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
4.2.1.74
-
RECOMMENDED NAME
GeneOntology No.
long-chain-enoyl-CoA hydratase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
a long-chain (3S)-3-hydroxyacyl-CoA = a long-chain trans-2-enoyl-CoA + H2O
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
addition
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
Fatty acid degradation
-
Fatty acid elongation
-
Metabolic pathways
-
pyruvate fermentation to hexanol
-
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.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
2-enoyl-CoA hydratase 2
-
-
-
-
2-enoyl-CoA hydratase 2
-
-
D-3-hydroxyacyl-CoA dehydratase
-
-
-
-
enoyl-CoA hydratase
-
a component enzyme of the trifunctional beta-oxidation complex, which is associated with the inner membrane of the mitochondria, contains long-chain specific activities of enoyl-CoA hydratase, L-3-hydroxyacyl-CoA dehydrogenase, and 3-ketoacyl-CoA thiolase
hydratase, long-chain enoyl coenzyme A
-
-
-
-
long chain enoyl coenzyme A hydratase
-
-
long chain enoyl coenzyme A hydratase
-
-
CAS REGISTRY NUMBER
COMMENTARY
62009-81-8
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
trans-2-decenoyl-CoA + H2O
(3S)-3-hydroxydecanoyl-CoA
show the reaction diagram
-
74% of the activity with trans-2-octenoyl-CoA
-
-
?
trans-2-decenoyl-CoA + H2O
(3S)-3-hydroxydecanoyl-CoA
show the reaction diagram
-
86% of the activity with trans-2-tetradecenoyl-CoA
-
-
?
trans-2-decenoyl-CoA + H2O
(3S)-3-hydroxydecanoyl-CoA
show the reaction diagram
-
Vmax is 74% of Vmax for trans-octenoyl-CoA
-
-
?
trans-2-dodecenoyl-CoA + H2O
(3S)-3-hydroxydodecanoyl-CoA
show the reaction diagram
-
42% of the activity with trans-2-octenoyl-CoA
-
-
?
trans-2-dodecenoyl-CoA + H2O
(3S)-3-hydroxydodecanoyl-CoA
show the reaction diagram
-
Vmax is 42% of Vmax for trans-octenoyl-CoA
-
-
?
trans-2-hexadecenoyl-CoA + H2O
(3S)-3-hydroxyhexadecanoyl-CoA
show the reaction diagram
-
50% of the activity with trans-2-tetradecenoyl-CoA
-
-
?
trans-2-hexenoyl-CoA + H2O
(3S)-3-hydroxyhexanoyl-CoA
show the reaction diagram
-
57% of the activity with trans-2-tetradecenoyl-CoA
-
-
?
trans-2-hexenoyl-CoA + H2O
(3S)-3-hydroxyhexanoyl-CoA
show the reaction diagram
-
78% of the activity with trans-2-octenoyl-CoA
-
-
?
trans-2-hexenoyl-CoA + H2O
(3S)-3-hydroxyhexanoyl-CoA
show the reaction diagram
-
Vmax is 78% of Vmax for trans-octenoyl-CoA
-
-
?
trans-2-octenoyl-CoA + H2O
(3S)-3-hydroxyoctanoyl-CoA
show the reaction diagram
-
best substrate
-
-
?
trans-2-octenoyl-CoA + H2O
(3S)-3-hydroxyoctanoyl-CoA
show the reaction diagram
-
71% of the activity with trans-2-tetradecenoyl-CoA
-
-
?
trans-2-tetradecenoyl-CoA + H2O
(3S)-3-hydroxytetradecanoyl-CoA
show the reaction diagram
-
best substrate
-
-
?
trans-2-tetradecenoyl-CoA + H2O
(3S)-3-hydroxytetradecanoyl-CoA
show the reaction diagram
-
Vmax is 34% of Vmax for trans-octenoyl-CoA
-
-
?
trans-2-tetradecenoyl-CoA + H2O
(3S)-3-hydroxytetradecenoyl-CoA
show the reaction diagram
-
34% of the activity with trans-2-octenoyl-CoA
-
-
?
enoyl-CoA + H2O
?
show the reaction diagram
-
-, inhibitory effects of acetylenic acids on fatty acid oxidation
-
-
?
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
-
-
-
additional information
?
-
-
activity with crotonyl-CoA is 1% of the activity with trans-decenoyl-CoA
-
-
-
additional information
?
-
-
no activity with crotonyl-CoA
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
enoyl-CoA + H2O
?
show the reaction diagram
-
-
-
-
?
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
N-Methylmaleimide
-
-
N-Methylmaleimide
-
1 mM, 69% inhibition, substrate: trans-octenoyl-CoA
oct-2-yn-4-enoyl-CoA
-
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
-
-
p-chloromercuribenzoate
-
1 mM, complete inhibition
iodoacetamide
-
5 mM, 16% inhibition
additional information
-
long chain enoyl-CoA hydratase of pig heart is not inhibited by acetoacetyl-CoA
-
additional information
-
no inhibition by acetoacetyl-CoA
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.024
-
trans-2-decenoyl-CoA
-
-
0.024
-
trans-2-decenoyl-CoA
-
25C
0.024
-
trans-2-dodecenoyl-CoA
-
-
0.024
-
trans-2-dodecenoyl-CoA
-
25C
0.045
-
trans-2-Hexenoyl-CoA
-
-
0.045
-
trans-2-Hexenoyl-CoA
-
25C
0.024
-
trans-2-octenoyl-CoA
-
-
0.024
-
trans-2-octenoyl-CoA
-
25C
0.024
-
trans-2-Tetradecenoyl-CoA
-
-
0.024
-
trans-2-Tetradecenoyl-CoA
-
25C
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.025
-
2-enoyl-CoA hydratase 2
-
irreversible inhibition, covalent modification shown by peptide mass spectrometry, catalytic residue Glu47 covalently labelled by the inhibitor
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
additional information
-
-
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
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
8.5
-
-
-
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7
9
-
pH 7: about 50% of maximal activity, pH 9: 80% of maximal activity
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
25
-
-
inhibition assay at
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
inner membrane
Manually annotated by BRENDA team
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 81000 + x * 45000, SDS-PAGE
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
- 20C, stable for several months
-
-20C, purified enzyme is stable for several months
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
gel filtration
-
partial
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expression in Escherichia coli
-