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

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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:
Homo sapiens
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
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-enoyl-CoA hydratase
2-octenoyl coenzyme A hydrase
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-
-
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acyl coenzyme A hydrase
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-
-
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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
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-
-
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crotonyl hydrase
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-
-
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D-3-hydroxyacyl-CoA dehydratase
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-
-
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ECHS1
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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-
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enoyl coenzyme A hydratase
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enoyl hydrase
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enoyl-CoA hydratase
enoyl-CoA hydratase short chain 1
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hydratase, enoyl coenzyme A
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mitochondrial short-chain enoyl-CoA hydratase
the classification is ambiguous because the stereochemistry is not exactly determined
mitochondrial short-chain enoyl-CoA hydratase-1
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short chain enoyl coenzyme A hydratase
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-
-
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short-chain enoyl-CoA hydratase
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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-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl-CoA + H2O
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
elimination
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-
-
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hydration
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-
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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
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
4-(N,N-dimethylamino)cinnamoyl-CoA + H2O
?
show the reaction diagram
-
-
-
?, r
crotonyl-CoA + H2O
(3S)-hydroxybutyryl-CoA
show the reaction diagram
-
-
-
r
crotonyl-CoA + H2O
3-hydroxybutyryl-CoA
show the reaction diagram
tiglyl-CoA + H2O
3-hydroxy-2-methylbutanoyl-CoA
show the reaction diagram
low activity
-
-
r
additional information
?
-
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
4-(N,N-dimethylamino)cinnamoyl-CoA + H2O
?
show the reaction diagram
-
-
-
?
crotonyl-CoA + H2O
(3S)-hydroxybutyryl-CoA
show the reaction diagram
-
-
-
r
crotonyl-CoA + H2O
3-hydroxybutyryl-CoA
show the reaction diagram
-
-
-
r
tiglyl-CoA + H2O
3-hydroxy-2-methylbutanoyl-CoA
show the reaction diagram
low activity
-
-
r
additional information
?
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
the enzyme is controlled by feed-back inhibition, overview
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
9
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
physiological function
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
ECHA_HUMAN
763
0
83000
Swiss-Prot
Mitochondrion (Reliability: 1)
ECHM_HUMAN
290
0
31387
Swiss-Prot
Mitochondrion (Reliability: 1)
ECHP_HUMAN
723
0
79495
Swiss-Prot
Mitochondrion (Reliability: 5)
E9KL44_HUMAN
763
0
83000
TrEMBL
Mitochondrion (Reliability: 1)
B4DRH6_HUMAN
717
0
78315
TrEMBL
Mitochondrion (Reliability: 1)
A0A2R8Y4F5_HUMAN
728
0
79467
TrEMBL
Mitochondrion (Reliability: 1)
H0YFD6_HUMAN
792
0
86372
TrEMBL
Mitochondrion (Reliability: 1)
AUHM_HUMAN
339
0
35609
Swiss-Prot
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
460000
-
about, enoyl-CoA hydratase complex, gel filtration
49291
-
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
SUBUNIT
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
-
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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A3D/F279S
naturally occuring mutations, identification of heterozygous ECHS1 mutations c.836T>C (novel) (p.F279S) and and c.8C>A (p.A3D) identified by whole exome sequencing, lethal neonatal case. SCEH deficiency is confirmed with very low SCEH activity in fibroblasts and nearly absent immunoreactivity of SCEH. The patient has a severe neonatal course with elevated blood and cerebrospinal fluid (CSF) lactate and pyruvate concentrations, high plasma alanine and slightly low plasma cystine. 2-Methyl-2,3-dihydroxybutyric acid is markedly elevated as are metabolites of the three branched-chain ketoacids on urine organic acids analysis. These urine metabolites notably decrease when lactic acidosis decreases in blood. Lymphocyte pyruvate dehydrogenase complex (PDC) activity is deficient, but PDC and 2-oxoglutarate dehydrogenase complex activities in cultured fibroblasts are normal. Oxidative phosphorylation analysis on intact digitonin-permeabilized fibroblasts is suggestive of slightly reduced PDC activity relative to control range in mitochondria
L230F
naturally occuring mutation
additional information
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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gene ECHS1, located on chromosome 10, genotyping
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kanazawa, M.; Ohtake, A.; Abe, H.; Yamamoto, S.; Satoh, Y.; Takayanagi, M.; Niimi, H.; Mori, M.; Hashimoto, T.
Molecular cloning and sequence analysis of the cDNA for human mitochondrial short-chain enoyl-CoA hydratase
Enzyme Protein
47
9-13
1993
Homo sapiens (P30084), Homo sapiens
Manually annotated by BRENDA team
Hiromasa, Y.; Yan, X.; Roche, T.E.
Specific ion influences on self-association of pyruvate dehydrogenase kinase isoform 2 (PDHK2), binding of PDHK2 to the L2 lipoyl domain, and effects of the lipoyl group-binding site inhibitor, Nov3r
Biochemistry
47
2312-2324
2008
Homo sapiens, Mus musculus, Rattus norvegicus
Manually annotated by BRENDA team
Fould, B.; Garlatti, V.; Neumann, E.; Fenel, D.; Gaboriaud, C.; Arlaud, G.J.
Structural and functional characterization of the recombinant human mitochondrial trifunctional protein
Biochemistry
49
8608-8617
2010
Homo sapiens
Manually annotated by BRENDA team
Liu, X.; Feng, R.; Du, L.
The role of enoyl-CoA hydratase short chain 1 and peroxiredoxin 3 in PP2-induced apoptosis in human breast cancer MCF-7 cells
FEBS Lett.
584
3185-3192
2010
Homo sapiens
Manually annotated by BRENDA team
Mohrig, J.R.; Reiter, N.J.; Kirk, R.; Zawadski, M.R.; Lamarre-Vincent, N.
Effect of buffer general acid-base catalysis on the stereoselectivity of ester and thioester H/D exchange in D2O
J. Am. Chem. Soc.
133
5124-5128
2011
Homo sapiens
Manually annotated by BRENDA team
Zhang, Y.; Yang, X.; Yu, H.; Ma, G.
Theoretical insight into the catalytic mechanism of enoyl-CoA hydratase
Acta Chim. Sin.
75
494-500
2017
Homo sapiens (P30084)
-
Manually annotated by BRENDA team
Al Mutairi, F.; Shamseldin, H.E.; Alfadhel, M.; Rodenburg, R.J.; Alkuraya, F.S.
A lethal neonatal phenotype of mitochondrial short-chain enoyl-CoA hydratase-1 deficiency
Clin. Genet.
91
629-633
2017
Homo sapiens (P30084), Homo sapiens
Manually annotated by BRENDA team
Bedoyan, J.K.; Yang, S.P.; Ferdinandusse, S.; Jack, R.M.; Miron, A.; Grahame, G.; DeBrosse, S.D.; Hoppel, C.L.; Kerr, D.S.; Wanders, R.J.A.
Lethal neonatal case and review of primary short-chain enoyl-CoA hydratase (SCEH) deficiency associated with secondary lymphocyte pyruvate dehydrogenase complex (PDC) deficiency
Mol. Genet. Metab.
120
342-349
2017
Homo sapiens (P30084)
Manually annotated by BRENDA team