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(R)-specific 2-enoyl-CoA hydratase
2,3-dehydroadipyl-CoA hydratase
2-enoyl-CoA hydratase-1
-
-
2-octenoyl coenzyme A hydrase
-
-
-
-
acyl coenzyme A hydrase
-
-
-
-
beta-hydroxyacid dehydrase
-
-
-
-
beta-hydroxyacyl-CoA dehydrase
-
-
-
-
classic 2-enoyl-CoA hydratase
-
-
D-3-hydroxyacyl-CoA dehydratase
-
-
-
-
DELTA2-enoyl-CoA hydratase-1
-
enol-CoA hydratase
-
-
-
-
Enoyl coenzyme A hydrase (D)
-
-
-
-
enoyl coenzyme A hydrase (L)
-
-
-
-
enoyl coenzyme A hydratase
-
-
-
-
enoyl coenzyme A hydratase (L)
-
-
enoyl coenzyme A hydratase 1
-
-
enoyl-CoA hydratase 2
-
-
enoyl-CoA hydratase short chain 1
-
-
enoyl-CoA hydratase/isomerase
-
enoyl-coenzyme A hydratase
-
-
enoyl-coenzyme A hydratase/isomerase
-
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
mitochondrial short-chain enoyl-CoA hydratase-1
-
multifunctional enzyme type 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
peroxisomal bifunctional enzyme
UniProt
peroxisomal multifunctional enzyme, type 1
-
R-3-hydroxyacyl-CoA enoyl-CoA hydratase
-
-
R-3-hydroxyacyl-CoA enoyl-CoA hydratases
-
-
rat peroxisomal multifunctional enzyme type 1
-
S-3-hydroxyacyl-CoA enoyl-CoA hydratase
-
-
S-3-hydroxyacyl-CoA enoyl-CoA hydratases
-
-
short chain enoyl coenzyme A hydratase
-
-
-
-
short-chain enoyl-CoA hydratase
trans-2-enoyl-CoA hydratase
-
-
-
-
unsaturated acyl-CoA hydratase
-
-
-
-
(R)-specific 2-enoyl-CoA hydratase
-
-
(R)-specific 2-enoyl-CoA hydratase
-
-
-
2,3-dehydroadipyl-CoA hydratase
-
2,3-dehydroadipyl-CoA hydratase
-
-
2,3-dehydroadipyl-CoA hydratase
-
-
2,3-dehydroadipyl-CoA hydratase
-
-
-
2-enoyl-CoA hydratase
-
-
-
-
2-enoyl-CoA hydratase
-
-
2-enoyl-CoA hydratase 1
-
-
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)
CCH/HBCD
-
-
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
crotonyl-CoA hydratase
-
-
crotonyl-CoA hydratase
-
-
-
ECH
-
-
-
-
ECH-1
-
S-specific
ECH-2
-
R-specific
ECH1
-
-
ECHS1
-
-
enoyl-CoA hydratase
-
-
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
enoyl-CoA hydratase 1
-
-
enoyl-CoA hydratase 1
UniProt
FadB'
-
FadRBs
-
-
H16_A0461
-
PaaF
-
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
-
-
-
-
short-chain enoyl-CoA hydratase
-
YsiA
-
-
additional information
PaaF is a member of the crotonase superfamily
additional information
-
PaaF is a member of the crotonase superfamily
additional information
-
PaaF is a member of the crotonase superfamily
additional information
-
PaaF is a member of the crotonase superfamily
-
additional information
crotonase superfamily enzyme
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(2E)-5-methylhexa-2,4-dienoyl-CoA + H2O
3-hydroxy-5-methylhex-4-enoyl-CoA
(2E)-enoyl-CoA + H2O
(3S)-hydroxyacyl-CoA
(2E)-octenoyl-CoA + H2O
?
-
36% of the activity with crotonyl-CoA. The classification is ambiguous because the stereochemistry is not exactly determined
-
-
?
(3S)-3-hydroxyacyl-CoA
(E)-2(or 3)-enoyl-CoA + H2O
-
-
-
?
(S)-3-hydroxybutyryl-CoA
crotonoyl-CoA + H2O
(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-didehydroadipyl-CoA + H2O
(3S)-3-hydroxyadipyl-CoA
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
-
-
?
3'-dephosphocrotonyl-CoA + H2O
?
