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(3R)-hydroxyacyl-CoA dehydrogenase/2-enoyl-CoA hydratase 2
-
-
(R)-specific enoyl coenzyme A hydratase
-
(R)-specific enoyl-CoA hydratase
(R)-specific enoyl-coenzyme A hydratase
2E-enoyl-CoA hydratase 2
-
-
D-(-)-3-hydroxyacyl-CoA hydro-lyase
-
-
D-3-hydroxyacyl-CoA dehydratase
-
-
D-3-hydroxyacyl-CoA hydro-lyase
-
-
D-bifunctional enzyme
-
-
D-specific 2-trans-enoyl-CoA hydratase
-
-
Mfe2p [CtMfe2p(dha+bdelta)]
-
2-enoyl-CoA hydratase 2 domain of Candida tropicalis
multifunctional enzyme type 2
multifunctional enzyme type 2 hydratase
-
-
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
R-specific enoyl coenzyme A hydratase
R-specific enoyl-CoA hydratase
(R)-specific ECH
-
(R)-specific enoyl-CoA hydratase
-
-
(R)-specific enoyl-CoA hydratase
-
(R)-specific enoyl-CoA hydratase
-
-
(R)-specific enoyl-coenzyme A hydratase
-
(R)-specific enoyl-coenzyme A hydratase
-
2-enoyl-CoA hydratase
-
-
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
-
-
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
is a part of multifunctional enzyme type 2
2-enoyl-CoA hydratase 2
-
-
2-enoyl-CoA hydratase 2
-
domain in human MFE-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
-
-
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
-
-
2-enoyl-CoA hydratase 2
-
part of the multifunctional enzyme (MHE)
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
At1g76150
-
AtECH2
gene name. Alignment of AtECH2 with homologous proteins is shown
AtECH2
monofunctional enzyme in Arabidopsis thaliana
ECH2
-
enoyl-CoA hydratase 2
-
enoyl-CoA hydratase 2
monofunctional enzyme in Arabidopsis thaliana
enoyl-CoA hydratase 2
-
-
MaoC
-
-
MaoC
-
the classification is ambiguous because the stereochemistry of the reaction product is not exactly determined
MaoC-like protein
-
MFE-2
-
(3R)-hydroxyacyl-CoA dehydrogenase/2-enoyl-CoA hydratase 2
MFE-2
-
multifunctional enzyme
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
MFE2
-
-
multifunctional enzyme type 2
-
(3R)-hydroxyacyl-CoA dehydrogenase/2-enoyl-CoA hydratase 2
multifunctional enzyme type 2
-
-
multifunctional enzyme type 2
-
-
-
peroxisomal enoyl-CoA hydratase 2
-
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 coenzyme A hydratase
-
-
-
R-specific enoyl coenzyme A hydratase
-
R-specific enoyl-CoA hydratase
-
R-specific enoyl-CoA hydratase
-
-
R-specific enoyl-CoA hydratase
-
-
R-specific enoyl-CoA hydratase
-
-
-
R-specific enoyl-CoA hydratase
-
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(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)-2-enoyl-CoA + H2O
(3R)-3-hydroxyacyl-CoA
(2E)-butenoyl-CoA + H2O
(3R)-hydroxybutanoyl-CoA
-
-
-
-
?
(2E)-crotonyl-CoA + H2O
(3R)-3-hydroxybutanoyl-CoA
(2E)-decenoyl-CoA + H2O
(3R)-3-hydroxydecanoyl-CoA
(2E)-enoyl-CoA + H2O
(3R)-hydroxyacyl-CoA
(2E)-hexadecenoyl-CoA + H2O
(3R)-3-hydroxyhexadecanoyl-CoA
-
-
-
?
(2E)-hexenoyl-CoA + H2O
(3R)-3-hydroxyhexanoyl-CoA
(2E)-oct-2-enoyl-CoA + H2O
(R)-3-hydroxyoctanoyl-CoA
(3R)-3-hydroxyacyl-CoA
(2E)-2-enoyl-CoA + H2O
(3R)-3-hydroxydecanoyl-CoA
(2E)-2-decenoyl-CoA + H2O
(3R)-3-hydroxyhexadecanoyl-CoA
(2E)-2-hexadecenoyl-CoA + H2O
(R)-3-hydroxydecanoyl-CoA
trans-2-decenoyl-CoA + H2O
-
-
-
-
r
(R)-3-hydroxyoctanoyl-CoA
octenoyl-CoA + H2O
-
no activity with (S)-3-hydroxyoctanoyl-CoA
-
-
r
2-trans-butenoyl-CoA + H2O
(3R)-hydroxybutanoyl-CoA
-
-
-
-
?
2-trans-decenoyl-CoA + H2O
(3R)-3-hydroxydecanoyl-CoA
-
-
-
-
?
Crotonyl-CoA + H2O
(3R)-3-Hydroxybutanoyl-CoA
crotonyl-CoA + H2O
(R)-3-hydroxybutanoyl-CoA
crotonyl-CoA + H2O
3-hydroxybutanoyl-CoA
-
-
-
?
dec-2-enoyl-CoA + H2O
(R)-3-hydroxydecanoyl-CoA
-
9-12% of the activity with hexenoyl-CoA, depending on preparation
-
-
?
dec-2-enoyl-CoA + H2O
3-hydroxydecanoyl-CoA
-
-
-
?
dodec-2-enoyl-CoA + H2O
(R)-3-hydroxydodecanoyl-CoA
-
4-5% of the activity with hexenoyl-CoA, depending on preparation
-
-
?
dodec-2-enoyl-CoA + H2O
3-hydroxydodecanoyl-CoA
-
-
-
?
hex-2-enoyl-CoA + H2O
(R)-3-hydroxyhexanoyl-CoA
hexenoyl-CoA + H2O
3-hydroxyhexanoyl-CoA
-
-
-
?
oct-2-enoyl-CoA + H2O
(R)-3-hydroxyoctanoyl-CoA
oct-2-enoyl-CoA + H2O
3-hydroxyoctanoyl-CoA
-
-
-
?
pent-2-enoyl-CoA + H2O
(R)-3-hydroxypentanoyl-CoA
-
-
-
-
?
tetradec-2-enoyl-CoA + H2O
?
