Information on EC 4.2.1.17 - enoyl-CoA hydratase and Organism(s) Homo sapiens

for references in articles please use BRENDA:EC4.2.1.17
Word Map on EC 4.2.1.17
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This record set is specific for:
Homo sapiens


The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea


The taxonomic range for the selected organisms is: Homo sapiens

EC NUMBER
COMMENTARY hide
4.2.1.17
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RECOMMENDED NAME
GeneOntology No.
enoyl-CoA hydratase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl-CoA + H2O
show the reaction diagram
reaction mechanism, overview
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
elimination
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hydration
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
(4Z,7Z,10Z,13Z,16Z)-docosapentaenoate biosynthesis (6-desaturase)
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(8E,10E)-dodeca-8,10-dienol biosynthesis
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4-coumarate degradation (aerobic)
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4-coumarate degradation (anaerobic)
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4-hydroxybenzoate biosynthesis III (plants)
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androstenedione degradation
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benzoyl-CoA degradation I (aerobic)
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docosahexaenoate biosynthesis III (6-desaturase, mammals)
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fatty acid beta-oxidation I
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fatty acid beta-oxidation II (peroxisome)
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fatty acid beta-oxidation VI (peroxisome)
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fatty acid salvage
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fermentation to 2-methylbutanoate
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jasmonic acid biosynthesis
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L-isoleucine degradation I
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L-valine degradation I
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methyl ketone biosynthesis (engineered)
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oleate beta-oxidation
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phenylacetate degradation I (aerobic)
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pyruvate fermentation to hexanol (engineered)
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Spodoptera littoralis pheromone biosynthesis
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unsaturated, even numbered fatty acid beta-oxidation
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adipate degradation
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alanine metabolism
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lipid metabolism
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phenylacetate degradation (aerobic)
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valine metabolism
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Fatty acid elongation
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Fatty acid degradation
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Valine, leucine and isoleucine degradation
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Geraniol degradation
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Lysine degradation
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Phenylalanine metabolism
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Benzoate degradation
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Tryptophan metabolism
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beta-Alanine metabolism
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alpha-Linolenic acid metabolism
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Aminobenzoate degradation
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Propanoate metabolism
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Butanoate metabolism
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Carbon fixation pathways in prokaryotes
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Limonene and pinene degradation
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Caprolactam degradation
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Biosynthesis of unsaturated fatty acids
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Metabolic pathways
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Biosynthesis of secondary metabolites
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Microbial metabolism in diverse environments
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Biosynthesis of antibiotics
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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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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
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the human mitochondrial trifunctional protein enoyl-CoA hydratase is a multienzyme complex involved in fatty acid beta-oxidation. The pathway shows feed-back inhibition, overview
physiological function
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recombinant enoyl-CoA hydratase displays 2-enoyl-CoA hydratase, L-3-hydroxyacyl-CoA dehydrogenase, EC 1.1.1.35, and 3-ketoacyl-CoA thiolase, EC 2.3.1.16, activities
additional information
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key role of ECHS1 and PRDX3 in regulation of 4-amino-5-(4-chlorophenyl)-7-(t-butyl)pyrazolo[3,4-d]pyrimidine, PP2, -induced apoptosis, downregulation of ECHS1 and PRDX3 potentiates PP2-induced apoptosis in MCF-7 cells, overview
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
additional information
?
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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the enzyme is controlled by feed-back inhibition, overview
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
9
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assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
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assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
UNIPROT
ORGANISM
P30084
Homo sapiens;
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
49291
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x * 79014, alpha-subunit, + x * 49291, beta-subunit, mass spectrometry and gel filtration
79014
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x * 79014, alpha-subunit, + x * 49291, beta-subunit, mass spectrometry and gel filtration
460000
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about, enoyl-CoA hydratase complex, gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oligomer
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x * 79014, alpha-subunit, + x * 49291, beta-subunit, mass spectrometry and gel filtration
additional information
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the alpha and beta subunits of the human mitochondrial trifunctional protein enoyl-CoA hydratase are part of the multienzyme complex, with predominance of alpha2beta2 and alpha4beta4 complexes, with higher order oligomers
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant alpha- and His-tagged beta-subunits from Escherichia coli by nickel affinity chromatography to homogeneity
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
co-expression of His-tagged alpha- and beta-subunits in Escherichia coli strain Rosetta-2(DE3)
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
ECHS1 expression level in patients with simple steatosis is reduced
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ECHS1 is downregulated by 4-amino-5-(4-chlorophenyl)-7-(t-butyl)pyrazolo[3,4-d]pyrimidine, i.e. PP2, that induces apoptosis in breast cancer MCF-7 cells
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
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ECHS1 down-regulation contributes to high-fat diet-induced hepatic steatosis