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EC Tree
IUBMB Comments Acts in the reverse direction. With cis-compounds, yields (3R)-3-hydroxyacyl-CoA. cf. EC 4.2.1.74 long-chain-enoyl-CoA hydratase.
The taxonomic range for the selected organisms is: Escherichia coli The enzyme appears in selected viruses and cellular organisms
Synonyms
enoyl-coa hydratase, echs1, peroxisomal bifunctional enzyme, 2-enoyl-coa hydratase, amech, short-chain enoyl-coa hydratase, enoyl-coa hydratase/isomerase, beta-hydroxyacyl-coa dehydrase, enoyl-coenzyme a hydratase, enoyl coenzyme a hydratase 1,
more
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2,3-dehydroadipyl-CoA hydratase
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2-enoyl-CoA hydratase
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2-octenoyl coenzyme A hydrase
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acyl coenzyme A hydrase
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beta-hydroxyacid dehydrase
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beta-hydroxyacyl-CoA dehydrase
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D-3-hydroxyacyl-CoA dehydratase
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enol-CoA hydratase
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Enoyl coenzyme A hydrase (D)
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enoyl coenzyme A hydrase (L)
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enoyl coenzyme A hydratase
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hydratase, enoyl coenzyme A
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R-3-hydroxyacyl-CoA enoyl-CoA hydratases
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S-3-hydroxyacyl-CoA enoyl-CoA hydratases
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short chain enoyl coenzyme A hydratase
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short-chain enoyl-CoA hydratase
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trans-2-enoyl-CoA hydratase
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unsaturated acyl-CoA hydratase
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additional information
PaaF is a member of the crotonase superfamily
crotonase
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crotonase
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multienzyme of fatty acid oxidation contains in addition to enoyl-CoA hydratase, EC 1.1.1.35 (L-3-hydroxyacyl-CoA dehydrogenase), EC 2.3.1.16 (3-ketoacyl-CoA thiolase), EC 5.1.2.2 (3-hydroxyacyl-CoA epimerase) and EC 5.3.3.3 (DELTA3-cis-DELTA2-trans-enoyl-CoA isomerase)
crotonase
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the classification is ambiguous because the stereochemistry of the reaction product is not exactly determined
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KEGG
alpha-Linolenic acid metabolism , Aminobenzoate degradation , Benzoate degradation , beta-Alanine metabolism , Biosynthesis of secondary metabolites , Butanoate metabolism , Caprolactam degradation , Carbon fixation pathways in prokaryotes , Fatty acid degradation , Fatty acid elongation , Geraniol degradation , Limonene and pinene degradation , Lysine degradation , Microbial metabolism in diverse environments , Phenylalanine metabolism , Propanoate metabolism , Tryptophan metabolism , Valine, leucine and isoleucine degradation
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-, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -
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(3S)-3-hydroxyacyl-CoA hydro-lyase
Acts in the reverse direction. With cis-compounds, yields (3R)-3-hydroxyacyl-CoA. cf. EC 4.2.1.74 long-chain-enoyl-CoA hydratase.
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2,3-didehydroadipyl-CoA + H2O
(3S)-3-hydroxyadipyl-CoA
2,3-octadienoyl-CoA + H2O
3-ketooctanoyl-CoA
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the classification is ambiguous because the stereochemistry is not exactly determined
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2-trans-octenoyl-CoA + H2O
3-hydroxyoctanoyl-CoA
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the classification is ambiguous because the stereochemistry is not exactly determined
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3-octynoyl-CoA + H2O
3-ketooctanoyl-CoA
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2,3-octadienoyl-CoA is an intermediate. The classification is ambiguous because the stereochemistry is not exactly determined
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crotonyl-CoA + H2O
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the classification is ambiguous because the stereochemistry is not exactly determined
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decenoyl-CoA + H2O
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the classification is ambiguous because the stereochemistry is not exactly determined
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trans-2-decenoyl-CoA + H2O
(3R)-3-hydroxydecanoyl-CoA
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Escherichia coli enzyme activity is of the S-specific ECH-1 type
the distribution of R- and S-enantiomers of produced 3-hydroxydecanoate is in favour of the S-enantiomer in case of Escherichia coli
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trans-2-decenoyl-CoA + H2O
(3S)-3-hydroxydecanoyl-CoA
