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Information on EC 4.2.1.17 - enoyl-CoA hydratase
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EC Tree
4.2.1.17 enoyl-CoA hydrataseIUBMB Comments
Acts in the reverse direction. With cis-compounds, yields (3R)-3-hydroxyacyl-CoA. cf. EC 4.2.1.74 long-chain-enoyl-CoA hydratase.
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Word Map
- 4.2.1.17
-
beta-oxidation
-
thiolase
- 3-ketoacyl-coa
-
trifunctional
- l-3-hydroxyacyl-coa
- carnitine
- crotonase
- leigh
- palmitoyl-coa
-
2,4-dienoyl-coa
- clofibrate
- polyhydroxyalkanoate
-
2-trans-enoyl-coas
- acetoacetyl-coa
- proliferators
-
r-specific
-
1.1.1.35
-
leigh-like
- 3-oxoacyl-coa
-
d-bifunctional
- octanoyl-coa
-
hydratase/3-hydroxyacyl-coa
- medicine
-
even-numbered
The enzyme appears in viruses and cellular organisms
Synonyms
enoyl-coa hydratase, echs1, peroxisomal bifunctional enzyme, 2-enoyl-coa hydratase, amech, short-chain enoyl-coa hydratase, enoyl-coa hydratase/isomerase, beta-hydroxyacyl-coa dehydrase, enoyl-coenzyme a hydratase, fadb', 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
(R)-specific 2-enoyl-CoA hydratase
2,3-dehydroadipyl-CoA hydratase
2-enoyl-CoA hydratase
2-enoyl-CoA hydratase 1
2-octenoyl coenzyme A hydrase
-
-
-
-
acyl coenzyme A hydrase
-
-
-
-
beta-hydroxyacid dehydrase
-
-
-
-
beta-hydroxyacyl-CoA dehydrase
-
-
-
-
CCH/HBCD
crotonase
crotonyl hydrase
-
-
-
-
crotonyl-CoA hydratase
D-3-hydroxyacyl-CoA dehydratase
-
-
-
-
ECH
ECH-1
ECH-2
ECH1
ECHS1
enol-CoA hydratase
-
-
-
-
Enoyl coenzyme A hydrase (D)
-
-
-
-
enoyl coenzyme A hydrase (L)
-
-
-
-
enoyl coenzyme A hydratase
-
-
-
-
enoyl hydrase
-
-
-
-
enoyl-CoA hydratase
enoyl-CoA hydratase 1
FadB'
FadRBs
H16_A0461
hydratase, enoyl coenzyme A
-
-
-
-
mitochondrial enoyl coenzyme A hydratase
the classification is ambiguous because the stereochemistry is not exactly determined
mitochondrial short-chain enoyl-CoA hydratase
the classification is ambiguous because the stereochemistry is not exactly determined
PaaF
perMFE-1
perMFE-I
-
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
SCEH
short chain enoyl coenzyme A hydratase
-
-
-
-
short-chain enoyl-CoA hydratase
trans-2-enoyl-CoA hydratase
-
-
-
-
unsaturated acyl-CoA hydratase
-
-
-
-
YsiA
additional information
2-enoyl-CoA hydratase
-
-
-
-
2-enoyl-CoA hydratase 1
-
is part of peroxisomal multifunctional enzyme perMFE-I together with L-specific 3-hydroxyacyl-CoA dehydrogenase (1.1.1.35)
crotonase
-
-
-
-
crotonase
-
the classification is ambiguous because the stereochemistry is not exactly determined
crotonase
-
the classification is ambiguous because the stereochemistry of the reaction product is not exactly determined
crotonase
-
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)
crotonase
-
the classification is ambiguous because the stereochemistry of the reaction product is not exactly determined
crotonase
-
the classification is ambiguous because the stereochemistry of the reaction product is not exactly determined
ECH
-
-
-
-
enoyl-CoA hydratase
-
the classification is ambiguous because the stereochemistry is not exactly determined
enoyl-CoA hydratase
the classification is ambiguous because the stereochemistry is not exactly determined
perMFE-1
-
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
SCEH
-
-
-
-
SCEH
the classification is ambiguous because the stereochemistry is not exactly determined
short-chain enoyl-CoA hydratase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
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
-
(3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl-CoA + H2O