-
-
-
-
?
3-octynoyl-CoA + H2O
3-ketooctanoyl-CoA
4-(N,N-dimethylamino)cinnamoyl-CoA + H2O
?
-
-
-
?, r
crotonoyl-CoA + H2O
(S)-3-hydroxybutyryl-CoA
crotonyl-CoA + H2O
(3S)-3-hydroxybutanoyl-CoA
crotonyl-CoA + H2O
(3S)-hydroxybutyryl-CoA
crotonyl-CoA + H2O
3-hydroxybutyryl-CoA
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
-
-
?
methacrylyl-CoA + H2O
3-hydroxy-2-methylpropanoyl-CoA
methacrylyl-CoA + H2O
?
-
-
-
r
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
-
-
?
tiglyl-CoA + H2O
3-hydroxy-2-methylbutanoyl-CoA
low activity
-
-
r
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-decenoyl-CoA + H2O
(3S)-hydroxydecanoyl-CoA
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
-
-
?
trans-2-hexenoyl-CoA + H2O
(3S)-3-hydroxyhexanoyl-CoA
trans-crotonyl-CoA + H2O
(S)-3-hydroxybutanoyl-CoA
trans-decenoyl-CoA + H2O
?
-
as active as crotonyl-CoA
-
-
?
additional information
?
-
(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 + 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
-
-
?
(S)-3-hydroxybutyryl-CoA
crotonoyl-CoA + H2O
-
-
-
r
(S)-3-hydroxybutyryl-CoA
crotonoyl-CoA + H2O
-
-
-
r
(S)-3-hydroxybutyryl-CoA
crotonoyl-CoA + H2O
-
-
-
-
r
(S)-3-hydroxybutyryl-CoA
crotonoyl-CoA + H2O
-
-
-
-
r
2,3-didehydroadipyl-CoA + H2O
(3S)-3-hydroxyadipyl-CoA
-
-
-
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
-
-
-
-
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
-
-
-
-
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
-
-
-
-
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
-
-
?
crotonoyl-CoA + H2O
(S)-3-hydroxybutyryl-CoA
-
-
-
r
crotonoyl-CoA + H2O
(S)-3-hydroxybutyryl-CoA
-
-
-
r
crotonoyl-CoA + H2O
(S)-3-hydroxybutyryl-CoA
-
-
-
-
r
crotonoyl-CoA + H2O
(S)-3-hydroxybutyryl-CoA
-
-
-
-
r
crotonyl-CoA + H2O
(3S)-3-hydroxybutanoyl-CoA
-
-
-
-
?
crotonyl-CoA + H2O
(3S)-3-hydroxybutanoyl-CoA
-
-
-
-
r
crotonyl-CoA + H2O
(3S)-3-hydroxybutanoyl-CoA
-
-
-
-
?
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
(3S)-hydroxybutyryl-CoA
-
-
-
r
crotonyl-CoA + H2O
(3S)-hydroxybutyryl-CoA
-
-
-
r
crotonyl-CoA + H2O
(3S)-hydroxybutyryl-CoA
-
-
-
-
r
crotonyl-CoA + H2O
3-hydroxybutyryl-CoA
-
-
-
r
crotonyl-CoA + H2O
3-hydroxybutyryl-CoA
preferred substrate
-
-
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
?
-
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
-
-
?
hexenoyl-CoA + H2O
?
-
-
-
-
?
methacrylyl-CoA + H2O
3-hydroxy-2-methylpropanoyl-CoA
-
-
-
r
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
-
-
-
-
?
trans-2-decenoyl-CoA + H2O
(3S)-hydroxydecanoyl-CoA
-
-
-
?
trans-2-decenoyl-CoA + H2O
(3S)-hydroxydecanoyl-CoA
-
ratio of hydration rates trans-2-decenoyl-CoA/crotonyl-CoA is 0.29
-
-
r
trans-2-hexenoyl-CoA + H2O
(3S)-3-hydroxyhexanoyl-CoA
-
-
-
-
?
trans-2-hexenoyl-CoA + H2O
(3S)-3-hydroxyhexanoyl-CoA
-
-
-
?
trans-crotonyl-CoA + H2O
(S)-3-hydroxybutanoyl-CoA
-
-
-
?
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
?
