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Information on EC 4.2.1.119 - enoyl-CoA hydratase 2
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4.2.1.119 enoyl-CoA hydratase 2IUBMB Comments
This enzyme catalyses a hydration step in peroxisomal beta-oxidation. The human multifunctional enzyme type 2 (MFE-2) is a 79000 Da enzyme composed of three functional units: (3R)-hydroxyacyl-CoA dehydrogenase, 2-enoyl-CoA hydratase 2 and sterol carrier protein 2-like units . The enzymes from Aeromonas caviae and Arabidopsis thaliana are monofunctional enzymes. 2-Enoyl-CoA hydratase 3 from Candida tropicalis is a part from multifunctional enzyme type 2 .
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Word Map
- 4.2.1.119
-
beta-oxidation
- enoyl-coas
- polyhydroxyalkanoate
- mfe-2s
- trans-2-enoyl-coa
-
r-3-hydroxyacyl-coas
- aconitate
-
phajs
- caviae
-
3r-hydroxyacyl-coa
-
even-numbered
- biotechnology
The enzyme appears in viruses and cellular organisms
Synonyms
hydratase 2, multifunctional enzyme type 2, phaj1, phaj4, atech2, enoyl-coa hydratase 2, phaj1pp, phaj1pa, r-hydratase, phajyb4, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
(R)-specific ECH
(R)-specific enoyl-CoA hydratase
(R)-specific enoyl-coenzyme A hydratase
2-enoyl-CoA hydratase
2-enoyl-CoA hydratase 2
At1g76150
AtECH2
ECH2
enoyl-CoA hydratase 2
MaoC
MaoC-like protein
MFE-2
MFE2
Mfe2p [CtMfe2p(dha+bdelta)]
-
2-enoyl-CoA hydratase 2 domain of Candida tropicalis
multifunctional enzyme type 2
perMFE-II
-
peroxisomal multifunctional enzyme perMFE-II has 2-enoyl-CoA hydratase 2 (D-specific) activity and D-specific 3-hydroxyacyl-CoA dehydrogenase (EC 1.1.1.36) activity. 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 (EC 1.1.1.35) activity
peroxisomal enoyl-CoA hydratase 2
phaJ
PhaJ1
PhaJ4aRe
PhaJ4bRe
PhaJ4cRe
PhaJAc
PhaJYB4
R-ECH
R-hydratase
R-specific enoyl coenzyme A hydratase
R-specific enoyl-CoA hydratase
(R)-specific ECH
Haloferax mediterranei ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4
-
-
(R)-specific enoyl-CoA hydratase
Haloferax mediterranei ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4
-
-
2-enoyl-CoA hydratase
-
monofunctional, has not been observed as a wild-type protein. Part of perMFE-2 (2-enoyl-CoA hydratase 2/(R)-3-hydroxyacyl-CoA dehydrogenase)
2-enoyl-CoA hydratase 2
-
domain of multifunctional enzyme type 2 (MFE-2), (3R)-hydroxyacyl-CoA dehydrogenase/2-enoyl-CoA hydratase 2
2-enoyl-CoA hydratase 2
-
domain of multifunctional enzyme type 2 (MFE-2), (3R)-hydroxyacyl-CoA dehydrogenase/2-enoyl-CoA hydratase 2
2-enoyl-CoA hydratase 2
the enzyme is the middle part of the mammalian peroxisomal multifunctional enzyme type 2 (MFE-2)
2-enoyl-CoA hydratase 2
-
evidence that hydratase 2 can be either an integral part and/or a fragmentation product of a multifunctional beta-oxidation protein, perMFE-II
2-enoyl-CoA hydratase 2
-
has also D-3-hydroxyacyl-CoA dehydrogenase activity
2-enoyl-CoA hydratase 2
-
is part of peroxisomal multifunctional enzyme perMFE-II together with D-specific 3-hydroxyacyl-CoA dehydrogenase (EC 1.1.1.36)
