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Information on EC 4.2.1.17 - enoyl-CoA hydratase and Organism(s) Escherichia coli and UniProt Accession P76082

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EC Tree
     4 Lyases
         4.2 Carbon-oxygen lyases
             4.2.1 Hydro-lyases
                4.2.1.17 enoyl-CoA hydratase
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.
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This record set is specific for:
Escherichia coli
UNIPROT: P76082
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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
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2,3-dehydroadipyl-CoA hydratase
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2-enoyl-CoA hydratase
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-
-
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2-octenoyl coenzyme A hydrase
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-
-
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acyl coenzyme A hydrase
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beta-hydroxyacid dehydrase
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-
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beta-hydroxyacyl-CoA dehydrase
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-
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crotonase
crotonyl hydrase
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-
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D-3-hydroxyacyl-CoA dehydratase
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-
-
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ECH
-
-
-
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ECH-1
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S-specific
ECH-2
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R-specific
enol-CoA hydratase
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-
-
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Enoyl coenzyme A hydrase (D)
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-
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enoyl coenzyme A hydrase (L)
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enoyl coenzyme A hydratase
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enoyl hydrase
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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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SCEH
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-
-
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short chain enoyl coenzyme A hydratase
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-
-
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short-chain enoyl-CoA hydratase
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-
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trans-2-enoyl-CoA hydratase
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-
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unsaturated acyl-CoA hydratase
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-
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additional information
PaaF is a member of the crotonase superfamily
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
elimination
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-
-
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hydration
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-
-
-
SYSTEMATIC NAME
IUBMB Comments
(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.
CAS REGISTRY NUMBER
COMMENTARY hide
9027-13-8
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2,3-didehydroadipyl-CoA + H2O
(3S)-3-hydroxyadipyl-CoA
show the reaction diagram
2,3-octadienoyl-CoA + H2O
3-ketooctanoyl-CoA
show the reaction diagram
-
the classification is ambiguous because the stereochemistry is not exactly determined
-
-
?
2-trans-octenoyl-CoA + H2O
3-hydroxyoctanoyl-CoA
show the reaction diagram
-
the classification is ambiguous because the stereochemistry is not exactly determined
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-
?
3-octynoyl-CoA + H2O
3-ketooctanoyl-CoA
show the reaction diagram
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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
?
show the reaction diagram
-
the classification is ambiguous because the stereochemistry is not exactly determined
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-
?
decenoyl-CoA + H2O
?
show the reaction diagram
-
the classification is ambiguous because the stereochemistry is not exactly determined
-
-
?
trans-2-decenoyl-CoA + H2O
(3R)-3-hydroxydecanoyl-CoA
show the reaction diagram
-
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
-
?
trans-2-decenoyl-CoA + H2O
(3S)-3-hydroxydecanoyl-CoA
show the reaction diagram
-
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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-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
2,3-didehydroadipyl-CoA + H2O
(3S)-3-hydroxyadipyl-CoA
show the reaction diagram
-
-
-
r
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.008
2-decenoyl-CoA
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-
0.05
crotonyl-CoA
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
420
-
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
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene paaF encoded in the paa gene cluster
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
the enzyme catalyzes a reaction step of the beta-oxidation, as part of the catabolic gene cluster for phenylacetate degradation, overview
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
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
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
lipoprotein
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Binstock, J.F.; Schulz, H.
Fatty acid oxidation complex from Escherichia coli
Methods Enzymol.
71
403-411
1981
Escherichia coli
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team