-
-
-
-
?
trans-2-decenoyl-CoA
(3R)-hydroxydecanoyl-CoA + H2O
-
-
-
-
?
trans-2-decenoyl-CoA + H2O
(3R)-3-hydroxydecanoyl-CoA
-
-
-
-
r
trans-2-decenoyl-CoA + H2O
(3R)-hydroxydecanoyl-CoA
-
ratio of hydration rates trans-2-decenoyl-CoA/crotonyl-CoA is 14.4
-
-
r
trans-2-hexadecenoyl-CoA
(3R)-hydroxyhexadecanoyl-CoA + H2O
-
-
-
-
?
trans-2-octenoyl-CoA + H2O
3-hydroxyoctanoyl-CoA
-
-
-
?
trans-dec-2-enoyl-CoA
?
-
activity is 7fold lower than activity with crotonyl-CoA
-
-
?
additional information
?
-
(2E)-2-enoyl-CoA + H2O
(3R)-3-hydroxyacyl-CoA
-
-
-
r
(2E)-2-enoyl-CoA + H2O
(3R)-3-hydroxyacyl-CoA
-
-
-
r
(2E)-2-enoyl-CoA + H2O
(3R)-3-hydroxyacyl-CoA
-
-
-
r
(2E)-2-enoyl-CoA + H2O
(3R)-3-hydroxyacyl-CoA
-
-
-
r
(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
-
-
-
r
(2E)-2-enoyl-CoA + H2O
(3R)-3-hydroxyacyl-CoA
-
-
-
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
-
-
?
(2E)-2-enoyl-CoA + H2O
(3R)-3-hydroxyacyl-CoA
-
-
-
r
(2E)-2-enoyl-CoA + H2O
(3R)-3-hydroxyacyl-CoA
-
-
-
r
(2E)-2-enoyl-CoA + H2O
(3R)-3-hydroxyacyl-CoA
-
-
-
-
r
(2E)-2-enoyl-CoA + H2O
(3R)-3-hydroxyacyl-CoA
-
-
-
?
(2E)-crotonyl-CoA + H2O
(3R)-3-hydroxybutanoyl-CoA
-
-
-
r
(2E)-crotonyl-CoA + H2O
(3R)-3-hydroxybutanoyl-CoA
-
-
-
r
(2E)-crotonyl-CoA + H2O
(3R)-3-hydroxybutanoyl-CoA
-
-
-
r
(2E)-crotonyl-CoA + H2O
(3R)-3-hydroxybutanoyl-CoA
-
-
-
r
(2E)-decenoyl-CoA + H2O
(3R)-3-hydroxydecanoyl-CoA
-
-
-
r
(2E)-decenoyl-CoA + H2O
(3R)-3-hydroxydecanoyl-CoA
-
-
-
-
?
(2E)-decenoyl-CoA + H2O
(3R)-3-hydroxydecanoyl-CoA
-
-
-
-
?
(2E)-enoyl-CoA + H2O
(3R)-hydroxyacyl-CoA
-
-
-
-
?
(2E)-enoyl-CoA + H2O
(3R)-hydroxyacyl-CoA
-
straight-chain
-
-
?
(2E)-hexenoyl-CoA + H2O
(3R)-3-hydroxyhexanoyl-CoA
-
-
-
?
(2E)-hexenoyl-CoA + H2O
(3R)-3-hydroxyhexanoyl-CoA
-
-
-
-
?
(2E)-hexenoyl-CoA + H2O
(3R)-3-hydroxyhexanoyl-CoA
-
-
-
-
?
(2E)-oct-2-enoyl-CoA + H2O
(R)-3-hydroxyoctanoyl-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
-
-
-
-
?
(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
-
-
-
-
?
(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
-
-
-
-
?
(3R)-3-hydroxyacyl-CoA
(2E)-2-enoyl-CoA + H2O
-
-
-
?
(3R)-3-hydroxyacyl-CoA
(2E)-2-enoyl-CoA + H2O
-
-
-
-
?
(3R)-3-hydroxyacyl-CoA
(2E)-2-enoyl-CoA + H2O
-
a peroxisomal beta-oxidation intermediate
-
-
?
(3R)-3-hydroxydecanoyl-CoA
(2E)-2-decenoyl-CoA + H2O
-
-
-
-
?
(3R)-3-hydroxydecanoyl-CoA
(2E)-2-decenoyl-CoA + H2O
-
-
-
-
r
(3R)-3-hydroxyhexadecanoyl-CoA
(2E)-2-hexadecenoyl-CoA + H2O
-
-
-
-
?
(3R)-3-hydroxyhexadecanoyl-CoA
(2E)-2-hexadecenoyl-CoA + H2O
-
-
-
-
?
Crotonyl-CoA + H2O
(3R)-3-Hydroxybutanoyl-CoA
-
-
-
-
?
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
-
-
-
-
?
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
-
-
?
hex-2-enoyl-CoA + H2O
(R)-3-hydroxyhexanoyl-CoA
-
-
-
-
?
hex-2-enoyl-CoA + H2O
(R)-3-hydroxyhexanoyl-CoA
-
-
-
-
r
oct-2-enoyl-CoA + H2O
(R)-3-hydroxyoctanoyl-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
?
-
-
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
?
-
-
no activity with (S)-3-hydroxyoctanoyl-CoA
-
-
?
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
?
-
-
the (S)-3-hydroxy-CoA is not dehydrated
-
-
?
