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Enzyme Nomenclature
Information on EC 4.2.1.74 - long-chain-enoyl-CoA hydratase
for references in articles please use BRENDA:EC4.2.1.74
Word Map on EC 4.2.1.74
- 4.2.1.74
- peroxisomal
-
beta-oxidation
-
hydration
- d-3-hydroxyacyl-coas
-
enoyl-coas
- trans-2-enoyl-coa
- acyl-coas
- tropicalis
-
polyunsaturated
-
short-chain
-
2,4-dienoyl-coa
- 3-ketoacyl-coa
-
epimerization
- mfe-2s
-
epimerase
-
3r-hydroxyacyl-coas
-
stereochemical
-
l-isomers
- crotonase
-
spiral
-
monofunctional
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bulkier
-
n-domain
-
straight-chain
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unliganded
-
thiolase
-
dehydrogenate
-
two-domain
-
2-trans-enoyl-coa
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The enzyme appears in viruses and cellular organisms
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EC NUMBER 
COMMENTARY 
4.2.1.74
-
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RECOMMENDED NAME
GeneOntology No.
long-chain-enoyl-CoA hydratase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
a long-chain (3S)-3-hydroxyacyl-CoA = a long-chain trans-2-enoyl-CoA + H2O
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
addition
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-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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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.
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CAS REGISTRY NUMBER
COMMENTARY
62009-81-8
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
trans-2-hexadecenoyl-CoA + H2O
(3S)-3-hydroxyhexadecanoyl-CoA
-
50% of the activity with trans-2-tetradecenoyl-CoA
-
-
?
trans-2-tetradecenoyl-CoA + H2O
(3S)-3-hydroxytetradecenoyl-CoA
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34% of the activity with trans-2-octenoyl-CoA
-
-
?
enoyl-CoA + H2O
?
-
inhibitory effects of acetylenic acids on fatty acid oxidation
-
-
?
trans-2-decenoyl-CoA + H2O
(3S)-3-hydroxydecanoyl-CoA
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74% of the activity with trans-2-octenoyl-CoA
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-
?
trans-2-decenoyl-CoA + H2O
(3S)-3-hydroxydecanoyl-CoA
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86% of the activity with trans-2-tetradecenoyl-CoA
-
-
?
trans-2-decenoyl-CoA + H2O
(3S)-3-hydroxydecanoyl-CoA
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Vmax is 74% of Vmax for trans-octenoyl-CoA
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-
?
trans-2-dodecenoyl-CoA + H2O
(3S)-3-hydroxydodecanoyl-CoA
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42% of the activity with trans-2-octenoyl-CoA
-
-
?
trans-2-dodecenoyl-CoA + H2O
(3S)-3-hydroxydodecanoyl-CoA
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Vmax is 42% of Vmax for trans-octenoyl-CoA
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-
?
trans-2-hexenoyl-CoA + H2O
(3S)-3-hydroxyhexanoyl-CoA
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57% of the activity with trans-2-tetradecenoyl-CoA
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-
?
trans-2-hexenoyl-CoA + H2O
(3S)-3-hydroxyhexanoyl-CoA
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78% of the activity with trans-2-octenoyl-CoA
-
-
?
trans-2-hexenoyl-CoA + H2O
(3S)-3-hydroxyhexanoyl-CoA
-
Vmax is 78% of Vmax for trans-octenoyl-CoA
-
-
?
trans-2-octenoyl-CoA + H2O
(3S)-3-hydroxyoctanoyl-CoA
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71% of the activity with trans-2-tetradecenoyl-CoA
-
-
?
trans-2-tetradecenoyl-CoA + H2O
(3S)-3-hydroxytetradecanoyl-CoA
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best substrate
-
-
?
trans-2-tetradecenoyl-CoA + H2O
(3S)-3-hydroxytetradecanoyl-CoA
-
Vmax is 34% of Vmax for trans-octenoyl-CoA
-
-
?
additional information
?
-
-
activity of the trifunctional enzyme complex with C4 substrates is less than 2% of the long-chain activities. The trifunctional beta-oxidation complex contains long-chain specific activities of enoyl-CoA hydratase, L-3-hydroxyacyl-CoA dehydrogenase, and 3-ketoacyl-CoA thiolase
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additional information
?
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activity with crotonyl-CoA is 1% of the activity with trans-decenoyl-CoA
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-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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)
additional information
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long chain enoyl-CoA hydratase of pig heart is not inhibited by acetoacetyl-CoA
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additional information
-
long chain enoyl-CoA hydratase of pig heart is not inhibited by acetoacetyl-CoA
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
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
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
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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LINKS TO OTHER DATABASES (specific for EC-Number 4.2.1.74)
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