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Escherichia coli enzyme activity is of the S-specific ECH-1 type
the distribution of R- and S-enantiomers of produced 3-hydroxydecanoate is in favour of the S-enantiomer in case of Escherichia coli
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additional information
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development of a chiral high-performance liquid chromatography-tandem mass spectrometry method for analysis of stereospecificity of enoyl-coenzyme A hydratases/isomerases, including reaction of the 3-hydroxyl group on the chiral carbon with 3,5-dimethylphenyl isocyanate, resolving of the resulting urethane derivatives, and monitoring of the liberated free hydroxy fatty acid fragment ion, detailed overview
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2,3-didehydroadipyl-CoA + H2O
(3S)-3-hydroxyadipyl-CoA
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r
2,3-didehydroadipyl-CoA + H2O
(3S)-3-hydroxyadipyl-CoA
substrate and product identification by mass spectrometry
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r
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2,3-didehydroadipyl-CoA + H2O
(3S)-3-hydroxyadipyl-CoA
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r
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420
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hydration of 3-octynoyl-CoA
650
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hydration of 2,3-octadienoyl-CoA
973
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hydration of 2-trans-octenoyl-CoA
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gene paaF encoded in the paa gene cluster
UniProt
brenda
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metabolism
the enzyme catalyzes a reaction step of the beta-oxidation, as part of the catabolic gene cluster for phenylacetate degradation, overview
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160000
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multienzyme complex of fatty acid oxidation: EC 4.2.1.17/EC 1.1.1.35/EC2.3.1.16/EC 5.1.2.3/EC 5.3.3.3, gel filtration, non-denaturing PAGE
420000
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x * 420000, + x * 78000, two subunits are present in equimolar amounts, multienzyme complex of fatty acid oxidation: EC 4.2.1.17/EC1.1.1.35/EC 2.3.1.16/EC 5.1.2.3/EC 5.3.3.3, SDS-PAGE
78000
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x * 420000, + x * 78000, two subunits are present in equimolar amounts, multienzyme complex of fatty acid oxidation: EC 4.2.1.17/EC1.1.1.35/EC 2.3.1.16/EC 5.1.2.3/EC 5.3.3.3, SDS-PAGE
additional information
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MW of multienzyme complex of fatty acid oxidation, EC 4.2.1.17/EC 1.1.1.35/EC 2.3.1.16/EC 5.1.2.3/EC 5.3.3.3: 270000-300000 Da
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?
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x * 420000, + x * 78000, two subunits are present in equimolar amounts, multienzyme complex of fatty acid oxidation: EC 4.2.1.17/EC1.1.1.35/EC 2.3.1.16/EC 5.1.2.3/EC 5.3.3.3, SDS-PAGE
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lipoprotein
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multienzyme complex of fatty acid oxidation: EC4.2.1.17/EC1.1.1.35/EC2.3.1.16/EC5.1.2.3/EC5.3.3.3 contains phospholipid
lipoprotein
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63 nmol of lipid phosphate per mg of protein, phosphatidylethanolamine, phosphatidylglycerol, cardiolipin. Multienzyme complex of fatty acid oxidation: EC4.2.1.17/EC1.1.1.35/EC2.3.1.16/EC5.1.2.3/EC5.3.3.3 contains phospholipid
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multienzyme complex of fatty acid oxidation: EC4.2.1.17/EC1.1.1.35/EC2.3.1.16/EC5.1.2.3/EC5.3.3.3
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Pawar, S.; Schulz, H.
The structure of the multienzyme complex of fatty acid oxidation from Escherichia coli
J. Biol. Chem.
256
3894-3899
1981
Escherichia coli, Escherichia coli B / ATCC 11303
brenda
Yang, S.Y.; Li, J.; He, X.Y.; Cosloy, S.D.; Schulz, H.
Evidence that the fadB gene of the fadAB operon of Escherichia coli encodes 3-hydroxyacyl-coenzyme A (CoA) epimerase, DELTA3-cis-DELTA2-trans-enoyl-CoA isomerase, and enoyl-CoA hydratase in addition to 3-hydroxyacyl-CoA dehydrogenase
J. Bacteriol.
170
2543-2548
1988
Escherichia coli
brenda
Alipui, O.D.; Zhang, D.; Schulz, H.
Direct hydration of 3-octynoyl-CoA by crotonase: A missing link in Konrad Bloch's enzymatic studies with 3-alkynoyl thioesters
Biochem. Biophys. Res. Commun.
292
1171-1174
2002
Escherichia coli
brenda
Binstock, J.F.; Schulz, H.
Fatty acid oxidation complex from Escherichia coli
Methods Enzymol.
71
403-411
1981
Escherichia coli
brenda
Teufel, R.; Mascaraque, V.; Ismail, W.; Voss, M.; Perera, J.; Eisenreich, W.; Haehnel, W.; Fuchs, G.
Bacterial phenylalanine and phenylacetate catabolic pathway revealed
Proc. Natl. Acad. Sci. USA
107
14390-14395
2010
Escherichia coli (P76082), Pseudomonas putida, Pseudomonas sp., Pseudomonas sp. Y2
brenda
Abdel-Mawgoud, A.; Lepine, F.; Deziel, E.
A chiral high-performance liquid chromatography-tandem mass spectrometry method for the stereospecific analysis of enoyl-coenzyme A hydratases/isomerases
J. Chromatogr. A
1306
37-43
2013
Escherichia coli, Pseudomonas aeruginosa
brenda