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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0.05
-
L654G/V130G mutant with crotonyl-CoA as substrate, cell extract
0.08
-
L65A/V130G mutant with crotonyl-CoA as substrate, cell extract
0.12
-
strain HsMFE-2(D490A)
0.16
-
strain HsMFE-2(G16S)
0.2
-
strain HsMFE-2(H532A)
0.21
-
strain HsMFE-2(D370A), strain HsMFE-2(H406A)
0.24
-
strain HsMFE-2(Y410A)
0.26
-
strain HsMFE-2(D517A), strain HsMFE-2(E408A)
0.55
-
S62A mutant with octenoyl-CoA as substrate, cell extract
0.86
-
wild-type with octenoyl-CoA as substrate, cell extract
0.994
-
pH and temperature not specified in the publication
1.2
0.03 mM (2E)-hexadecenoyl-CoA as a substrate
1.98
-
L65G mutant with octenoyl-CoA as substrate, cell extract
12.4
0.1 mM, 3-hydroxydecanoyl-CoA as a substrate
1256
-
L65A mutant with crotonyl-CoA as substrate, cell extract
1288
-
V130A mutant with crotonyl-CoA as substrate, cell extract
15.8
-
L65G mutant with crotonyl-CoA as substrate, cell extract
1538
-
L65V mutant with crotonyl-CoA as substrate, cell extract
1594
-
wild-type with crotonyl-CoA as substrate, cell extract
1880
-
L65I mutant with crotonyl-CoA as substrate, cell extract
2.25
-
L65I mutant with octenoyl-CoA as substrate, cell extract
21.2
-
V130G mutant with octenoyl-CoA as substrate, cell extract
3.5
0.03 m (2E)-hexenoyl-CoA as a substrate
30
0.05 mM (2E)-decenoyl-CoA as a substrate
33.4
-
pET-Hydr2 expressed in Escherichia coli, soluble extract of the cells
48
-
recombinant 46 kDa hydratase 2, last purification step: size exclusion
6.59
-
V130A mutant with octenoyl-CoA as substrate, cell extract
67
-
S62A mutant with crotonyl-CoA as substrate, cell extract
68.5
-
V130G mutant with crotonyl-CoA as substrate, cell extract
69.8
-
L65A mutant with octenoyl-CoA as substrate, cell extract
7.92
-
L65V mutant with octenoyl-CoA as substrate, cell extract
883
-
V130G mutant with crotonyl-CoA as substrate, purified enzyme
additional information
-
activity is below the detection limit of the assay system when using extracts from non-transformed cells or cells transformed with the vector only
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evolution
-
phylogenetic tree of MaoC-like domains in PhaJ homologues encoded in Ralstonia eutropha H16 genome and domains in the known PhaJ proteins from Aeromonas caviae and Pseudomonas aeruginosa
evolution
phylogenetic tree of MaoC-like domains in PhaJ homologues encoded in Ralstonia eutropha H16 genome and domains in the known PhaJ proteins from Aeromonas caviae and Pseudomonas aeruginosa
evolution
all HFX-gene encoded proteins contain a MaoC-like domain (pfam01575), similar to PhaJAc, which is involved in PHA biosynthesis for supplying (R)-3HB-CoA from fatty acid beta-oxidation
evolution
enzyme PhaJYB4 shows a high homology to short chain-length (C4-C6)-specific PhaJs, e.g. Pseudomonas aeruginosa PhaJ1Pa and Aeromonas caviae PhaJAc, rather than medium chain-length (C8-C12)-specific PhaJs, e.g. Pseudomonas aeruginosa PhaJ4Pa4
evolution
-
enzyme PhaJYB4 shows a high homology to short chain-length (C4-C6)-specific PhaJs, e.g. Pseudomonas aeruginosa PhaJ1Pa and Aeromonas caviae PhaJAc, rather than medium chain-length (C8-C12)-specific PhaJs, e.g. Pseudomonas aeruginosa PhaJ4Pa4
-
evolution
-
all HFX-gene encoded proteins contain a MaoC-like domain (pfam01575), similar to PhaJAc, which is involved in PHA biosynthesis for supplying (R)-3HB-CoA from fatty acid beta-oxidation
-
evolution
-
phylogenetic tree of MaoC-like domains in PhaJ homologues encoded in Ralstonia eutropha H16 genome and domains in the known PhaJ proteins from Aeromonas caviae and Pseudomonas aeruginosa
-
malfunction
-
deletion of phaJ4aRe from the chromosome results in significant decrease of (R)-3-hydroxyhexanoate composition in the accumulated copolyester, whereas no change is observed with deletion of phaJ4bRe or phaJ4cRe
malfunction
-
inactivating mutations of multifunctional enzyme type 2 hydratase lead to D-bifunctional protein deficiency type II
malfunction
defects in either HC-PPase or ECH2 compromise cell proliferation due to defects in mobilizing seed storage lipids, phenotype, overview. Enoyl-CoA hydratase 2 (ECH2) gene mutation causes the A#3-1sm phenotypes, overview. Mutant A#3-1 has a cell size that is severely reduced, but the cell number remains similar to that of original fugu5-1. The cell number decreases in A#3-1 single mutant (A#3-1sm), similar to that of fugu5-1, but cell size is almost equal to that of the wild-type. A#3-1 mutation does not affect CCE in other compensation exhibiting mutant backgrounds, such as an3-4 and fugu2-1/fas1-6
malfunction
polyhydroxyalkanoate contents are slightly reduced in a phaJ deletion mutant DELTAphaJ1 compared to wild-type
malfunction
-
polyhydroxyalkanoate contents are slightly reduced in a phaJ deletion mutant DELTAphaJ1 compared to wild-type
-
malfunction
-
defects in either HC-PPase or ECH2 compromise cell proliferation due to defects in mobilizing seed storage lipids, phenotype, overview. Enoyl-CoA hydratase 2 (ECH2) gene mutation causes the A#3-1sm phenotypes, overview. Mutant A#3-1 has a cell size that is severely reduced, but the cell number remains similar to that of original fugu5-1. The cell number decreases in A#3-1 single mutant (A#3-1sm), similar to that of fugu5-1, but cell size is almost equal to that of the wild-type. A#3-1 mutation does not affect CCE in other compensation exhibiting mutant backgrounds, such as an3-4 and fugu2-1/fas1-6
-
malfunction
-
deletion of phaJ4aRe from the chromosome results in significant decrease of (R)-3-hydroxyhexanoate composition in the accumulated copolyester, whereas no change is observed with deletion of phaJ4bRe or phaJ4cRe
-
metabolism
-
the enzyme is involved in the peroxisomal beta-oxidation of fatty acids and their derivatives
metabolism
as the hydration reaction catalyzed by R-ECHs is a reversible process, R-ECHs may be involved in PHA degradation as well as in PHA biosynthesis
metabolism
-
as the hydration reaction catalyzed by R-ECHs is a reversible process, R-ECHs may be involved in PHA degradation as well as in PHA biosynthesis
-
metabolism
-
the enzyme is involved in the peroxisomal beta-oxidation of fatty acids and their derivatives
-
physiological function
-
MFE2 consists of a (3R)-hydroxyacyl-CoA dehydrogenase, HD, domain, a (2E)-enoyl-CoA hydratase 2, H2, domain, and a sterol carrier protein 2-like domain, and is known to catalyze the second and third steps of the peroxisomal beta-oxidation of fatty acids and their derivatives
