyme	697212
E164D	Rattus norvegicus	-	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	650113
E164Q	Rattus norvegicus	-	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	650113
Q162A	Rattus norvegicus	-	kcat for trans-2-hexenoyl-CoA is nearly identical to wild-type value	649889
Q162L	Rattus norvegicus	-	kcat for trans-2-hexenoyl-CoA is nearly identical to wild-type value	649889
Q162M	Rattus norvegicus	-	kcat for trans-2-hexenoyl-CoA is nearly identical to wild-type value	649889
G141P	Rattus norvegicus	-	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	650113
additional information	Rattus norvegicus	-	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	649739

Renatured/COMMENTARY	ORGANISM	UNIPROT ACCESSION NO.	LITERATURE
No entries in this field

APPLICATION	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
medicine	Homo sapiens, Mus musculus, Rattus norvegicus	-	ECHS1 down-regulation contributes to high-fat diet-induced hepatic steatosis	702229

DISEASE	TITLE OF PUBLICATION	LINK TO PUBMED
3-hydroxyacyl-coa dehydrogenase deficiency	A novel HPLC-based method to diagnose peroxisomal D-bifunctional protein enoyl-CoA hydratase deficiency.	PubMed
acetyl-coa c-acetyltransferase deficiency	A coupled assay detecting defects in fibroblast isoleucine degradation distal to enoyl-CoA hydratase: application to 3-oxothiolase deficiency.	PubMed
Adrenoleukodystrophy	Clinical consequences of defects in peroxisomal beta-oxidation.	PubMed
alpha-methylacyl-coa racemase deficiency	Clinical consequences of defects in peroxisomal beta-oxidation.	PubMed
Breast Neoplasms	The role of enoyl-CoA hydratase short chain 1 and peroxiredoxin 3 in PP2-induced apoptosis in human breast cancer MCF-7 cells.	PubMed
Carcinoma	The role of enoyl-CoA hydratase short chain 1 and peroxiredoxin 3 in PP2-induced apoptosis in human breast cancer MCF-7 cells.	PubMed
Dehydration	4-Hydroxybutyryl-CoA dehydratase from Clostridium aminobutyricum: characterization of FAD and iron-sulfur clusters involved in an overall non-redox reaction.	PubMed
Dehydration	Channeling of 3-hydroxy-4-trans-decenoyl coenzyme A on the bifunctional beta-oxidation enzyme from rat liver peroxisomes and on the large subunit of the fatty acid oxidation complex from Escherichia coli.	PubMed
Dehydration	D-3-hydroxyacyl coenzyme A dehydratase from rat liver peroxisomes. Purification and characterization of a novel enzyme necessary for the epimerization of 3-hydroxyacyl-CoA thioesters.	PubMed
Dehydration	Enoyl-coenzyme A hydratase-catalyzed exchange of the alpha-protons of coenzyme A thiol esters: a model for an enolized intermediate in the enzyme-catalyzed elimination?	PubMed
Dehydration	Isotope effects on the crotonase reaction.	PubMed
Dehydration	Mössbauer study of 4-hydroxybutyryl-CoA dehydratase--probing the role of an iron-sulfur cluster in an overall non-redox reaction.	PubMed
Dehydration	Succinate-ethanol fermentation in Clostridium kluyveri: purification and characterisation of 4-hydroxybutyryl-CoA dehydratase/vinylacetyl-CoA delta 3-delta 2-isomerase.	PubMed
Dehydration	Synthesis of (13)C-labeled gamma-hydroxybutyrates for EPR studies with 4-hydroxybutyryl-CoA dehydratase.	PubMed
