4.2.1.119 (24E)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholest-24-enoyl-CoA + H2O reaction of the recombinant enzyme, protein converted rapidly Rattus norvegicus (24R,25R)-3alpha,7alpha,12alpha,24-tetrahydroxy-5beta-cholestanoyl-CoA a physiological intermediate in bile acid synthesis ? 375418 4.2.1.119 (2E)-2-decenoyl-CoA + H2O activity measurements are based on the formation of the magnesium complex of 3-ketoacyl-CoA from (2E)-2-decenoyl-CoA Candida tropicalis (3R)-3-hydroxydecanoyl-CoA - ? 395058 4.2.1.119 (2E)-2-enoyl-CoA + H2O - Rattus norvegicus (3R)-3-hydroxyacyl-CoA - r 394591 4.2.1.119 (2E)-2-enoyl-CoA + H2O - Saccharomyces cerevisiae (3R)-3-hydroxyacyl-CoA - ? 394591 4.2.1.119 (2E)-2-enoyl-CoA + H2O - Arabidopsis thaliana (3R)-3-hydroxyacyl-CoA - r 394591 4.2.1.119 (2E)-2-enoyl-CoA + H2O - Pseudomonas aeruginosa (3R)-3-hydroxyacyl-CoA - r 394591 4.2.1.119 (2E)-2-enoyl-CoA + H2O - Haloferax mediterranei (3R)-3-hydroxyacyl-CoA - r 394591 4.2.1.119 (2E)-2-enoyl-CoA + H2O - Pseudomonas putida (3R)-3-hydroxyacyl-CoA - r 394591 4.2.1.119 (2E)-2-enoyl-CoA + H2O - Bacillus cereus (3R)-3-hydroxyacyl-CoA - r 394591 4.2.1.119 (2E)-2-enoyl-CoA + H2O 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 Candida tropicalis (3R)-3-hydroxyacyl-CoA - ? 394591 4.2.1.119 (2E)-2-enoyl-CoA + H2O 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 Homo sapiens (3R)-3-hydroxyacyl-CoA - ? 394591 4.2.1.119 (2E)-2-enoyl-CoA + H2O - Bacillus cereus YB-4 (3R)-3-hydroxyacyl-CoA - r 394591 4.2.1.119 (2E)-2-enoyl-CoA + H2O - Haloferax mediterranei ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4 (3R)-3-hydroxyacyl-CoA - r 394591 4.2.1.119 (2E)-2-enoyl-CoA + H2O - Arabidopsis thaliana Col-0 (3R)-3-hydroxyacyl-CoA - r 394591 4.2.1.119 (2E)-butenoyl-CoA + H2O - Drosophila melanogaster (3R)-hydroxybutanoyl-CoA - ? 415832 4.2.1.119 (2E)-crotonyl-CoA + H2O - Pseudomonas aeruginosa (3R)-3-hydroxybutanoyl-CoA - r 444476 4.2.1.119 (2E)-crotonyl-CoA + H2O - Pseudomonas putida (3R)-3-hydroxybutanoyl-CoA - r 444476 4.2.1.119 (2E)-crotonyl-CoA + H2O - Bacillus cereus (3R)-3-hydroxybutanoyl-CoA - r 444476 4.2.1.119 (2E)-crotonyl-CoA + H2O - Bacillus cereus YB-4 (3R)-3-hydroxybutanoyl-CoA - r 444476 4.2.1.119 (2E)-decenoyl-CoA + H2O - Drosophila melanogaster (3R)-3-hydroxydecanoyl-CoA - ? 395063 4.2.1.119 (2E)-decenoyl-CoA + H2O - Rattus norvegicus (3R)-3-hydroxydecanoyl-CoA - ? 395063 4.2.1.119 (2E)-decenoyl-CoA + H2O - Arabidopsis thaliana (3R)-3-hydroxydecanoyl-CoA - r 395063 4.2.1.119 (2E)-enoyl-CoA + H2O - Drosophila melanogaster (3R)-hydroxyacyl-CoA - ? 390113 4.2.1.119 (2E)-enoyl-CoA + H2O straight-chain Rattus norvegicus (3R)-hydroxyacyl-CoA - ? 390113 4.2.1.119 (2E)-hexadecenoyl-CoA + H2O - Arabidopsis thaliana (3R)-3-hydroxyhexadecanoyl-CoA - ? 395066 4.2.1.119 (2E)-hexenoyl-CoA + H2O - Drosophila melanogaster (3R)-3-hydroxyhexanoyl-CoA - ? 395068 4.2.1.119 (2E)-hexenoyl-CoA + H2O - Rattus norvegicus (3R)-3-hydroxyhexanoyl-CoA - ? 395068 4.2.1.119 (2E)-hexenoyl-CoA + H2O - Arabidopsis thaliana (3R)-3-hydroxyhexanoyl-CoA - ? 395068 4.2.1.119 (2E)-oct-2-enoyl-CoA + H2O - Pseudomonas aeruginosa (R)-3-hydroxyoctanoyl-CoA - r 444480 4.2.1.119 (2E)-oct-2-enoyl-CoA + H2O - Pseudomonas putida (R)-3-hydroxyoctanoyl-CoA - r 444480 4.2.1.119 (3R)-3-hydroxyacyl-CoA - Rattus norvegicus (2E)-2-enoyl-CoA + H2O - ? 394595 4.2.1.119 (3R)-3-hydroxyacyl-CoA - Pseudomonas aeruginosa (2E)-2-enoyl-CoA + H2O - ? 