-
-
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
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additional information
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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
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additional information
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ECH (XI) also has enoyl-CoA isomerase activity at approximately 1/5000 the level of its hydratase activity, overview
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additional information
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the enzyme also catalyzes DELTA3-DELTA2-isomerization of trans-3-hexenoyl-CoA
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additional information
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(3R)-3-hydroxyacyl-CoA is a peroxisomal specific intermediate
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additional information
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development and evaluation of a quantitative product separation method by a chiral column chromatography, overview
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additional information
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enzyme ECH displays activity toward unsaturated CoA thioesters with different chain lengths, although the turnover rate decreases for longer substrates
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additional information
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enzyme ECH displays activity toward unsaturated CoA thioesters with different chain lengths, although the turnover rate decreases for longer substrates
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additional information
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enzyme ECH displays activity toward unsaturated CoA thioesters with different chain lengths, although the turnover rate decreases for longer substrates
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(2E)-5-methylhexa-2,4-dienoyl-CoA + H2O
3-hydroxy-5-methylhex-4-enoyl-CoA
(3S)-3-hydroxyacyl-CoA
(E)-2(or 3)-enoyl-CoA + H2O
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-
-
?
(S)-3-hydroxybutyryl-CoA
crotonoyl-CoA + H2O
(Z)-2-butenoyl-CoA + H2O
(3R)-3-hydroxybutanoyl-CoA
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kcat is 12fold slower than with the trans-iosmer crotonyl-CoA
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?
2,3-didehydroadipyl-CoA + H2O
(3S)-3-hydroxyadipyl-CoA
4-(N,N-dimethylamino)cinnamoyl-CoA + H2O
?
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?
crotonoyl-CoA + H2O
(S)-3-hydroxybutyryl-CoA
crotonyl-CoA + H2O
(3S)-3-hydroxybutanoyl-CoA
crotonyl-CoA + H2O
(3S)-hydroxybutyryl-CoA
crotonyl-CoA + H2O
3-hydroxybutyryl-CoA
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r
feruloyl-CoA + H2O
3-(4-hydroxy-3-methoxyphenyl)propanoyl-CoA
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formation of the precursor of vanillin
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r
methacrylyl-CoA + H2O
3-hydroxy-2-methylpropanoyl-CoA
methacrylyl-CoA + H2O
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r
tiglyl-CoA + H2O
3-hydroxy-2-methylbutanoyl-CoA
low activity
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r
additional information
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(2E)-5-methylhexa-2,4-dienoyl-CoA + H2O
3-hydroxy-5-methylhex-4-enoyl-CoA
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(2E)-5-methylhexa-2,4-dienoyl-CoA + H2O
3-hydroxy-5-methylhex-4-enoyl-CoA
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(S)-3-hydroxybutyryl-CoA
crotonoyl-CoA + H2O
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r
(S)-3-hydroxybutyryl-CoA
crotonoyl-CoA + H2O
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r
2,3-didehydroadipyl-CoA + H2O
(3S)-3-hydroxyadipyl-CoA
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r
2,3-didehydroadipyl-CoA + H2O
(3S)-3-hydroxyadipyl-CoA
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r
2,3-didehydroadipyl-CoA + H2O
(3S)-3-hydroxyadipyl-CoA
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r
2,3-didehydroadipyl-CoA + H2O
(3S)-3-hydroxyadipyl-CoA
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r
crotonoyl-CoA + H2O
(S)-3-hydroxybutyryl-CoA
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r
crotonoyl-CoA + H2O
(S)-3-hydroxybutyryl-CoA
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r
crotonyl-CoA + H2O
(3S)-3-hydroxybutanoyl-CoA
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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
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r
crotonyl-CoA + H2O
(3S)-3-hydroxybutanoyl-CoA
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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))
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r
crotonyl-CoA + H2O
(3S)-hydroxybutyryl-CoA
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r
crotonyl-CoA + H2O
(3S)-hydroxybutyryl-CoA
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r
crotonyl-CoA + H2O
(3S)-hydroxybutyryl-CoA
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r
methacrylyl-CoA + H2O
3-hydroxy-2-methylpropanoyl-CoA
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r
methacrylyl-CoA + H2O
3-hydroxy-2-methylpropanoyl-CoA
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r
additional information
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stereoselectivity of 2-enoyl-CoA dehydratase
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additional information
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stereoselectivity of 2-enoyl-CoA dehydratase
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additional information
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the enzyme catalyzes the second step of the mitochondrial fatty acid beta-oxidation spiral
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additional information
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the enzyme catalyzes the second step of the mitochondrial fatty acid beta-oxidation spiral
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additional information
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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
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additional information
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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
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additional information
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biosynthetic pathway of medium-chain-length polyhydroxyalkanoates
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additional information
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biosynthetic pathway of medium-chain-length polyhydroxyalkanoates
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additional information
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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
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additional information
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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
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?
additional information
?