enoyl-coa hydratase 2 deficiency	Enoyl-CoA hydratase deficiency: identification of a new type of D-bifunctional protein deficiency.	PubMed
enoyl-coa hydratase deficiency	A novel HPLC-based method to diagnose peroxisomal D-bifunctional protein enoyl-CoA hydratase deficiency.	PubMed
enoyl-coa hydratase deficiency	Enoyl-CoA hydratase deficiency: identification of a new type of D-bifunctional protein deficiency.	PubMed
Glioblastoma	Suppression of virus replication via down-modulation of mitochondrial short chain enoyl-CoA hydratase in human glioblastoma cells.	PubMed
Hepatomegaly	Amino acid and nucleotide sequences of human peroxisomal enoyl-CoA hydratase: 3-hydroxyacyl-CoA dehydrogenase cDNA.	PubMed
Hepatomegaly	Peroxisome proliferation and induction of peroxisomal enzymes in mouse and rat liver by dehydroepiandrosterone feeding.	PubMed
long-chain-3-hydroxyacyl-coa dehydrogenase deficiency	Mitochondrial trifunctional protein deficiency. Catalytic heterogeneity of the mutant enzyme in two patients.	PubMed
Lymphatic Metastasis	Enoyl coenzyme A hydratase 1 is an important factor in the lymphatic metastasis of tumors.	PubMed
Muscle Hypotonia	Amino acid and nucleotide sequences of human peroxisomal enoyl-CoA hydratase: 3-hydroxyacyl-CoA dehydrogenase cDNA.	PubMed
Neoplasms	Enoyl coenzyme A hydratase 1 is an important factor in the lymphatic metastasis of tumors.	PubMed
Neoplasms	Micropreparative immobilized pH gradient two-dimensional electrophoresis in combination with protein microsequencing for the analysis of human liver proteins.	PubMed
Protein Deficiency	Enoyl-CoA hydratase deficiency: identification of a new type of D-bifunctional protein deficiency.	PubMed
Sarcoma	High-performance liquid chromatography/nano-electrospray ionization tandem mass spectrometry, two-dimensional difference in-gel electrophoresis and gene microarray identification of lymphatic metastasis-associated biomarkers.	PubMed
Starvation	Mevalonate governs interdependency of ergosterol and siderophore biosyntheses in the fungal pathogen Aspergillus fumigatus.	PubMed
Starvation	Regulation of the pehA gene encoding the major polygalacturonase of Xanthomonas campestris by Clp and RpfF.	PubMed
Tauopathies	Identification of non-Alzheimer's disease tauopathies-related proteins by proteomic analysis.	PubMed
Tuberculosis	Cloning of an ORF with homology to Mycobacterium echA1, encoding the enoyl-CoA hydratase, in Rhodococcus fascians.	PubMed
Tuberculosis	Multiparameter screening on SlipChip used for nanoliter protein crystallization combining free interface diffusion and microbatch methods.	PubMed
Xeroderma Pigmentosum	[Screening of binding proteins to interferon-alpha promoter DNA by phage display technique]	PubMed
Zellweger Syndrome	Amino acid and nucleotide sequences of human peroxisomal enoyl-CoA hydratase: 3-hydroxyacyl-CoA dehydrogenase cDNA.	PubMed
Zellweger Syndrome	Peroxisomal beta-oxidation enzyme proteins in the Zellweger syndrome.	PubMed

REF.	AUTHORS	TITLE	JOURNAL	VOL.	PAGES	YEAR	ORGANISM	LINK TO PUBMED	SOURCE