physiological function
(R)-specific enoyl-CoA hydratase mediates polyhydroxyalkanoate mobilization in Haloferax mediterranei. Enoyl coenzyme A (enoyl-CoA) hydratases (ECHs) reversibly catalyze the syn and anti hydration of 2-enoyl-CoA to produce (S)- or (R)-3-hydroxyacyl-CoA (3HA-CoA). The (S)-specific ECHs (S-ECHs, EC 4.2.1.17) are involved in fatty acid beta-oxidation. Through catalyzing the hydration of intermediates in fatty acid beta-oxidation, the (R)-specific ECHs (R-ECHs) may play an important role in fatty acid metabolism in eukaryotes and in polyhydroxyalkanoate (PHA) biosynthesis in bacteria. Function of PhaJ1 on PHA mobilization
physiological function
(R)-specific enoyl-coenzyme A (enoyl-CoA) hydratases (PhaJs) are capable of supplying monomers from fatty acid beta-oxidation to polyhydroxyalkanoate (PHA) biosynthesis. PhaJ1Pp from Pseudomonas putida shows a broader substrate specificity
physiological function
(R)-specific enoyl-coenzyme A (enoyl-CoA) hydratases (PhaJs) are capable of supplying monomers from fatty acid beta-oxidation to polyhydroxyalkanoate (PHA) biosynthesis. PhaJ1Pp from Pseudomonas putida shows a broader substrate specificity
physiological function
Bacillus cereus accumulates polyhydroxyalkanoate (PHA). The MaoC-like protein has an R-specific enoyl-CoA hydratase activity and is referred to as PhaJ when involved in the PHA metabolism. In an in vivo assay using Escherichia coli as a host for PHA accumulation, the recombinant strain expressing PhaJYB4 and PHA synthase leads to increased PHA accumulation, suggesting that PhaJYB4 functioned as a monomer supplier
physiological function
comparison of the enzymes from Pseudomonas putida with residue 72Val resulting in increased preference for enoyl-coenzyme A substrates with shorter chain lengths and Pseudomonas aeruginosa with residue 72Ile resulting in an increased preference for enoyl-CoAs with longer chain lengths
physiological function
comparison of the enzymes from Pseudomonas putida with residue Val72 resulting in increased preference for enoyl-coenzyme A substrates with shorter chain lengths and Pseudomonas aeruginosa with residue Ile72 resulting in an increased preference for enoyl-CoAs with longer chain lengths
physiological function
role of the monofunctional peroxisomal enoyl-CoA hydratase 2 in compensated cell enlargement (CCE). Enzyme ECH2 alone likely promotes CCE during the post-mitotic cell expansion stage of cotyledon development, probably by converting indolebutyric acid to indole acetic acid
physiological function
-
Bacillus cereus accumulates polyhydroxyalkanoate (PHA). The MaoC-like protein has an R-specific enoyl-CoA hydratase activity and is referred to as PhaJ when involved in the PHA metabolism. In an in vivo assay using Escherichia coli as a host for PHA accumulation, the recombinant strain expressing PhaJYB4 and PHA synthase leads to increased PHA accumulation, suggesting that PhaJYB4 functioned as a monomer supplier
-
physiological function
-
(R)-specific enoyl-CoA hydratase mediates polyhydroxyalkanoate mobilization in Haloferax mediterranei. Enoyl coenzyme A (enoyl-CoA) hydratases (ECHs) reversibly catalyze the syn and anti hydration of 2-enoyl-CoA to produce (S)- or (R)-3-hydroxyacyl-CoA (3HA-CoA). The (S)-specific ECHs (S-ECHs, EC 4.2.1.17) are involved in fatty acid beta-oxidation. Through catalyzing the hydration of intermediates in fatty acid beta-oxidation, the (R)-specific ECHs (R-ECHs) may play an important role in fatty acid metabolism in eukaryotes and in polyhydroxyalkanoate (PHA) biosynthesis in bacteria. Function of PhaJ1 on PHA mobilization
-
physiological function
-
role of the monofunctional peroxisomal enoyl-CoA hydratase 2 in compensated cell enlargement (CCE). Enzyme ECH2 alone likely promotes CCE during the post-mitotic cell expansion stage of cotyledon development, probably by converting indolebutyric acid to indole acetic acid
-
physiological function
-
MFE2 consists of a (3R)-hydroxyacyl-CoA dehydrogenase, HD, domain, a (2E)-enoyl-CoA hydratase 2, H2, domain, and a sterol carrier protein 2-like domain, and is known to catalyze the second and third steps of the peroxisomal beta-oxidation of fatty acids and their derivatives
-
additional information
-
D-bifunctional enzyme is R-specific, while L-bifunctional enzyme is S-specific
additional information
-
MFE2 hydratase is R-specific, while MFE1 hydratase is S-specific
additional information
contribution of the distal pocket residue to the acyl-chain-length specificity of (R)-specific enoyl-coenzyme A hydratases from Pseudomonas spp., enzyme structure homology modeling, structure comparisons of the enzymes from Pseudomonas putida and Pseudomonas aeruginosa, PhaJ1Pp and PhaJ1Pa, overview
additional information
contribution of the distal pocket residue to the acyl-chain-length specificity of (R)-specific enoyl-coenzyme A hydratases from Pseudomonas spp., enzyme structure homology modeling, structure comparisons of the enzymes from Pseudomonas putida and Pseudomonas aeruginosa, PhaJ1Pp and PhaJ1Pa, overview
additional information
-
contribution of the distal pocket residue to the acyl-chain-length specificity of (R)-specific enoyl-coenzyme A hydratases from Pseudomonas spp., enzyme structure homology modeling, structure comparisons of the enzymes from Pseudomonas putida and Pseudomonas aeruginosa, PhaJ1Pp and PhaJ1Pa, overview
additional information
contribution of the distal pocket residue to the acyl-chain-length specificity of (R)-specific enoyl-coenzyme A hydratases from Pseudomonas spp., enzyme structure homology modeling, structure comparisons of the enzymes from Pseudomonas putida and Pseudomonas aeruginosa, PhaJ1Pp and PhaJ1Pa, overview. Active site and acyl-chain-binding pocket structure
additional information
-
contribution of the distal pocket residue to the acyl-chain-length specificity of (R)-specific enoyl-coenzyme A hydratases from Pseudomonas spp., enzyme structure homology modeling, structure comparisons of the enzymes from Pseudomonas putida and Pseudomonas aeruginosa, PhaJ1Pp and PhaJ1Pa, overview. Active site and acyl-chain-binding pocket structure
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monomer
-
size-exclusion chromatography on a Superdex 200 HR column gives a native molecular mass of 59 kDa, suggesting that the recombinant protein is monomeric
?