2-enoyl-CoA hydratase 2
domain of multifunctional enzyme type 2 (MFE-2), (3R)-hydroxyacyl-CoA dehydrogenase/2-enoyl-CoA hydratase 2
2-enoyl-CoA hydratase 2
part of the multifunctional protein (MFP) containing crotonase, L-3-hydroxyacyl-CoA dehydrogenase, D-3-hydroxyacyl-CoA dehydrogenase, and 3-hydroxyacyl-CoA epimerase
AtECH2
gene name. Alignment of AtECH2 with homologous proteins is shown
enoyl-CoA hydratase 2
monofunctional enzyme in Arabidopsis thaliana
MaoC
-
the classification is ambiguous because the stereochemistry of the reaction product is not exactly determined
MFE-2
-
multifunctional enzyme with 2-enoyl-CoA hydratase 2 activity and 2/(3R)-hydroxyacyl-CoA dehydrogenase (EC 1.1.1.36) activity
MFE-2
-
peroxisomal hydratase 2 together with (3R)-hydroxyacyl-CoA dehydrogenase is present as multifunctional enzyme
multifunctional enzyme type 2
-
(3R)-hydroxyacyl-CoA dehydrogenase/2-enoyl-CoA hydratase 2
R-specific enoyl coenzyme A hydratase
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(3R)-3-hydroxyacyl-CoA = (2E)-2-enoyl-CoA + H2O
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydration
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
(3R)-3-hydroxyacyl-CoA hydro-lyase
This enzyme catalyses a hydration step in peroxisomal beta-oxidation. The human multifunctional enzyme type 2 (MFE-2) is a 79000 Da enzyme composed of three functional units: (3R)-hydroxyacyl-CoA dehydrogenase, 2-enoyl-CoA hydratase 2 and sterol carrier protein 2-like units [1]. The enzymes from Aeromonas caviae [4] and Arabidopsis thaliana [5] are monofunctional enzymes. 2-Enoyl-CoA hydratase 3 from Candida tropicalis is a part from multifunctional enzyme type 2 [3].
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CAS REGISTRY NUMBER
COMMENTARY
9027-13-8
cf. EC 4.2.1.17
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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
(24E)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholest-24-enoyl-CoA + H2O
(24R,25R)-3alpha,7alpha,12alpha,24-tetrahydroxy-5beta-cholestanoyl-CoA
-
reaction of the recombinant enzyme, protein converted rapidly
a physiological intermediate in bile acid synthesis
-
?
(2E)-2-decenoyl-CoA + H2O
(3R)-3-hydroxydecanoyl-CoA
-
activity measurements are based on the formation of the magnesium complex of 3-ketoacyl-CoA from (2E)-2-decenoyl-CoA
-
-
?
(2E)-hexadecenoyl-CoA + H2O
(3R)-3-hydroxyhexadecanoyl-CoA
-
-
-
?
(R)-3-hydroxyoctanoyl-CoA
octenoyl-CoA + H2O
-
no activity with (S)-3-hydroxyoctanoyl-CoA
-
-
r
dec-2-enoyl-CoA + H2O
(R)-3-hydroxydecanoyl-CoA
-
9-12% of the activity with hexenoyl-CoA, depending on preparation
-
-
?
dodec-2-enoyl-CoA + H2O
(R)-3-hydroxydodecanoyl-CoA
-
4-5% of the activity with hexenoyl-CoA, depending on preparation
-
-
?
trans-2-decenoyl-CoA + H2O
(3R)-hydroxydecanoyl-CoA
-
ratio of hydration rates trans-2-decenoyl-CoA/crotonyl-CoA is 14.4
-
-
r
trans-dec-2-enoyl-CoA
?
-
activity is 7fold lower than activity with crotonyl-CoA
-
-
?