2207	Pawar, S.; Schulz, H.	The structure of the multienzyme complex of fatty acid oxidation from Escherichia coli	J. Biol. Chem.	256	3894-3899	1981	Escherichia coli	PubMed
2210	Yang, S.Y.; Li, J.; He, X.Y.; Cosloy, S.D.; Schulz, H.	Evidence that the fadB gene of the fadAB operon of Escherichia coli encodes 3-hydroxyacyl-coenzyme A (CoA) epimerase, DELTA3-cis-DELTA2-trans-enoyl-CoA isomerase, and enoyl-CoA hydratase in addition to 3-hydroxyacyl-CoA dehydrogenase	J. Bacteriol.	170	2543-2548	1988	Escherichia coli	PubMed
5792	Moskowitz, G.J.; Merrick, J.M.	Metabolism of poly-beta-hydroxybutyrate. II. Enzymatic synthesis of D(-)-beta-hydroxybutyryl coenzyme A by an enoyl hydrase from Rhodospirillum rubrum	Biochemistry	8	2748-2754	1969	Rhodospirillum rubrum	PubMed
5866	Fong, J.C.; Schulz, H.	Purification and properties of pig heart crotonase and the presence of short chain and long chain enoyl coenzyme A hydratases in pig and guinea pig tissues	J. Biol. Chem.	252	542-547	1977	Sus scrofa	PubMed
33713	Sumegi, B.; Srere, P.A.	Binding of the enzymes of fatty acid beta-oxidation and some related enzymes to pig heart inner mitochondrial membrane	J. Biol. Chem.	259	8748-8752	1984	Sus scrofa	PubMed
33718	He, X.Y.; Yang, S.Y.; Schulz, H.	Inhibition of enoyl-CoA hydratase by long-chain L-3-hydroxyacyl-CoA and its possible effect on fatty acid oxidation	Arch. Biochem. Biophys.	298	527-531	1992	Bos taurus	PubMed
33729	Waterson, R.M.; Castellino, F.J.; Hass, G.M.; Hill, R.L.	Purification and characterization of cortonase from Clostridium acetobutylicum	J. Biol. Chem.	247	5266-5271	1972	Clostridium acetobutylicum	PubMed
33730	Waterson, R.M.; Hill, R.L.	Enoyl coenzyme A hydratase (crotonase). Catalytic properties of crotonase and its possible regulatory role in fatty acid oxidation	J. Biol. Chem.	247	5258-5265	1972	Bos taurus	PubMed
33734	Engel, C.K.; Kiema, T.R.; Hiltunen, J.K.; Wierenga, R.K.	The crystal structure of enoyl-CoA hydratase complexed with octanoyl-CoA reveals the structural adaptations required for binding of a long chain fatty acid-CoA molecule	J. Mol. Biol.	275	847-859	1998	Rattus norvegicus	PubMed
649591	Alipui, O.D.; Zhang, D.; Schulz, H.	Direct hydration of 3-octynoyl-CoA by crotonase: A missing link in Konrad Bloch's enzymatic studies with 3-alkynoyl thioesters	Biochem. Biophys. Res. Commun.	292	1171-1174	2002	Escherichia coli	PubMed
649739	Kiema, T.R.; Taskinen, J.P.; Pirilae, P.L.; Koivuranta, K.T.; Wierenga, R.K.; Hiltunen, J.K.	Organization of the multifunctional enzyme type 1: interaction between N- and C-terminal domains is required for the hydratase-1/isomerase activity	Biochem. J.	367	433-441	2002	Rattus norvegicus	PubMed
649889	Kiema, T.R.; Engel, C.K.; Schmitz, W.; Filppula, S.A.; Wierenga, R.K.; Hiltunen, J.K.	Mutagenic and enzymological studies of the hydratase and isomerase activities of 2-enoyl-CoA hydratase-1	Biochemistry	38	2991-2999	1999	Rattus norvegicus	PubMed
650113	Feng, Y.; Hofstein, H.A.; Zwahlen, J.; Tonge, P.J.	Effect of mutagenesis on the stereochemistry of enoyl-CoA hydratase	Biochemistry	41	12883-12890	2002	Rattus norvegicus	PubMed