reaction mechansim of enoyl-CoA hydration, overview
(3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl-CoA + H2O
the CoA moiety of the substrate adopts the typical horseshoe conformation in a binding pocket formed from two adjacent monomers, while the active site catalytic residues are provided by a single monomer. The active site of rat liver mitochondrial ECH contains an oxyanion hole formed from the backbone amides of Gly141 and Ala98, which serves to polarize the carbonyl group of the alpha,beta-unsaturated enoyl-CoA substrate and stabilize the enolate intermediate. Two active site glutamate residues (Glu144 and Glu164) are proposed to act as a general base(s) for the conjugate addition of water onto the substrate enone and to protonate the resultant enolate
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
addition
double-bond hydration
elimination
-
-
-
-
hydration
-
-
-
-
addition
-
-
double bond
-
addition
-
-
of H2O to carbon carbon double bond
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
alpha-Linolenic acid metabolism, Aminobenzoate degradation, Benzoate degradation, beta-Alanine metabolism, Biosynthesis of secondary metabolites, Butanoate metabolism, Caprolactam degradation, Carbon fixation pathways in prokaryotes, Fatty acid degradation, Fatty acid elongation, Geraniol degradation, Limonene and pinene degradation, Lysine degradation, Microbial metabolism in diverse environments, Phenylalanine metabolism, Propanoate metabolism, Tryptophan metabolism, Valine, leucine and isoleucine degradation
-
, , , , , , Aminobenzoate degradation, Aminobenzoate degradation, Benzoate degradation, Benzoate degradation, Carbon fixation pathways in prokaryotes, Carbon fixation pathways in prokaryotes, Carbon fixation pathways in prokaryotes, Carbon fixation pathways in prokaryotes, Carbon fixation pathways in prokaryotes, Lysine degradation, Microbial metabolism in diverse environments, phenylacetate degradation (aerobic), Phenylalanine metabolism, Propanoate metabolism, Valine, leucine and isoleucine degradation
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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.
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CAS REGISTRY NUMBER
COMMENTARY
9027-13-8
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(2E)-octenoyl-CoA + H2O
?
-
36% of the activity with crotonyl-CoA. The classification is ambiguous because the stereochemistry is not exactly determined
-
-
?
(Z)-2-butenoyl-CoA + H2O
(3R)-3-hydroxybutanoyl-CoA
-
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
-
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-octadienoyl-CoA + H2O
3-ketooctanoyl-CoA
-
the classification is ambiguous because the stereochemistry is not exactly determined
-
-
?
2-trans-octenoyl-CoA + H2O
3-hydroxyoctanoyl-CoA
-
the classification is ambiguous because the stereochemistry is not exactly determined
-
-
?
dec-2-enoyl-CoA + H2O
?
-
32% of the activity with crotonyl-CoA. The classification is ambiguous because the stereochemistry is not exactly determined
-
-
?
dodec-2-enoyl-CoA + H2O
?
-
9.6% of the activity with crotonyl-CoA. The classification is ambiguous because the stereochemistry is not exactly determined
-
-
?
dodecenoyl-CoA + H2O
?
-
7% of the activity with crotonyl-CoA. The classification is ambiguous because the stereochemistry is not exactly determined
-
-
?
feruloyl-CoA + H2O
3-(4-hydroxy-3-methoxyphenyl)propanoyl-CoA
-
formation of the precursor of vanillin
-
-
r
hex-2-enoyl-CoA + H2O
?
-
77% of the activity with crotonyl-CoA. The classification is ambiguous because the stereochemistry is not exactly determined
-
-
?
hexadec-2-enoyl-CoA + H2O
?