x * 34000, calculated from sequence
?
-
x * 63000, both recombinant CtMfe2p(dha+bdelta) and its SeMet analogue, SDS-PAGE
?
-
x * 17500, recombinant isozyme His-tagged PhaJ4aRe, SDS-PAGE, x * 17000, recombinant His-tagged PhaJ4bRe, SDS-PAGE, x * 16500, recombinant His-tagged PhaJ4cRe, SDS-PAGE
?
-
x * 17500, recombinant isozyme His-tagged PhaJ4aRe, SDS-PAGE, x * 17000, recombinant His-tagged PhaJ4bRe, SDS-PAGE, x * 16500, recombinant His-tagged PhaJ4cRe, SDS-PAGE
-
?
-
x * 45000, HsMFE-2(dhdelta), HsMFE-2(dhdelta, E366A), HsMFE-2(dhdelta, D510A), SDS-PAGE
?
-
x * 80000, SDS-PAGE
-
dimer
-
2 * 13954, calculated from sequence
dimer
-
2 * 64100, MFE-2, SDS-PAGE
homodimer
-
2 * 33000, SDS-PAGE
homodimer
-
2 * 31500, microsomal isoform, SDS-PAGE
homodimer
-
2 * 33500, peroxisomal isoform, SDS-PAGE
additional information
-
necessity of dimerization, domain organization, MFE-2 structure-function studies, overview
additional information
-
MFE2 consists of a (3R)-hydroxyacyl-CoA dehydrogenase, HD, domain, a (2E)-enoyl-CoA hydratase 2, H2, domain, and a sterol carrier protein 2-like domain
additional information
-
MFE2 consists of a (3R)-hydroxyacyl-CoA dehydrogenase, HD, domain, a (2E)-enoyl-CoA hydratase 2, H2, domain, and a sterol carrier protein 2-like domain
-
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sitting drop vapour diffusion against a reservoir solution containing 20% polyethylene glycol 4000, 5% 2-propanol and 20 mM HEPES pH 7.0 at 25°C. Crystals belong to the monoclinic space group C2, with unit-cell parameters a = 111.54 A, b = 59.29 A, c = 47.27 A, beta = 113.04° and contain a dimeric molecule in the asymmetric unit
-
hanging-drop vapour-diffusion method. Crystals of native and SeMet CtMfe2p(dha+bdelta)
-
structure determination. The eukaryotic hydratase 2 has a complete hot dog fold only in its C-domain, whereas the N-domain lacks a long central alpha-helix, thus creating space for bulkier substrates in the binding pocket. The hydrogen bonding network of the active site of 2-enoyl-CoA hydratase 2 resembles the active site geometry of mitochondrial (S)-specific 2-enoyl-CoA hydratase 1, although in a mirror image fashion
purified recombinant detagged MFE-2, 5 mg/ml protein in 0.1 Msodium phosphate, pH 7.2, and 0.2 M NaF, sitting and hanging drop vapour diffusion methods are used at 21°C, mixing of equal volumes of protein and reservoir solutions, the latter contains 100 mM Tris-HCl, pH 8.0, 1.0 M NaCl, 20% w/v PEG 5000 MME and 5 mM NAD+, X-ray diffraction structure determination and analysis at 2.15 A resolution
-
hanging-drop vapor diffusion method, crystal structure to 3 A resolution. MFE-2 has a two-domain subunit structure with a C-domain complete hot-dog fold housing the active site, and an N-domain incomplete hot-dog fold housing the cavity for the aliphatic acyl part of the substrate molecule. The ability of human hydratase 2 to utilize such bulky compounds which are not physiological substrates for the fungal ortholog, e.g. CoA esters of C26 fatty acids, pristanic acid and di/trihydroxycholestanoic acids, is explained by a large hydrophobic cavity formed upon the movements of the extremely mobile loops IIII in the N-domain. In the unliganded form of human hydratase 2, however, the loop I blocks the entrance of fatty enoyl-CoAs with chain-length above C8
homology modeling of strcuture. In the acyl-chain binding pocket, the amino acid at position 72 is the only difference between the two structures of Pseudomonas aeruginosa and Pseudomonas putida isoforms
purified recombinant enzyme PhaJ1Pa, sitting drop vapor diffusion, mixing of 10 mg/ml protein in 20 mM Tris-HCl, pH 7.5, with mother liquor containing 15 to 20% w/v PEG 3350, 20% v/v glycerol, and 0.1 M bis-Tris, pH 6.0-6.5, X-ray diffraction structure determination and analysis at 1.7 A resolution
homology modeling of strcuture. In the acyl-chain binding pocket, the amino acid at position 72 is the only difference between the two structures of Pseudomonas aeruginosa and Pseudomonas putida isoforms
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L654G/V130G
-
decreased specific activity for crotonyl-CoA
L65A
-
enzyme activity similar to wild-type enzyme
L65A/V130G
-
decreased specific activity for crotonyl-CoA
L65G
-
enzyme activity similar to wild-type enzyme
L65I
-
specific activity with crotonyl-CoA similar to wild-type enzyme
L65V
-
specific activity with crotonyl-CoA similar to wild-type enzyme
S62A
-
decreased specific activity for crotonyl-CoA
V130A
-
specific activity with crotonyl-CoA similar to wild-type enzyme
V130G
-
enzyme activity similar to wild-type enzyme, lower structural stability than wild-type enzyme
A348T
-
site-directed mutagenesis, the mutation does not affect the enzyme
A427V
-
site-directed mutagenesis, the mutation does not affect the enzyme, the mutant shows a slight increase in activity
A491T
-
site-directed mutagenesis, the mutation does not affect the enzyme
A606S
-
site-directed mutagenesis, the mutant shows reduced activity
D370A
-
reduced specific acitivity of 2-enoyl-CoA hydratase 2 when expressed in Saccharomyces cerevisiae
D490A
-
reduced specific acitivity of 2-enoyl-CoA hydratase 2 when expressed in Saccharomyces cerevisiae
D510A
-
inactive mutant enzyme
D510Y
-
site-directed mutagenesis, inactive mutant, the mutation disrupts active site architecture
D517A
-
reduced specific acitivity of 2-enoyl-CoA hydratase 2 when expressed in Saccharomyces cerevisiae
E366A
-
kcat/Km 100times lower than that of the wild type
E366G
-
site-directed mutagenesis, inactive mutant, the mutation disrupts dimerization
E408A
-
reduced specific acitivity of 2-enoyl-CoA hydratase 2 when expressed in Saccharomyces cerevisiae
G16S
-
reduced specific acitivity of 2-enoyl-CoA hydratase 2 when expressed in Saccharomyces cerevisiae
G533R
-
site-directed mutagenesis, inactive mutant, the mutation disrupts ligand interaction