651567	Wu, W.J.; Feng, Y.; He, X.; Hofstein, H.A.; Raleigh, D.P.; Tonge, P.J.	Stereospecificity of the reaction catalyzed by enoyl-CoA hydratase	J. Am. Chem. Soc.	122	3987-3994	2000	Rattus norvegicus	-
684952	Qin, Y.; Haapalainen, A.M.; Conry, D.; Cuebas, D.A.; Hiltunen, J.K.; Novikov, D.K.	Recombinant 2-enoyl-CoA hydratase derived from rat peroxisomal multifunctional enzyme 2: role of the hydratase reaction in bile acid synthesis	Biochem. J.	328	377-382	1997	Rattus norvegicus	-
687485	Hiltunen, J.K.; Palosaari, P.M.; Kunau, W.H.	Epimerization of 3-hydroxyacyl-CoA esters in rat liver. Involvement of two 2-enoyl-CoA hydratases	J. Biol. Chem.	264	13536-13540	1989	Rattus norvegicus	PubMed
689308	Wu, L.; Lin, S.; Li, D.	Comparative inhibition studies of enoyl-CoA hydratase 1 and enoyl-CoA hydratase 2 in long-chain fatty acid oxidation	Org. Lett.	10	3355-3358	2008	Rattus norvegicus	PubMed
693287	Vo, M.T.; Lee, K.W.; Jung, Y.M.; Lee, Y.H.	Comparative effect of overexpressed phaJ and fabG genes supplementing (R)-3-hydroxyalkanoate monomer units on biosynthesis of mcl-polyhydroxyalkanoate in Pseudomonas putida KCTC1639	J. Biosci. Bioeng.	106	95-98	2008	Pseudomonas putida	PubMed
695584	Friedrich, P.; Darley, D.J.; Golding, B.T.; Buckel, W.	The complete stereochemistry of the enzymatic dehydration of 4-hydroxybutyryl coenzyme A to crotonyl coenzyme A	Angew. Chem.	47	3254-3257	2008	Clostridium aminobutyricum	PubMed
696077	Qin, Y.M.; Poutanen, M.H.; Helander, H.M.; Kvist, A.P.; Siivari, K.M.; Schmitz, W.; Conzelmann, E.; Hellman, U.; Hiltunen, J.K.	Peroxisomal multifunctional enzyme of beta-oxidation metabolizing D-3-hydroxyacyl-CoA esters in rat liver: molecular cloning, expression and characterization	Biochem. J.	321	21-28	1997	Rattus norvegicus	PubMed
696477	Stern, J.R.	Thioltranscrotylase and beta-hydroxybutyryl CoA racemase activities of crystalline crotonase	Biochim. Biophys. Acta	26	641-643	1957	Bos taurus	PubMed
697212	Hamed, R.B.; Batchelar, E.T.; Clifton, I.J.; Schofield, C.J.	Mechanisms and structures of crotonase superfamily enzymes - how nature controls enolate and oxyanion reactivity	Cell. Mol. Life Sci.	65	2507-2527	2008	Rattus norvegicus	PubMed
697604	Engel, C.K.; Mathieu, M.; Zeelen, J.P.; Hiltunen, J.K.; Wierenga, R.K.	Crystal structure of enoyl-coenzyme A (CoA) hydratase at 2.5 angstroms resolution: a spiral fold defines the CoA-binding pocket	EMBO J.	15	5135-5145	1996	Rattus norvegicus	PubMed
697671	Kanazawa, M.; Ohtake, A.; Abe, H.; Yamamoto, S.; Satoh, Y.; Takayanagi, M.; Niimi, H.; Mori, M.; Hashimoto, T.	Molecular cloning and sequence analysis of the cDNA for human mitochondrial short-chain enoyl-CoA hydratase	Enzyme Protein	47	9-13	1993	Homo sapiens	PubMed
697690	Minami-Ishii, N.; Taketani, S.; Osumi, T.; Hashimoto, T.	Molecular cloning and sequence analysis of the cDNA for rat mitochondrial enoyl-CoA hydratase. Structural and evolutionary relationships linked to the bifunctional enzyme of the peroxisomal beta-oxidation system	Eur. J. Biochem.	185	73-78	1989	Rattus norvegicus	PubMed