(2E)-2-enoyl-CoA + H2O
(3R)-3-hydroxyacyl-CoA
2-enoyl-CoA hydratase 2 is a part of multifunctional enzyme type 2, hydrates trans-2-enoyl-CoA to 3-hydroxyacyl-CoA as a key enzyme in the (3R)-hydroxy-dependent route of peroxisomal beta-oxidation of fatty acids
-
-
?
(2E)-2-enoyl-CoA + H2O
(3R)-3-hydroxyacyl-CoA
Haloferax mediterranei ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4
-
-
-
r
(2E)-2-enoyl-CoA + H2O
(3R)-3-hydroxyacyl-CoA
peroxisomal multifunctional enzyme type 2 (MFE-2) is a 79000 Da enzyme composed of three functional units: (3R)-hydroxyacyl-CoA dehydrogenase, 2-enoyl-CoA hydratase 2 and sterol carrier protein 2-like units. It catalyzes the second and third steps of peroxisomal beta-oxidation, and its importance in human lipid metabolism is shown by the severe clinical symptoms (dysmorphic features, such as macrocephaly and large fontanelles, hypotonia, seizures, etc.) in patients having defects in the gene encoding MFE-2. Typical biochemical observations include a high ratio of C26:0 to C22:0 fatty acids and elevated levels of pristanic acid (2,6,10,14-tetramethylpentadecanoic acid) in the patientsâ plasma and fibroblasts, indicating the significance of MFE-2 in the breakdown of very-long-chain and alpha-methylbranched-chain fatty acids. The patients also have high levels of di- and trihydroxycholestanoic acids, which are precursors of bile acids, showing that MFE-2 also participates in bile acid synthesis
-
-
?
(2E)-crotonyl-CoA + H2O
(3R)-3-hydroxybutanoyl-CoA
-
-
-
r
(2E)-oct-2-enoyl-CoA + H2O
(R)-3-hydroxyoctanoyl-CoA
-
-
-
r
(3R)-3-hydroxyacyl-CoA
(2E)-2-enoyl-CoA + H2O
AtECH2 participates in vivo in the conversion of the intermediate (3R)-hydroxyacyl-CoA, generated by the metabolism of fatty acids with a cis (Z)-unsaturated bond on an even-numbered carbon, to the (2E)-enoyl-CoA for further degradation through the core beta-oxidation cycle. AtECH2 is a monofunctional enzyme in Arabidopsis thaliana that is devoid of 3-hydroxyacyl-CoA dehydrogenase activity
-
-
?
(3R)-3-hydroxyacyl-CoA
(2E)-2-enoyl-CoA + H2O
-
recombinant forms of the three proteins, PhaJ4aRe to PhaJ4cRe, show enoyl-CoA hydratase activity with R specificity, and the catalytic efficiencies are elevated as the substrate chain length increases from C4 to C8. PhaJ4aRe and PhaJ4bRe show over 10fold higher catalytic efficiency than PhaJ4cRe
-
-
?
(3R)-3-hydroxyacyl-CoA
(2E)-2-enoyl-CoA + H2O
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
-
-
-
-
?
(3R)-3-hydroxyacyl-CoA
(2E)-2-enoyl-CoA + H2O
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
-
recombinant forms of the three proteins, PhaJ4aRe to PhaJ4cRe, show enoyl-CoA hydratase activity with R specificity, and the catalytic efficiencies are elevated as the substrate chain length increases from C4 to C8. PhaJ4aRe and PhaJ4bRe show over 10fold higher catalytic efficiency than PhaJ4cRe
-
-
?
(3R)-3-hydroxyacyl-CoA
(2E)-2-enoyl-CoA + H2O
-
a peroxisomal beta-oxidation intermediate
-
-
?
Crotonyl-CoA + H2O
(3R)-3-Hydroxybutanoyl-CoA
-
ratio of hydration rates trans-2-decenoyl-CoA/crotonyl-CoA is 14.4
-
-
r
crotonyl-CoA + H2O
(R)-3-hydroxybutanoyl-CoA
-
very low activity with crotonyl-CoA
-
-
r
crotonyl-CoA + H2O
?