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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
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additional information
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(3R)-3-hydroxyacyl-CoA is a peroxisomal specific intermediate
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?
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evolution
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the crotonases comprise a widely distributed enzyme superfamily that has multiple roles in both primary and secondary metabolism. Enoyl-CoA hydratase (ECH) and enoyl-CoA isomerase (ECI) are prototypical crotonases. The term crotonase has been used to refer specifically to ECH, but it is also used to refer to the entirety of the superfamily of enzymes bearing the crotonase-type fold
evolution
the crotonases comprise a widely distributed enzyme superfamily that has multiple roles in both primary and secondary metabolism. Enoyl-CoA hydratase (ECH) and enoyl-CoA isomerase (ECI) are prototypical crotonases. The term crotonase has been used to refer specifically to ECH, but it is also used to refer to the entirety of the superfamily of enzymes bearing the crotonase-type fold. Some enzymes (e.g. rat peroxisomal multifunctional enzyme, type 1) have both ECH and ECI activities. These enzymes employ an active site with two glutamate residues. Rat mitochondrial ECH-1 (which has the two glutamate residues typical of ECH) has isomerase activity, albeit much lower than its hydratase activity. While the hydratase activity depends on both glutamate residues, the isomerase activity (as with dedicated ECI enzymes) relies mostly on a single glutamate
evolution
the crotonases comprise a widely distributed enzyme superfamily that has multiple roles in both primary and secondary metabolism. Enoyl-CoA hydratase (ECH) and enoyl-CoA isomerase (ECI) are prototypical crotonases. The term crotonase has been used to refer specifically to ECH, but it is also used to refer to the entirety of the superfamily of enzymes bearing the crotonase-type fold. Some enzymes, e.g. rat peroxisomal multifunctional enzyme, type 1, have both ECH and ECI activities. These enzymes employ an active site with two glutamate residues. Through the use of an additional domain, some multifunctional crotonase enzymes can also catalyze a further step in fatty acid catabolism, i.e. the oxidation of the enoyl-CoA hydratase product. While the hydratase activity depends on both glutamate residues, the isomerase activity (as with dedicated ECI enzymes) relies mostly on a single glutamate
malfunction
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siRNA-mediated knockdown of ECHS1 in the murine hepatocyte cell line alpha mouse liver 12 demonstrate increased cellular lipid accumulation induced by free fatty acid overload. Administering ECHS1 siRNA specifically reduces the expression of ECHS1 protein in mice liver, which significantly exacerbates the hepatic steatosis induced by an high fat diet
malfunction
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Ech1 shRNA interference decreases Hca-F cell proliferation and the in situ adhesive capacity of Hca-F cells to lymph nodes, phenotype, overview
malfunction
inactivation of dspI abolishes biofilm dispersion autoinduction in continuous cultures of Pseudommonas aeruginosa and results in biofilms that are significantly greater in thickness and biomass compared to the parental wild-type strain. But dispersion can be induced in dspI mutants by the exogenous addition of synthetic cis-2-decenoic acid or by complementation of DELTAdspI in trans under the control of an arabinose-inducible promoter
malfunction
deficiency of the enzyme causes an early childhood Leigh syndrome phenotype. Two homozygous truncation mutations in ECHS1 in two siblings lead to development of lethal neonatal lactic acidosis, potential genotype/phenotype correlation, overview
malfunction
mutations in ECHS1 result in short-chain enoyl-CoA hydratase (SCEH) deficiency which mainly affects the catabolism of various amino acids, particularly valine. Patients show a Leigh syndrome-like phenotype, important diagnostic markers for this disorder include S-(2-carboxypropyl)-L-cysteine and S-(2-carboxypropyl)cysteamine (which are derived from methacrylyl-CoA), S-(2-carboxyethyl)-L-cysteine and S-(2-carboxyethyl)cysteamine (which are derived from acryloyl-CoA), and 2-methyl-2,3-dihydroxybutyric acid (MDHB). In a lethal neonatal case, SCEH deficiency is confirmed with very low SCEH activity in fibroblasts and nearly absent immunoreactivity of SCEH. The patient has a severe neonatal course with elevated blood and cerebrospinal fluid (CSF) lactate and pyruvate concentrations, high plasma alanine and slightly low plasma cystine. 