-
2.4% of the activity with crotonyl-CoA. The classification is ambiguous because the stereochemistry is not exactly determined
-
-
?
hexadecenoyl-CoA + H2O
?
-
1% of the activity with crotonyl-CoA. The classification is ambiguous because the stereochemistry is not exactly determined
-
-
?
oct-2-enoyl-CoA + H2O
?
-
54% of the activity with crotonyl-CoA. The classification is ambiguous because the stereochemistry is not exactly determined
-
-
?
tetradecenoyl-CoA + H2O
?
-
2% of the activity with crotonyl-CoA. The classification is ambiguous because the stereochemistry is not exactly determined
-
-
?
trans-2-decenoyl-CoA + H2O
(3R)-3-hydroxydecanoyl-CoA
-
Escherichia coli enzyme activity is of the S-specific ECH-1 type
the distribution of R- and S-enantiomers of produced 3-hydroxydecanoate is in favour of the S-enantiomer in case of Escherichia coli
-
?
trans-2-decenoyl-CoA + H2O
(3S)-3-hydroxydecanoyl-CoA
-
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-hexadecenoyl-CoA + H2O
(3S)-3-hydroxyhexadecanoyl-CoA + (3R)-3-hydroxyhexadecanoyl-CoA
-
rat liver homogenate enzyme activity is (S)-specific
(3S)-3-hydroxyhexadecanoyl-CoA is the dominant product
-
?
trans-2-hexadecenoyl-CoA + H2O
(3S)-hydroxyhexadecanoyl-CoA
-
Vmax is 82fold lower than with crotonyl-CoA
-
-
?
(2E)-5-methylhexa-2,4-dienoyl-CoA + H2O
3-hydroxy-5-methylhex-4-enoyl-CoA
-
-
-
-
?
(2E)-5-methylhexa-2,4-dienoyl-CoA + H2O
3-hydroxy-5-methylhex-4-enoyl-CoA
-
-
-
-
?
(2E)-enoyl-CoA + H2O
(3S)-hydroxyacyl-CoA
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
-
-
?
2,3-didehydroadipyl-CoA + H2O
(3S)-3-hydroxyadipyl-CoA
substrate and product identification by mass spectrometry
-
-
r
2,3-didehydroadipyl-CoA + H2O
(3S)-3-hydroxyadipyl-CoA
-
substrate and product identification by mass spectrometry
-
-
r
2,3-didehydroadipyl-CoA + H2O
(3S)-3-hydroxyadipyl-CoA
-
substrate and product identification by mass spectrometry
-
-
r
2,3-didehydroadipyl-CoA + H2O
(3S)-3-hydroxyadipyl-CoA
-
substrate and product identification by mass spectrometry
-
-
r
3-octynoyl-CoA + H2O
3-ketooctanoyl-CoA
-
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
-
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
-
-
?
crotonyl-CoA + H2O
(3S)-3-hydroxybutanoyl-CoA
-
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
-
as active as trans-decenoyl-CoA
-
-
?
crotonyl-CoA + H2O
(3S)-3-hydroxybutanoyl-CoA
-
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
-
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
-
ratio of hydration rates trans-2-decenoyl-CoA/crotonyl-CoA is 0.29
-
-
r
crotonyl-CoA + H2O
(3S)-3-hydroxybutanoyl-CoA
stereoselective reaction mechanism, Glu144 and Glu164 are essential for ECH catalysis, overview
-
-
?
crotonyl-CoA + H2O
(3S)-3-hydroxybutanoyl-CoA
-
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
-
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
?
-
best substrate. The classification is ambiguous because the stereochemistry is not exactly determined
-
-
?
crotonyl-CoA + H2O
?
-
the classification is ambiguous because the stereochemistry is not exactly determined
-
-
?
crotonyl-CoA + H2O
?
-
the classification is ambiguous because the stereochemistry is not exactly determined
-
-
?
crotonyl-CoA + H2O
?