-
the classification is ambiguous because the stereochemistry of the reaction product is not exactly determined
-
-
?
crotonyl-CoA + H2O
?
-
activity is 7fold higher than activity with trans-decenoyl-CoA
-
-
?
oct-2-enoyl-CoA + H2O
(R)-3-hydroxyoctanoyl-CoA
-
30-40% of the activity with hexenoyl-CoA, depending on preparation
-
-
r
additional information
?
-
-
channelling pathway for supplying (R)-3-hydroxyacyl-CoA monomer units from fatty acid beta-oxidation to poly(3-hydroxybutyrate-co-3-hydroxyhexanoate) biosynthesis
-
-
?
additional information
?
-
-
the enzyme is essential for polyhydroxyalkanoate biosynthesis
-
-
?
additional information
?
-
PhaJYB4 activity is thought to be specific for short chain-length enoyl-CoA
-
-
?
additional information
?
-
-
PhaJYB4 activity is thought to be specific for short chain-length enoyl-CoA
-
-
?
additional information
?
-
PhaJYB4 activity is thought to be specific for short chain-length enoyl-CoA
-
-
?
additional information
?
-
-
domains A and B have different enzymatic properties and both domains play a functional role in the beta-oxidation of fatty acids in yeast peroxisomes
-
-
?
additional information
?
-
-
in yeast, the second and the third reaction of the fatty-acid beta-oxidation spiral are catalysed by peroxisomal multifunctional enzyme type 2 (Mfe2p/Fox2p). This protein has two (3R)-hydroxyacyl-CoA dehydrogenase domains and a C-terminal 2-enoyl-CoA hydratase 2 domain
-
-
?
additional information
?
-
-
MFE-2 is a multifunctional enzyme with 2-enoyl-CoA hydratase 2 activity and 2/(3R)-hydroxyacyl-CoA dehydrogenase (EC 1.1.1.36) activity
-
-
?
additional information
?
-
-
engineered Ralstonia eutropha strains as host strains for PhaJ4aRe to PhaJ4cRe are capable of synthesizing poly((R)-3-hydroxybutyrate-co-(R)-3-hydroxyhexanoate) from soybean oil, but only PhaJ4aRe is one of the major enzymes supplying the (R)-3-hydroxyhexanoate-CoA monomer through beta-oxidation, pathway overview
-
-
?
additional information
?
-
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
-
engineered Ralstonia eutropha strains as host strains for PhaJ4aRe to PhaJ4cRe are capable of synthesizing poly((R)-3-hydroxybutyrate-co-(R)-3-hydroxyhexanoate) from soybean oil, but only PhaJ4aRe is one of the major enzymes supplying the (R)-3-hydroxyhexanoate-CoA monomer through beta-oxidation, pathway overview
-
-
?
additional information
?
-
-
the bifunctional peroxisomal multifunctional enzyme type 2 exhibits dehydrogenase and hydratase activity from separate entities
-
-
?
additional information
?
-
-
MFE-2 structure-function studies, overview
-
-
?
additional information
?
-
-
MaoC is an enoyl-CoA hydratase which is involved in converting enoyl-CoAs to (R)-3-hydroxyacyl coenzyme A in fadB mutant Escherichia coli. Metabolic link between fatty acid metabolism and polyhydroxyalkanoate biosynthesis
-
-
?
additional information
?
-
-
peroxisomal hydratase 2 together with (3R)-hydroxyacyl-CoA dehydrogenase, and peroxisomal hydratase 1 together with (3S)-hydroxyacyl-CoA dehydrogenase, are present as multifunctional enzymes. When present simultaneously in peroxisomes, beta-oxidation has two stereochemical possibilities
-
-
?
additional information
?