699508	Engel, C.K.; Kiema, T.R.; Hiltunen, J.K.; Wierenga, R.K.	The crystal structure of enoyl-CoA hydratase complexed with octanoyl-CoA reveals the structural adaptations required for binding of a long chain fatty acid-CoA molecule	J. Mol. Biol.	275	847-859	1998	Rattus norvegicus	PubMed
700005	Binstock, J.F.; Schulz, H.	Fatty acid oxidation complex from Escherichia coli	Methods Enzymol.	71	403-411	1981	Escherichia coli	PubMed
702229	Hiromasa, Y.; Yan, X.; Roche, T.E.	Specific ion influences on self-association of pyruvate dehydrogenase kinase isoform 2 (PDHK2), binding of PDHK2 to the L2 lipoyl domain, and effects of the lipoyl group-binding site inhibitor, Nov3r	Biochemistry	47	2312-2324	2008	Homo sapiens, Mus musculus, Rattus norvegicus	PubMed
704681	Kasaragod, P.; Venkatesan, R.; Kiema, T.R.; Hiltunen, J.K.; Wierenga, R.K.	The crystal structure of liganded rat peroxisomal multifunctional enzyme type 1: a flexible molecule with two interconnected active sites	J. Biol. Chem.	285	24089-24098	2010	Rattus norvegicus	PubMed
713767	Frandi, A.; Zucca, P.; Marvasi, M.; Mastromei, G.; Sanjust, E.; Perito, B.	Bacillus subtilis fadB (ysiB) gene encodes an enoyl-CoA hydratase	Ann. Microbiol.	61	371-374	2011	Bacillus subtilis	-
714222	Fould, B.; Garlatti, V.; Neumann, E.; Fenel, D.; Gaboriaud, C.; Arlaud, G.J.	Structural and functional characterization of the recombinant human mitochondrial trifunctional protein	Biochemistry	49	8608-8617	2010	Homo sapiens	PubMed
714400	Zhang, J.; Song, M.; Wang, J.; Sun, M.; Wang, B.; Li, R.; Huang, Y.; Hou, L.; Jin, Y.; Wang, M.; Tang, J.	Enoyl coenzyme A hydratase 1 is an important factor in the lymphatic metastasis of tumors	Biomed. Pharmacother.	65	157-162	2011	Mus musculus	PubMed
715023	Liu, X.; Feng, R.; Du, L.	The role of enoyl-CoA hydratase short chain 1 and peroxiredoxin 3 in PP2-induced apoptosis in human breast cancer MCF-7 cells	FEBS Lett.	584	3185-3192	2010	Homo sapiens	PubMed
715297	Mohrig, J.R.; Reiter, N.J.; Kirk, R.; Zawadski, M.R.; Lamarre-Vincent, N.	Effect of buffer general acid-base catalysis on the stereoselectivity of ester and thioester H/D exchange in D2O	J. Am. Chem. Soc.	133	5124-5128	2011	Homo sapiens	PubMed
715522	Arent, S.; Christensen, C.E.; Pye, V.E.; N?rgaard, A.; Henriksen, A.	The multifunctional protein in peroxisomal beta-oxidation: structure and substrate specificity of the Arabidopsis thaliana protein MFP2	J. Biol. Chem.	285	24066-24077	2010	Arabidopsis thaliana	PubMed
716755	Teufel, R.; Mascaraque, V.; Ismail, W.; Voss, M.; Perera, J.; Eisenreich, W.; Haehnel, W.; Fuchs, G.	Bacterial phenylalanine and phenylacetate catabolic pathway revealed	Proc. Natl. Acad. Sci. USA	107	14390-14395	2010	Escherichia coli, Pseudomonas putida, Pseudomonas sp.	PubMed
717129	Forster-Fromme, K.; Jendrossek, D.	Catabolism of citronellol and related acyclic terpenoids in pseudomonads	Appl. Microbiol. Biotechnol.	87	859-869	2010	Pseudomonas aeruginosa, Pseudomonas citronellolis	PubMed

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IUBMB Enzyme Nomenclature

PROSITE Database of protein families and domains

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Protein Mutant Database

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