394595 4.2.1.119 (3R)-3-hydroxyacyl-CoA - Cupriavidus necator (2E)-2-enoyl-CoA + H2O - ? 394595 4.2.1.119 (3R)-3-hydroxyacyl-CoA 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 Arabidopsis thaliana (2E)-2-enoyl-CoA + H2O - ? 394595 4.2.1.119 (3R)-3-hydroxyacyl-CoA a peroxisomal beta-oxidation intermediate Rattus norvegicus (2E)-2-enoyl-CoA + H2O - ? 394595 4.2.1.119 (3R)-3-hydroxyacyl-CoA 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 Cupriavidus necator (2E)-2-enoyl-CoA + H2O - ? 394595 4.2.1.119 (3R)-3-hydroxyacyl-CoA - Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1 (2E)-2-enoyl-CoA + H2O - ? 394595 4.2.1.119 (3R)-3-hydroxyacyl-CoA 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 Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1 (2E)-2-enoyl-CoA + H2O - ? 394595 4.2.1.119 (3R)-3-hydroxydecanoyl-CoA - Rattus norvegicus (2E)-2-decenoyl-CoA + H2O - r 395086 4.2.1.119 (3R)-3-hydroxydecanoyl-CoA - Pseudomonas aeruginosa (2E)-2-decenoyl-CoA + H2O - ? 395086 4.2.1.119 (3R)-3-hydroxyhexadecanoyl-CoA - Homo sapiens (2E)-2-hexadecenoyl-CoA + H2O - ? 429502 4.2.1.119 (3R)-3-hydroxyhexadecanoyl-CoA - Rattus norvegicus (2E)-2-hexadecenoyl-CoA + H2O - ? 429502 4.2.1.119 (R)-3-hydroxydecanoyl-CoA - Rattus norvegicus trans-2-decenoyl-CoA + H2O - r 407643 4.2.1.119 (R)-3-hydroxyoctanoyl-CoA no activity with (S)-3-hydroxyoctanoyl-CoA Homo sapiens octenoyl-CoA + H2O - r 403103 4.2.1.119 2-trans-butenoyl-CoA + H2O - Cucumis sativus (3R)-hydroxybutanoyl-CoA - ? 403642 4.2.1.119 2-trans-decenoyl-CoA + H2O - Cucumis sativus (3R)-3-hydroxydecanoyl-CoA - ? 403643 4.2.1.119 Crotonyl-CoA + H2O - Rattus norvegicus (3R)-3-Hydroxybutanoyl-CoA - ? 2030 4.2.1.119 Crotonyl-CoA + H2O ratio of hydration rates trans-2-decenoyl-CoA/crotonyl-CoA is 14.4 Rattus norvegicus (3R)-3-Hydroxybutanoyl-CoA - r 2030 4.2.1.119 crotonyl-CoA + H2O - Aeromonas caviae 3-hydroxybutanoyl-CoA - ? 18665 4.2.1.119 crotonyl-CoA + H2O - Aeromonas caviae (R)-3-hydroxybutanoyl-CoA - ? 404715 4.2.1.119 crotonyl-CoA + H2O very low activity with crotonyl-CoA Homo sapiens (R)-3-hydroxybutanoyl-CoA - r 404715 4.2.1.119 crotonyl-CoA + H2O activity is 7fold higher than activity with trans-decenoyl-CoA Rattus norvegicus ? - ? 404716 4.2.1.119 crotonyl-CoA + H2O the classification is ambiguous because the stereochemistry of the reaction product is not exactly determined Escherichia coli ? - ? 404716 4.2.1.119 dec-2-enoyl-CoA + H2O - Aeromonas caviae 3-hydroxydecanoyl-CoA - ? 18671 4.2.1.119 dec-2-enoyl-CoA + H2O 9-12% of the activity with hexenoyl-CoA, depending on preparation Homo sapiens (R)-3-hydroxydecanoyl-CoA - ? 404952 4.2.1.119 dodec-2-enoyl-CoA + H2O - Aeromonas caviae 3-hydroxydodecanoyl-CoA - ? 368255 4.2.1.119 dodec-2-enoyl-CoA + H2O 4-5% of the activity with hexenoyl-CoA, depending on preparation Homo sapiens (R)-3-hydroxydodecanoyl-CoA - ? 405042 4.2.1.119 hex-2-enoyl-CoA + H2O - Homo sapiens (R)-3-hydroxyhexanoyl-CoA - r 405415 4.2.1.119 hex-2-enoyl-CoA + H2O - Aeromonas caviae (R)-3-hydroxyhexanoyl-CoA - ? 405415 4.2.1.119 hexenoyl-CoA + H2O - Aeromonas caviae 3-hydroxyhexanoyl-CoA - ? 18667 4.2.1.119 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 Aeromonas caviae ? - ? 89 4.2.1.119 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 Candida tropicalis ? - ? 89 4.2.1.119 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 Candida tropicalis ? - ? 