Information on EC 4.2.1.74 - long-chain-enoyl-CoA hydratase

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The expected taxonomic range for this enzyme is: Eutheria

EC NUMBER
COMMENTARY hide
4.2.1.74
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RECOMMENDED NAME
GeneOntology No.
long-chain-enoyl-CoA hydratase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
a long-chain (3S)-3-hydroxyacyl-CoA = a long-chain trans-2-enoyl-CoA + H2O
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
addition
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Fatty acid degradation
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Fatty acid elongation
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Metabolic pathways
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SYSTEMATIC NAME
IUBMB Comments
long-chain-(3S)-3-hydroxyacyl-CoA hydro-lyase
Acts in the reverse direction. The best substrate is oct-3-enoyl-CoA. Unlike EC 4.2.1.17 enoyl-CoA hydratase, it does not act on crotonoyl-CoA.
CAS REGISTRY NUMBER
COMMENTARY hide
62009-81-8
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
enoyl-CoA + H2O
?
show the reaction diagram
trans-2-decenoyl-CoA + H2O
(3S)-3-hydroxydecanoyl-CoA
show the reaction diagram
trans-2-dodecenoyl-CoA + H2O
(3S)-3-hydroxydodecanoyl-CoA
show the reaction diagram
trans-2-hexadecenoyl-CoA + H2O
(3S)-3-hydroxyhexadecanoyl-CoA
show the reaction diagram
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50% of the activity with trans-2-tetradecenoyl-CoA
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-
?
trans-2-hexenoyl-CoA + H2O
(3S)-3-hydroxyhexanoyl-CoA
show the reaction diagram
trans-2-octenoyl-CoA + H2O
(3S)-3-hydroxyoctanoyl-CoA
show the reaction diagram
trans-2-tetradecenoyl-CoA + H2O
(3S)-3-hydroxytetradecanoyl-CoA
show the reaction diagram
trans-2-tetradecenoyl-CoA + H2O
(3S)-3-hydroxytetradecenoyl-CoA
show the reaction diagram
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34% of the activity with trans-2-octenoyl-CoA
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?
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
enoyl-CoA + H2O
?
show the reaction diagram
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?
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
iodoacetamide
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5 mM, 16% inhibition
N-Methylmaleimide
oct-2-yn-4-enoyl-CoA
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irreversible inhibitor of 2-enoyl-CoA hydratase 2 (ECH2), covalent modification shown by peptide mass spectrometry, hydratase reaction of 2-enoyl-CoA hydratase 2 requires two protic residues, suggesting that the reaction follows a process of acid-base catalysis, only a weak reversible inhibitor of 2-enoyl-CoA hydratase 1 (ECH1), inhibitor concentrations up to 25 microM, inactivates also the beta-subunit of the mitochondrial trifunctional enzyme (MTP) and medium-chain acyl-CoA dehydrogenase (MCAD)
p-chloromercuribenzoate
additional information
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.024
trans-2-decenoyl-CoA
0.045
trans-2-hexenoyl-CoA
0.024
trans-2-octenoyl-CoA
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.025
2-enoyl-CoA hydratase 2
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irreversible inhibition, covalent modification shown by peptide mass spectrometry, catalytic residue Glu47 covalently labelled by the inhibitor
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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cloning and purification of truncated rat 2-enoyl-CoA hydratase 2 (ECH2), effect of oct-2-yn-4-enoyl-CoA on the catalytic activity of 2-enoyl-CoA hydratase 2, characterization of oct-2-yn-4-enoyl-CoA as a multifunctional enzyme inhibitor in fatty acid oxidation, inactivates long-chain fatty acid metabolism in both mitochondria and peroxisomes, corresponding oct-2-yn-4-enoic acid or its esters useful for in vivo studies for lead compound discovery
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 9
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pH 7: about 50% of maximal activity, pH 9: 80% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
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inhibition assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
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x * 81000 + x * 45000, SDS-PAGE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
- 20C, stable for several months
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-20C, purified enzyme is stable for several months
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gel filtration
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partial
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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