4.2.1.119: enoyl-CoA hydratase 2
This is an abbreviated version!
For detailed information about enoyl-CoA hydratase 2, go to the full flat file.
Word Map on EC 4.2.1.119
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4.2.1.119
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beta-oxidation
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enoyl-coas
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polyhydroxyalkanoate
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mfe-2s
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trans-2-enoyl-coa
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r-3-hydroxyacyl-coas
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aconitate
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phajs
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caviae
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3r-hydroxyacyl-coa
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even-numbered
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biotechnology
- 4.2.1.119
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beta-oxidation
- enoyl-coas
- polyhydroxyalkanoate
- mfe-2s
- trans-2-enoyl-coa
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r-3-hydroxyacyl-coas
- aconitate
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phajs
- caviae
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3r-hydroxyacyl-coa
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even-numbered
- biotechnology
Reaction
Synonyms
(3R)-hydroxyacyl-CoA dehydrogenase/2-enoyl-CoA hydratase 2, (R)-specific ECH, (R)-specific enoyl coenzyme A hydratase, (R)-specific enoyl-CoA hydratase, (R)-specific enoyl-coenzyme A hydratase, 2-enoyl-CoA hydratase, 2-enoyl-CoA hydratase 2, 2-enoyl-hydratase 2, 2E-enoyl-CoA hydratase 2, At1g76150, AtECH2, D-(-)-3-hydroxyacyl-CoA hydro-lyase, D-3-hydroxyacyl-CoA dehydratase, D-3-hydroxyacyl-CoA hydro-lyase, D-bifunctional enzyme, D-BP, D-specific 2-trans-enoyl-CoA hydratase, ECH-2, ECH2, enoyl-CoA hydratase 2, HFX_1483, hydratase 2, MaoC, MaoC-like protein, MFE-2, MFE2, MFE2 hydratase, Mfe2p [CtMfe2p(dha+bdelta)], multifunctional enzyme type 2, multifunctional enzyme type 2 hydratase, perMFE-II, peroxisomal enoyl-CoA hydratase 2, phaJ, PhaJ1, PhaJ1Pa, PhaJ1Pp, PhaJ4, PhaJ4aRe, PhaJ4bRe, PhaJ4cRe, PhaJAc, PhaJYB4, R-ECH, R-hydratase, R-specific enoyl coenzyme A hydratase, R-specific enoyl-CoA hydratase
ECTree
4.2.1.119 enoyl-CoA hydratase 2Advanced search results
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results (Substrates Products
Substrates Products on EC 4.2.1.119 - enoyl-CoA hydratase 2
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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
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reaction of the recombinant enzyme, protein converted rapidly
a physiological intermediate in bile acid synthesis
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?
(2E)-2-decenoyl-CoA + H2O
(3R)-3-hydroxydecanoyl-CoA
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activity measurements are based on the formation of the magnesium complex of 3-ketoacyl-CoA from (2E)-2-decenoyl-CoA
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-
?
(2E)-hexadecenoyl-CoA + H2O
(3R)-3-hydroxyhexadecanoyl-CoA
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-
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?
(R)-3-hydroxyoctanoyl-CoA
octenoyl-CoA + H2O
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no activity with (S)-3-hydroxyoctanoyl-CoA
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r
dec-2-enoyl-CoA + H2O
(R)-3-hydroxydecanoyl-CoA
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9-12% of the activity with hexenoyl-CoA, depending on preparation
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-
?
dodec-2-enoyl-CoA + H2O
(R)-3-hydroxydodecanoyl-CoA
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4-5% of the activity with hexenoyl-CoA, depending on preparation
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?
trans-2-decenoyl-CoA + H2O
(3R)-hydroxydecanoyl-CoA
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ratio of hydration rates trans-2-decenoyl-CoA/crotonyl-CoA is 14.4
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r
trans-dec-2-enoyl-CoA
?
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activity is 7fold lower than activity with crotonyl-CoA
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-
?
(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
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?
(2E)-2-enoyl-CoA + H2O
(3R)-3-hydroxyacyl-CoA
Haloferax mediterranei ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4
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-
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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 patients 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
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?
(2E)-crotonyl-CoA + H2O
(3R)-3-hydroxybutanoyl-CoA
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r
(2E)-oct-2-enoyl-CoA + H2O
(R)-3-hydroxyoctanoyl-CoA
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-
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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
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?
(3R)-3-hydroxyacyl-CoA
(2E)-2-enoyl-CoA + H2O
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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
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?
(3R)-3-hydroxyacyl-CoA
(2E)-2-enoyl-CoA + H2O
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
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-
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?
(3R)-3-hydroxyacyl-CoA
(2E)-2-enoyl-CoA + H2O
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
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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
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?
(3R)-3-hydroxyacyl-CoA
(2E)-2-enoyl-CoA + H2O
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a peroxisomal beta-oxidation intermediate
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?
Crotonyl-CoA + H2O
(3R)-3-Hydroxybutanoyl-CoA
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ratio of hydration rates trans-2-decenoyl-CoA/crotonyl-CoA is 14.4
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r
crotonyl-CoA + H2O
(R)-3-hydroxybutanoyl-CoA
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very low activity with crotonyl-CoA
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r
crotonyl-CoA + H2O
?
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the classification is ambiguous because the stereochemistry of the reaction product is not exactly determined
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?
crotonyl-CoA + H2O
?
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activity is 7fold higher than activity with trans-decenoyl-CoA
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?
oct-2-enoyl-CoA + H2O
(R)-3-hydroxyoctanoyl-CoA
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30-40% of the activity with hexenoyl-CoA, depending on preparation
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r
additional information
?
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channelling pathway for supplying (R)-3-hydroxyacyl-CoA monomer units from fatty acid beta-oxidation to poly(3-hydroxybutyrate-co-3-hydroxyhexanoate) biosynthesis
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?
additional information
?
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the enzyme is essential for polyhydroxyalkanoate biosynthesis
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?
additional information
?
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PhaJYB4 activity is thought to be specific for short chain-length enoyl-CoA
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?
additional information
?
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PhaJYB4 activity is thought to be specific for short chain-length enoyl-CoA
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?
additional information
?
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PhaJYB4 activity is thought to be specific for short chain-length enoyl-CoA
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?
additional information
?
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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
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?
additional information
?
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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
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?
additional information
?
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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
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?
additional information
?
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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
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?
additional information
?
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Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
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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
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?
additional information
?
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the bifunctional peroxisomal multifunctional enzyme type 2 exhibits dehydrogenase and hydratase activity from separate entities
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?
additional information
?
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MFE-2 structure-function studies, overview
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?
additional information
?
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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
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?
additional information
?
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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
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?
additional information
?
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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
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?
additional information
?
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the enzyme is specific for enoyl-CoAs of medium chain length
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?
additional information
?
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the enzyme is specific for enoyl-CoAs of medium chain length
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?
additional information
?
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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
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?
additional information
?
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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
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?
additional information
?
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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
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?
additional information
?
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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
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?
additional information
?
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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
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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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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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?
additional information
?
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method deleopment and optimization of a separation and detection method for (3R)- and (3S)-hydroxyacyl-CoAs
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?
additional information
?
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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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?