-
-
development of a chiral HPLC method coupled with tandem mass spectrometry for the sensitive, direct, stereospecific and quantitative analysis of ECH-1/-2 reaction products, or R-/S-3-hydroxyalkanoates in general. The method is based on the reaction of the 3-hydroxyl group on the chiral carbon with 3,5-dimethylphenyl isocyanate, creating aurethane derivative which is then chirally resolved on a chiral HPLC column having 3,5-dimethylphenylcarbamate-derivatized cellulose as the chiral stationary phase. The resolved urethane derivatives are detected using tandem MS in the multiple reactions monitoring negative electrospray ionization mode by monitoring the free hydroxy fatty acid fragment ion liberated from its parent urethane derivative. The method resolves the R-/S-enantiomers of 3-hydroxy fatty acid homologues ranging from C6 to C16, overview
-
-
?
additional information
?
-
the enzyme is specific for enoyl-CoAs of medium chain length
-
-
?
additional information
?
-
-
the enzyme is specific for enoyl-CoAs of medium chain length
-
-
?
additional information
?
-
chain-length specificity of PhaJ1 is determined mainly by the bulkiness of the amino acid residue at position 72, but other factors, such as structural fluctuations, also affect specificity
-
-
?
additional information
?
-
-
chain-length specificity of PhaJ1 is determined mainly by the bulkiness of the amino acid residue at position 72, but other factors, such as structural fluctuations, also affect specificity
-
-
?
additional information
?
-
chain-length specificity of PhaJ1 is determined mainly by the bulkiness of the amino acid residue at position 72, but other factors, such as structural fluctuations, also affect specificity
-
-
?
additional information
?
-
chain-length specificity of PhaJ1 is determined mainly by the bulkiness of the amino acid residue at position 72, but other factors, such as structural fluctuations, also affect specificity
-
-
?
additional information
?
-
-
chain-length specificity of PhaJ1 is determined mainly by the bulkiness of the amino acid residue at position 72, but other factors, such as structural fluctuations, also affect specificity
-
-
?
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
?
-
-
identification of substrate binding sites, residues Trp249 to Arg251, using a photoreactive palmitic acid analogue bearing a diazirine moiety as a photophore in photoaffinity labeling of purified rat liver peroxisomes, ligand preparation, overview. The labeling efficiency competitively decreases in the presence of palmitoyl-CoA
-
-
?
additional information
?
-
-
method deleopment and optimization of a separation and detection method for (3R)- and (3S)-hydroxyacyl-CoAs
-
-
?
additional information
?
-
-
identification of substrate binding sites, residues Trp249 to Arg251, using a photoreactive palmitic acid analogue bearing a diazirine moiety as a photophore in photoaffinity labeling of purified rat liver peroxisomes, ligand preparation, overview. The labeling efficiency competitively decreases in the presence of palmitoyl-CoA
-
-
?
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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
(2E)-2-enoyl-CoA + H2O
(3R)-3-hydroxyacyl-CoA
2-enoyl-CoA hydratase 2 is a part of multifunctional enzyme type 2, hydrates trans-2-enoyl-CoA to 3-hydroxyacyl-CoA as a key enzyme in the (3R)-hydroxy-dependent route of peroxisomal beta-oxidation of fatty acids
-
-
?
(2E)-2-enoyl-CoA + H2O
(3R)-3-hydroxyacyl-CoA
Haloferax mediterranei ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4
-
-
-
r
(2E)-2-enoyl-CoA + H2O
(3R)-3-hydroxyacyl-CoA
peroxisomal multifunctional enzyme type 2 (MFE-2) is a 79000 Da enzyme composed of three functional units: (3R)-hydroxyacyl-CoA dehydrogenase, 2-enoyl-CoA hydratase 2 and sterol carrier protein 2-like units. It catalyzes the second and third steps of peroxisomal beta-oxidation, and its importance in human lipid metabolism is shown by the severe clinical symptoms (dysmorphic features, such as macrocephaly and large fontanelles, hypotonia, seizures, etc.) in patients having defects in the gene encoding MFE-2. Typical biochemical observations include a high ratio of C26:0 to C22:0 fatty acids and elevated levels of pristanic acid (2,6,10,14-tetramethylpentadecanoic acid) in the patientsâ plasma and fibroblasts, indicating the significance of MFE-2 in the breakdown of very-long-chain and alpha-methylbranched-chain fatty acids. The patients also have high levels of di- and trihydroxycholestanoic acids, which are precursors of bile acids, showing that MFE-2 also participates in bile acid synthesis
-
-
?