H406A
-
reduced specific acitivity of 2-enoyl-CoA hydratase 2 when expressed in Saccharomyces cerevisiae
H515A
-
inactive mutant enzyme
H532A
-
reduced specific acitivity of 2-enoyl-CoA hydratase 2 when expressed in Saccharomyces cerevisiae
H532R
-
site-directed mutagenesis, inactive mutant, the mutation disrupts active site architecture
I516T
-
site-directed mutagenesis, the mutation disrupts dimerization, the mutant shows reduced activity
I559V
-
site-directed mutagenesis, the mutation does not affect the enzyme
L405P
-
site-directed mutagenesis, inactive mutant, the mutation disrupts ligand interaction
N457D
-
site-directed mutagenesis, the mutant shows reduced activity
N457Y
-
site-directed mutagenesis, the mutation disrupts domain folding, the mutant shows reduced activity
P529L
-
site-directed mutagenesis, inactive mutant, the mutation disrupts active site architecture
R506C
-
site-directed mutagenesis, inactive mutant, the mutation disrupts dimerization
R506H
-
site-directed mutagenesis, inactive mutant, the mutation disrupts dimerization
W511R
-
site-directed mutagenesis, the mutation does not affect the enzyme
Y347A
-
inactive mutant enzyme
Y410A
-
reduced specific acitivity of 2-enoyl-CoA hydratase 2 when expressed in Saccharomyces cerevisiae
Y505A
-
inactive mutant enzyme
I72V
site-directed mutagenesis, the mutant has an increased preference for enoyl-CoAs with longer chain lengths compared to wild-type broadening the substrate specificity range, PHA accumulation in recombinant Escherichia coli LS5218 harboring parental or Val72/Ile72 mutant genes of phaJ1, overview
V72I
site-directed mutagenesis, the mutant has an increased preference for enoyl-coenzyme A (CoA) elements with shorter chain lengths compared to wild-type narrowing the substrate specificity range, PHA accumulation in recombinant Escherichia coli LS5218 harboring parental or Val72/Ile72 mutant genes of phaJ1, overview
R251A
-
site-directed mutagenesis, the mutant shows decreased labeling efficiency in photoaffinity labeling of substrate binding sites with photophores compared to the wild-type enzyme, overview
W249A
-
site-directed mutagenesis, the mutant shows decreased labeling efficiency in photoaffinity labeling of substrate binding sites with photophores compared to the wild-type enzyme, overview
W249G
-
site-directed mutagenesis, the mutant shows decreased labeling efficiency in photoaffinity labeling of substrate binding sites with photophores compared to the wild-type enzyme, overview
R251A
-
site-directed mutagenesis, the mutant shows decreased labeling efficiency in photoaffinity labeling of substrate binding sites with photophores compared to the wild-type enzyme, overview
-
W249A
-
site-directed mutagenesis, the mutant shows decreased labeling efficiency in photoaffinity labeling of substrate binding sites with photophores compared to the wild-type enzyme, overview
-
W249G
-
site-directed mutagenesis, the mutant shows decreased labeling efficiency in photoaffinity labeling of substrate binding sites with photophores compared to the wild-type enzyme, overview
-
DELTA629-990
truncated version (lacking the carboxyl-terminal 271 amino acids). The truncated form contains only the D-3-hydroxyacyl-CoA dehydrogenase activity
additional information
mutagenesis of fugu5-1 seeds with heavy-ion irradiation and screening of mutations that restrain compensated cell enlargement (CCE) to gain insight into the genetic pathway(s) involved in CCE. Mutant A#3-1 has a cell size that is severely reduced, but the cell number remains similar to that of original fugu5-1. The cell number decreases in A#3-1 single mutant (A#3-1sm), similar to that of fugu5-1, but cell size is almost equal to that of the wild-type. A#3-1 mutation does not affect CCE in other compensation exhibiting mutant backgrounds, such as an3-4 and fugu2-1/fas1-6. Subsequent map-based cloning combined with genome sequencing and HRM curve analysis identified enoyl-CoA hydratase 2 (ECH2) as the causal gene of A#3-1. The above phenotypes are consistently observed in the ech2-1 allele and supplying sucrose restores the morphological and cellular phenotypes in fugu5-1, ech2-1, A#3-1sm, fugu5-1 ech2-1, and A#3-1; fugu5-1. The ech2-1 mutant allele is indistinguishable from A#3-1sm and suppresses CCEin fugu5. Analysis of ech2-1 mutant. Enoyl-CoA hydratase 2 gene mutation causes the A#3-1sm phenotypes, overview
additional information
-
mutagenesis of fugu5-1 seeds with heavy-ion irradiation and screening of mutations that restrain compensated cell enlargement (CCE) to gain insight into the genetic pathway(s) involved in CCE. Mutant A#3-1 has a cell size that is severely reduced, but the cell number remains similar to that of original fugu5-1. The cell number decreases in A#3-1 single mutant (A#3-1sm), similar to that of fugu5-1, but cell size is almost equal to that of the wild-type. A#3-1 mutation does not affect CCE in other compensation exhibiting mutant backgrounds, such as an3-4 and fugu2-1/fas1-6. Subsequent map-based cloning combined with genome sequencing and HRM curve analysis identified enoyl-CoA hydratase 2 (ECH2) as the causal gene of A#3-1. The above phenotypes are consistently observed in the ech2-1 allele and supplying sucrose restores the morphological and cellular phenotypes in fugu5-1, ech2-1, A#3-1sm, fugu5-1 ech2-1, and A#3-1; fugu5-1. The ech2-1 mutant allele is indistinguishable from A#3-1sm and suppresses CCEin fugu5. Analysis of ech2-1 mutant. Enoyl-CoA hydratase 2 gene mutation causes the A#3-1sm phenotypes, overview
-
additional information