89 4.2.1.119 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 Escherichia coli ? - ? 89 4.2.1.119 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 Homo sapiens ? - ? 89 4.2.1.119 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 Rattus norvegicus ? - ? 89 4.2.1.119 additional information the enzyme is essential for polyhydroxyalkanoate biosynthesis Aeromonas caviae ? - ? 89 4.2.1.119 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 Candida tropicalis ? - ? 89 4.2.1.119 additional information no activity with (S)-3-hydroxyoctanoyl-CoA Homo sapiens ? - ? 89 4.2.1.119 additional information the (S)-3-hydroxy-CoA is not dehydrated Rattus norvegicus ? - ? 89 4.2.1.119 additional information the bifunctional peroxisomal multifunctional enzyme type 2 exhibits dehydrogenase and hydratase activity from separate entities Drosophila melanogaster ? - ? 89 4.2.1.119 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 Rattus norvegicus ? - ? 89 4.2.1.119 additional information MFE-2 structure-function studies, overview Drosophila melanogaster ? - ? 89 4.2.1.119 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 Pseudomonas aeruginosa ? - ? 89 4.2.1.119 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 Cupriavidus necator ? - ? 89 4.2.1.119 additional information method deleopment and optimization of a separation and detection method for (3R)- and (3S)-hydroxyacyl-CoAs Rattus norvegicus ? - ? 89 4.2.1.119 additional information the enzyme is specific for enoyl-CoAs of medium chain length Pseudomonas aeruginosa ? - ? 89 4.2.1.119 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 Pseudomonas aeruginosa ? - ? 89 4.2.1.119 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 Pseudomonas putida ? - ? 89 4.2.1.119 additional information PhaJYB4 activity is thought to be specific for short chain-length enoyl-CoA Bacillus cereus ? - ? 89 4.2.1.119 additional information PhaJYB4 activity is thought to be specific for short chain-length enoyl-CoA Bacillus cereus YB-4 ? - ? 89 4.2.1.119 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 Rattus norvegicus Wistar ? - ? 89 4.2.1.119 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 Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1 ? - ? 89 4.2.1.119 oct-2-enoyl-CoA + H2O - Aeromonas caviae 3-hydroxyoctanoyl-CoA - ? 18669 4.2.1.119 oct-2-enoyl-CoA + H2O - Aeromonas caviae (R)-3-hydroxyoctanoyl-CoA - ? 406227 4.2.1.119 oct-2-enoyl-CoA + H2O 30-40% of the activity with hexenoyl-CoA, depending on preparation Homo sapiens (R)-3-hydroxyoctanoyl-CoA - r 406227 4.2.1.119 pent-2-enoyl-CoA + H2O - Aeromonas caviae (R)-3-hydroxypentanoyl-CoA - ? 406348 4.2.1.119 tetradec-2-enoyl-CoA + H2O - Homo sapiens ? - ? 412963 4.2.1.119 trans-2-decenoyl-CoA - Candida tropicalis (3R)-hydroxydecanoyl-CoA + H2O - ? 406779 4.2.1.119 trans-2-decenoyl-CoA + H2O - Homo sapiens (3R)-3-hydroxydecanoyl-CoA - r 406777 4.2.1.119 trans-2-decenoyl-CoA + H2O ratio of hydration rates trans-2-decenoyl-CoA/crotonyl-CoA is 14.4 Rattus norvegicus (3R)-hydroxydecanoyl-CoA - r 406778 4.2.1.119 trans-2-hexadecenoyl-CoA - Candida tropicalis (3R)-hydroxyhexadecanoyl-CoA + H2O - ? 406782 4.2.1.119 trans-2-octenoyl-CoA + H2O - Aeromonas caviae 3-hydroxyoctanoyl-CoA - ? 368254 4.2.1.119 trans-dec-2-enoyl-CoA activity is 7fold lower than activity with crotonyl-CoA Rattus norvegicus ? - ? 406795