2-Methyl-2,3-dihydroxybutyric acid is markedly elevated as are metabolites of the three branched-chain ketoacids on urine organic acids analysis. These urine metabolites notably decrease when lactic acidosis decreases in blood. Lymphocyte pyruvate dehydrogenase complex (PDC) activity is deficient, but PDC and 2-oxoglutarate dehydrogenase complex activities in cultured fibroblasts are normal. Oxidative phosphorylation analysis on intact digitonin-permeabilized fibroblasts is suggestive of slightly reduced PDC activity relative to control range in mitochondria. Review of other cases of mutations with primary short-chain enoyl-CoA hydratase (SCEH) deficiency associated with secondary lymphocyte pyruvate dehydrogenase complex (PDC) deficiency, about half of cases with primary SCEH deficiency also exhibit secondary PDC deficiency, overview. To date, almost half of cases diagnosed with this autosomal recessive disorder perish within the neonatal or infantile period, but survival into adulthood is reported
malfunction
while mutation of Glu144 to alanine in this enzyme diminishes the isomerase activity by 10fold, mutation of Glu164 to alanine decreases the isomerase activity 1000fold, the hydratase activity is decreased 2000fold for both mutants
metabolism
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the human mitochondrial trifunctional protein enoyl-CoA hydratase is a multienzyme complex involved in fatty acid beta-oxidation. The pathway shows feed-back inhibition, overview
metabolism
two multifunctional peroxisomal isozymes, MFP2 and AIM1, both with 2-trans-enoyl-CoA hydratase and L-3-hydroxyacyl-CoA dehydrogenase activities, function in Arabidopsis thaliana peroxisomal beta-oxidation, where fatty acids are degraded by the sequential removal of two carbon units
metabolism
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the enzyme catalyzes a reaction of the beta-oxidation, overview
metabolism
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the enzyme catalyzes a reaction of the beta-oxidation, overview
metabolism
the enzyme catalyzes a reaction step of the beta-oxidation, as part of the catabolic gene cluster for phenylacetate degradation, overview
metabolism
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the enzyme catalyzes a reaction step of the beta-oxidation, overview
metabolism
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the enzyme catalyzes a reaction step of the beta-oxidation, overview
metabolism
short-chain enoyl-CoA hydratase (SCEH) is a mitochondrial enzyme involved in the oxidation of fatty acids and the catabolic pathway of valine and, to a lesser extent, isoleucine
metabolism
the prototypical crotonases enoyl-CoA hydratase (ECH) and enoyl-CoA isomerase (ECI) are crucially involved in the beta-oxidation pathway of fatty acid metabolism
metabolism
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the prototypical crotonases enoyl-CoA hydratase (ECH) and enoyl-CoA isomerase (ECI) are crucially involved in the beta-oxidation pathway of fatty acid metabolism
metabolism
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the enzyme catalyzes a reaction step of the beta-oxidation, overview
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physiological function
the multifunctional enzyme is involved in an alpha-methylacyl-CoAracemase-MFE2 independent synthesis pathway of bile acids from (24S)-hydroxyoxisterols, is involved in the beta-oxidation of long chain dicarboxylic acids
physiological function
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FadRBs or YsiA is a transcriptional regulatory protein which negatively regulates the expression of beta-oxidation genes including those belonging to the lcfA operon, including fadRBs or ysiA. FadBBs is active in the hydratation of crotonyl-CoA, supporting the possibility of its direct involvement in the beta-oxidation pathway
physiological function
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recombinant enoyl-CoA hydratase displays 2-enoyl-CoA hydratase, L-3-hydroxyacyl-CoA dehydrogenase, EC 1.1.1.35, and 3-ketoacyl-CoA thiolase, EC 2.3.1.16, activities
physiological function
enoyl-CoA hydratase is one of the enzymes involved in the peroxisomal beta-oxidation cycle
physiological function
the enzyme is responsible for catalyzing the formation of alpha,beta-unsaturated fatty acids and dspI is essential for production of cis-2-decenoic acid, and it is required for synthesis of the biofilm dispersion autoinducer cis-2-decenoic acid in the human pathogen Pseudomonas aeruginosa. Expression of dspI is correlated with cell density during planktonic and biofilm growth
physiological function
prototypical crotonase enoyl-CoA hydratase (ECH) and enoyl-CoA isomerase (ECI) are crucially involved in the beta-oxidation pathway of fatty acid metabolism. Enzyme ECH catalyzes the second step of the beta-oxidation pathway: i.e. the syn addition of a water molecule across the double bond of an alpha,beta-unsaturated enoyl-CoA thioester substrate, e.g. crotonyl or methacrylyl-CoA