Escherichia coli B / ATCC 11303
-
the classification is ambiguous because the stereochemistry is not exactly determined
-
-
?
crotonyl-CoA + H2O
?
-
best substrate. The classification is ambiguous because the stereochemistry is not exactly determined
-
-
?
crotonyl-CoA + H2O
?
-
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)
-
-
?
decenoyl-CoA + H2O
?
-
17% of the activity with crotonyl-CoA. The classification is ambiguous because the stereochemistry is not exactly determined
-
-
?
decenoyl-CoA + H2O
?
-
the classification is ambiguous because the stereochemistry is not exactly determined
-
-
?
hexenoyl-CoA + H2O
?
-
67% of the activity with crotonyl-CoA. The classification is ambiguous because the stereochemistry is not exactly determined
-
-
?
methacrylyl-CoA + H2O
3-hydroxy-2-methylpropanoyl-CoA
-
-
-
r
trans-2-decenoyl-CoA + H2O
(3S)-hydroxydecanoyl-CoA
-
Vmax is 8fold lower than with crotonyl-CoA
-
-
?
trans-2-decenoyl-CoA + H2O
(3S)-hydroxydecanoyl-CoA
-
ratio of hydration rates trans-2-decenoyl-CoA/crotonyl-CoA is 0.29
-
-
r
trans-crotonyl-CoA + H2O
(S)-3-hydroxybutanoyl-CoA
-
-
-
?
additional information
?
-
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
?
-
-
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
?
-
-
stereoselectivity of 2-enoyl-CoA dehydratase
-
-
?
additional information
?
-
-
stereoselectivity of 2-enoyl-CoA dehydratase
-
-
?
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
?
-
the enzyme catalyzes the second step of the mitochondrial fatty acid beta-oxidation spiral
-
-
?
additional information
?
-
-
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
?
-
-
recombinant TFP interacts strongly with cardiolipin and phosphatidylcholine
-
-
?
additional information
?
-
human SCEH has broad substrate specificity for acyl-CoAs, including crotonyl-CoA (from beta-oxidation), acryloyl-CoA (from metabolism of various amino acids), 3-methylcrotonyl-CoA (from leucine metabolism), tiglyl-CoA (from isoleucine metabolism), and methacrylyl-CoA (from valine metabolism). Although SCEH binds tiglyl-CoA, the rate of hydration is relatively low
-
-
?
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
?
-
-
biosynthetic pathway of medium-chain-length polyhydroxyalkanoates
-
-
?
additional information
?
-
Pseudomonas putida KCTC 1639 / ATCC 25544
-
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
-
-
?
additional information
?
-
-
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
?
-
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
?
-
-
(3R)-3-hydroxyacyl-CoA is a peroxisomal specific intermediate
-
-
?
additional information
?
-
-
development and evaluation of a quantitative product separation method by a chiral column chromatography, overview
-
-
?
additional information
?
-
enzyme ECH displays activity toward unsaturated CoA thioesters with different chain lengths, although the turnover rate decreases for longer substrates
-
-
?
additional information
?
-
enzyme ECH displays activity toward unsaturated CoA thioesters with different chain lengths, although the turnover rate decreases for longer substrates
-
-
?
additional information
?
-
-
enzyme ECH displays activity toward unsaturated CoA thioesters with different chain lengths, although the turnover rate decreases for longer substrates
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(Z)-2-butenoyl-CoA + H2O
(3R)-3-hydroxybutanoyl-CoA
-
kcat is 12fold slower than with the trans-iosmer crotonyl-CoA
-
-
?
feruloyl-CoA + H2O
3-(4-hydroxy-3-methoxyphenyl)propanoyl-CoA
-
formation of the precursor of vanillin
-
-
r
(2E)-5-methylhexa-2,4-dienoyl-CoA + H2O
3-hydroxy-5-methylhex-4-enoyl-CoA
-
-
-
-
?