in an in vivo assay using Escherichia coli as a host for polyhydroxyalkanoate (PHA) accumulation, the recombinant strain expressing PhaJYB4 and PHA synthase leads to increased PHA accumulation, suggesting that PhaJYB4 functioned as a monomer supplier. The pha cluster from Bacillus cereus strain YB-4 functions to accumulate PHA in Escherichia coli, but it does not function when the phaJYB4 gene is deleted. The recombinant strain utilizes butyrate, valerate, hexanoate, and dodecanoate for PHA synthesis
additional information
-
in an in vivo assay using Escherichia coli as a host for polyhydroxyalkanoate (PHA) accumulation, the recombinant strain expressing PhaJYB4 and PHA synthase leads to increased PHA accumulation, suggesting that PhaJYB4 functioned as a monomer supplier. The pha cluster from Bacillus cereus strain YB-4 functions to accumulate PHA in Escherichia coli, but it does not function when the phaJYB4 gene is deleted. The recombinant strain utilizes butyrate, valerate, hexanoate, and dodecanoate for PHA synthesis
additional information
-
in an in vivo assay using Escherichia coli as a host for polyhydroxyalkanoate (PHA) accumulation, the recombinant strain expressing PhaJYB4 and PHA synthase leads to increased PHA accumulation, suggesting that PhaJYB4 functioned as a monomer supplier. The pha cluster from Bacillus cereus strain YB-4 functions to accumulate PHA in Escherichia coli, but it does not function when the phaJYB4 gene is deleted. The recombinant strain utilizes butyrate, valerate, hexanoate, and dodecanoate for PHA synthesis
-
additional information
-
CtMfe2p(dha+bdelta) labelled with selenomethionine (SeMet), the plasmid pET3a::CtMfe2p(dha+bdelta) is transformed to the methionine-auxotrophic Escherichia coli strain B834(DE3). The incorporation of SeMet into the structure does not affect the hydratase 2 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 due to modifications enabling the biosynthesis of P(3HB-co-3HHx) composed of a larger 3HHx fraction without a negative impact on cell growth and PHA production on soybean oil, especially when phaJ4aRe or phaJ4bRe is tandemly introduced with phaJAc from Aeromonas caviae. Introduction of phaJ4aRe or phaJ4bRe into the Ralstonia eutropha strains using a broad-host-range vector enhances the 3HHx composition of the copolyesters, but the introduction of phaJ4cRe does not
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 due to modifications enabling the biosynthesis of P(3HB-co-3HHx) composed of a larger 3HHx fraction without a negative impact on cell growth and PHA production on soybean oil, especially when phaJ4aRe or phaJ4bRe is tandemly introduced with phaJAc from Aeromonas caviae. Introduction of phaJ4aRe or phaJ4bRe into the Ralstonia eutropha strains using a broad-host-range vector enhances the 3HHx composition of the copolyesters, but the introduction of phaJ4cRe does not
-
additional information
polyhydroxyalkanoate contents are slightly reduced in a phaJ deletion mutant DELTAphaJ1 compared to wild-type. phaJ1 gene complementation is performed in Haloferax mediterranei EPSDELTAphaJ1. GC analysis demonstrates that the mutant strain Haloferax mediterranei EPSDELTAphaJ1 utilizes much less amount of accumulated PHA than that of the wild-type Haloferax mediterranei EPS. In contrast, compared to the strain Haloferax mediterranei EPSDELTAphaJ (pWL502) harboring empty plasmid, the phaJ1 complementation strain Haloferax mediterranei EPSDELTAphaJ1 (pWLJ1) harboring the PhaJ1-expression plasmid significantly increases PHA degradation
additional information
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polyhydroxyalkanoate contents are slightly reduced in a phaJ deletion mutant DELTAphaJ1 compared to wild-type. phaJ1 gene complementation is performed in Haloferax mediterranei EPSDELTAphaJ1. GC analysis demonstrates that the mutant strain Haloferax mediterranei EPSDELTAphaJ1 utilizes much less amount of accumulated PHA than that of the wild-type Haloferax mediterranei EPS. In contrast, compared to the strain Haloferax mediterranei EPSDELTAphaJ (pWL502) harboring empty plasmid, the phaJ1 complementation strain Haloferax mediterranei EPSDELTAphaJ1 (pWLJ1) harboring the PhaJ1-expression plasmid significantly increases PHA degradation
additional information
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polyhydroxyalkanoate contents are slightly reduced in a phaJ deletion mutant DELTAphaJ1 compared to wild-type. phaJ1 gene complementation is performed in Haloferax mediterranei EPSDELTAphaJ1. GC analysis demonstrates that the mutant strain Haloferax mediterranei EPSDELTAphaJ1 utilizes much less amount of accumulated PHA than that of the wild-type Haloferax mediterranei EPS. In contrast, compared to the strain Haloferax mediterranei EPSDELTAphaJ (pWL502) harboring empty plasmid, the phaJ1 complementation strain Haloferax mediterranei EPSDELTAphaJ1 (pWLJ1) harboring the PhaJ1-expression plasmid significantly increases PHA degradation
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additional information
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mutant constructs are tested for complementation in Saccharomyces cerevisiae
additional information
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site-directed mutagenesis is used for construction of mutants corresponding to 17 reported missense mutations of multifunctional enzyme type 2 hydratase. Some mutants are almost or completely inactive causing the D-bifunctional protein deficiency type II
additional information
construction of three chimeric PhaJ1 enzymes, composed from Pseudomonas aeruginosa and Pseudomonas putida isoforms. All chimera show significant hydratase activity, and their substrate preferences is within the range exhibited by the parental PhaJ1 enzymes
additional information
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construction of three chimeric PhaJ1 enzymes, composed from Pseudomonas aeruginosa and Pseudomonas putida isoforms. All chimera show significant hydratase activity, and their substrate preferences is within the range exhibited by the parental PhaJ1 enzymes