(3R)-3-hydroxyacyl-CoA
(2E)-2-enoyl-CoA + H2O
AtECH2 participates in vivo in the conversion of the intermediate (3R)-hydroxyacyl-CoA, generated by the metabolism of fatty acids with a cis (Z)-unsaturated bond on an even-numbered carbon, to the (2E)-enoyl-CoA for further degradation through the core beta-oxidation cycle. AtECH2 is a monofunctional enzyme in Arabidopsis thaliana that is devoid of 3-hydroxyacyl-CoA dehydrogenase activity
-
-
?
(3R)-3-hydroxyacyl-CoA
(2E)-2-enoyl-CoA + H2O
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
-
-
-
-
?
(3R)-3-hydroxyacyl-CoA
(2E)-2-enoyl-CoA + H2O
-
a peroxisomal beta-oxidation intermediate
-
-
?
additional information
?
-
-
channelling pathway for supplying (R)-3-hydroxyacyl-CoA monomer units from fatty acid beta-oxidation to poly(3-hydroxybutyrate-co-3-hydroxyhexanoate) biosynthesis
-
-
?
additional information
?
-
-
the enzyme is essential for polyhydroxyalkanoate biosynthesis
-
-
?
additional information
?
-
-
domains A and B have different enzymatic properties and both domains play a functional role in the beta-oxidation of fatty acids in yeast peroxisomes
-
-
?
additional information
?
-
-
in yeast, the second and the third reaction of the fatty-acid beta-oxidation spiral are catalysed by peroxisomal multifunctional enzyme type 2 (Mfe2p/Fox2p). This protein has two (3R)-hydroxyacyl-CoA dehydrogenase domains and a C-terminal 2-enoyl-CoA hydratase 2 domain
-
-
?
additional information
?
-
-
the bifunctional peroxisomal multifunctional enzyme type 2 exhibits dehydrogenase and hydratase activity from separate entities
-
-
?
additional information
?
-
-
MaoC is an enoyl-CoA hydratase which is involved in converting enoyl-CoAs to (R)-3-hydroxyacyl coenzyme A in fadB mutant Escherichia coli. Metabolic link between fatty acid metabolism and polyhydroxyalkanoate biosynthesis
-
-
?
additional information
?
-
-
peroxisomal hydratase 2 together with (3R)-hydroxyacyl-CoA dehydrogenase, and peroxisomal hydratase 1 together with (3S)-hydroxyacyl-CoA dehydrogenase, are present as multifunctional enzymes. When present simultaneously in peroxisomes, beta-oxidation has two stereochemical possibilities
-
-
?
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
-
-
?
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(R)-methylenecyclopropylformyl-CoA
-
methylenecyclopropylformyl-CoA is a better inhibitor for enoyl-CoA hydratase 2 than for enoyl-CoA hydratase 1
(S)-methylenecyclopropylformyl-CoA
-
methylenecyclopropylformyl-CoA is a better inhibitor for enoyl-CoA hydratase 2 than for enoyl-CoA hydratase 1
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Dehydration
Enoyl-CoA hydratase mediates polyhydroxyalkanoate mobilization in Haloferax mediterranei.
Dehydration
Revisiting the assignment of Rv0241c to fatty acid synthase type II of Mycobacterium tuberculosis.
enoyl-coa hydratase 2 deficiency
[Peroxisomal D-bifunctional enzyme deficiency. A case report]
Infections