physiological function
prototypical crotonase enoyl-CoA hydratase (ECH) is crucially involved in the beta-oxidation pathway of fatty acid metabolism. Enzyme ECH catalyzes the second step of the beta-oxidation pathway: i.e. the syn addition of a water molecule across the double bond of an alpha,beta-unsaturated enoyl-CoA thioester substrate, e.g. crotonyl or methacrylyl-CoA. Rat mitochondrial ECH-1 (which has the two glutamate residues typical of ECH) has isomerase activity, albeit much lower than its hydratase activity
physiological function
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prototypical crotonase enoyl-CoA hydratase (ECH) is crucially involved in the beta-oxidation pathway of fatty acid metabolism. Enzyme ECH catalyzes the second step of the beta-oxidation pathway: i.e. the syn addition of a water molecule across the double bond of an alpha,beta-unsaturated enoyl-CoA thioester substrate, e.g. crotonyl or methacrylyl-CoA. The enzyme is also involved in the formation of vanillin, combined with aldolase activity
physiological function
the enzyme is the second requisite enzyme in the beta-oxidation pathway of fatty acids that catalyzes the syn hydration of alpha,beta-unsaturated thiolester substrates
physiological function
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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
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additional information
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key role of ECHS1 and PRDX3 in regulation of 4-amino-5-(4-chlorophenyl)-7-(t-butyl)pyrazolo[3,4-d]pyrimidine, PP2, -induced apoptosis, downregulation of ECHS1 and PRDX3 potentiates PP2-induced apoptosis in MCF-7 cells, overview
additional information
identification of residues involved in the ligand-enzyme interaction, homology modeling: the carbonyl group of hexadienoyl-CoA forms H-bonds with Ala32, Gly34, Val36 and Gly83. Phosphate groups of the substrate form two ionic bonds with Arg28. The enzyme shows few distinct structural changes which include structural variation in the mobile loop, formation and loss of certain interactions between the active site residues and substrates. AMECH is a monofunctional enzyme and has one catalytic glutamic acid Glu106, an essential catalytic residue. Asp114 might also be involved in the reaction mechanism, overview
additional information
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identification of residues involved in the ligand-enzyme interaction, homology modeling: the carbonyl group of hexadienoyl-CoA forms H-bonds with Ala32, Gly34, Val36 and Gly83. Phosphate groups of the substrate form two ionic bonds with Arg28. The enzyme shows few distinct structural changes which include structural variation in the mobile loop, formation and loss of certain interactions between the active site residues and substrates. AMECH is a monofunctional enzyme and has one catalytic glutamic acid Glu106, an essential catalytic residue. Asp114 might also be involved in the reaction mechanism, overview
additional information
transcript abundance of dspI correlates with cell density
additional information
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transcript abundance of dspI correlates with cell density
additional information
molecular mechanism analysis by density functional theory methods, overview. Residue Glu164 functions as the acid/base in catalysis. And although Glu144 is not directly involved in hydration, it induces the catalytic water molecule to locate in ideal orientation to attack the double bond of substrate by hydrogen-bonding interaction. The backbone NH groups of Ala98 and Gly141 form an oxyanion whole with substrate carbonyl oxygen, playing a key role in substrate binding and stabilization of generated transition states and intermediates
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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, Escherichia coli B / ATCC 11303
brenda
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
brenda
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
2748-2755
1969
Rhodospirillum rubrum
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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 (P14604)
brenda
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
brenda
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 (P14604)
brenda
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
brenda
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
brenda
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
-
brenda
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
-
brenda
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
brenda
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
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