additional information
construction of three chimeric PhaJ1 enzymes, composed from the enzymes from Pseudomonas putida and Pseudomonas aeruginosa, PhaJ1Pp and PhaJ1Pa. All mutants show significant hydratase activity, and their substrate preferences are within the range exhibited by the parental PhaJ1 enzymes
additional information
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construction of three chimeric PhaJ1 enzymes, composed from the enzymes from Pseudomonas putida and Pseudomonas aeruginosa, PhaJ1Pp and PhaJ1Pa. All mutants show significant hydratase activity, and their substrate preferences are within the range exhibited by the parental PhaJ1 enzymes
additional information
construction of three chimeric PhaJ1 enzymes, composed from Pseudomonas aeruginosa and Pseudomonas putida isoforms. All chimera show significant hydratase activity, and their substrate preferences is within the range exhibited by the parental PhaJ1 enzymes
additional information
construction of three chimeric PhaJ1 enzymes, composed from Pseudomonas aeruginosa and Pseudomonas putida isoforms. All chimera show significant hydratase activity, and their substrate preferences is within the range exhibited by the parental PhaJ1 enzymes
additional information
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construction of three chimeric PhaJ1 enzymes, composed from Pseudomonas aeruginosa and Pseudomonas putida isoforms. All chimera show significant hydratase activity, and their substrate preferences is within the range exhibited by the parental PhaJ1 enzymes
additional information
construction of three chimeric PhaJ1 enzymes, composed from the enzymes from Pseudomonas putida and Pseudomonas aeruginosa, PhaJ1Pp and PhaJ1Pa. All mutants show significant hydratase activity, and their substrate preferences are within the range exhibited by the parental PhaJ1 enzymes
additional information
construction of three chimeric PhaJ1 enzymes, composed from the enzymes from Pseudomonas putida and Pseudomonas aeruginosa, PhaJ1Pp and PhaJ1Pa. All mutants show significant hydratase activity, and their substrate preferences are within the range exhibited by the parental PhaJ1 enzymes
additional information
-
construction of three chimeric PhaJ1 enzymes, composed from the enzymes from Pseudomonas putida and Pseudomonas aeruginosa, PhaJ1Pp and PhaJ1Pa. All mutants show significant hydratase activity, and their substrate preferences are within the range exhibited by the parental PhaJ1 enzymes
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a truncated version (amino acid residues 318-735) of perMFE-2 is expressed in Escherichia coli BL21(DE3) plysS cells as a recombinant protein
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AtECH2 contains a peroxisome targeting signal at the C-terminal end, is addressed to the peroxisome in Saccharomyces cerevisiae, and a fusion protein between AtECH2 and a fluorescent protein is targeted to peroxisomes in onion cells. To assess the peroxisomal addressing of AtECH2, a fusion protein between an EYFP at the N terminus and AtECH2 at the C terminus is constructed and expressed under the control of a double cauliflower mosaic virus (CaMV) 35 S viral promoter to allow transient expression of the fusion protein in onion cells following biolistic bombardment. The fluorescence is examined by confocal microscopy after 12 h
expressed in Escherichia coli BL21(DE3)
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expression in Escherichia coli BL21 (DE3)
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expression in Escherichia coli BL21(DE3)
expression in Pichia pastoris
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expression of wild-type and mutant C-terminally His6-tagged MFE2s in Escherichia coli
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expression of wild-type and mutant hydratase domains of multifunctional enzyme type 2 hydratase as GFP-tagged protein in Escherichia coli strain JM109
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gene CG3415, Drosophila melanogaster MFE-2 complements a Saccharomyces cerevisiae MFE-2 deletion strain, functional expression of His-tagged MFE-2 in Escherichia coli strain BL21(DE3) pLysS
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gene ECH2, DNA and amino acid sequence determination and analysis, map-based cloning
gene phaJ or HFX_1483, DNA and amino acid sequence determination and analysis, genetic analysis of putative R-ECH homologous proteins encoded by genes HFX_2901, 5217, 6361, and 6433,
gene phaJ1, sequence comparison, recombinant expression of wild-type and mutant enzymes in Escherichia coli strains DH5alpha or JM109, and LS5218, overexpression of the enzyme in Escherichia coli strain BL21(DE3)
gene phaJ_1, DNA and amino acid sequence determination and analysis, sequence comparisons, the gene encoding MaoC-like protein locates in the pha cluster, functional recombinant expression in Escherichia coli strains DH5alpha and LS5218
overexpression of the three His6-tagged PhaJ4 homologues individually in Escherichia coli strain BL21(DE3)
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wild type (HsMFE-2) and its variants are expressed in Saccharomyces cerevisiae, the recombinant HsMFE-2(dhdelta) and its variants are expressed in Escherichia coli BL21(DE3)pLysS
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gene phaJ1, sequence comparison, recombinant expression of wild-type and mutant enzymes in Escherichia coli strains DH5alpha or JM109, and LS5218, overexpression of the enzyme in Escherichia coli strain BL21(DE3)
gene phaJ1, sequence comparison, recombinant expression of wild-type and mutant enzymes in Escherichia coli strains DH5alpha or JM109, and LS5218, overexpression of the enzyme in Escherichia coli strain BL21(DE3)
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