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EC Tree
IUBMB Comments Acts in the reverse direction. The best substrate for the porcine enzyme is oct-2-enoyl-CoA. Unlike EC 4.2.1.17 enoyl-CoA hydratase, it does not act on crotonoyl-CoA.
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
2-enoyl-coa hydratase 2, d-3-hydroxyacyl-coa dehydratase,
more
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D-3-hydroxyacyl-CoA dehydratase
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enoyl-CoA hydratase
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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
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incorrect
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long chain enoyl coenzyme A hydratase
long-chain enoyl coenzyme A hydratase
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incorrect
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long-chain-(3S)-3-hydroxyacyl-CoA hydro-lyase
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incorrect
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long-chain-enoyl-CoA hydratase
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incorrect
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2-enoyl-CoA hydratase 2
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2-enoyl-CoA hydratase 2
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long chain enoyl coenzyme A hydratase
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long chain enoyl coenzyme A hydratase
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a medium-chain (3S)-3-hydroxyacyl-CoA = a medium-chain trans-2-enoyl-CoA + H2O
a medium-chain acyl-CoA = an acyl-CoA thioester where the acyl chain contains 6 to 12 carbon atoms.
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medium-chain-(3S)-3-hydroxyacyl-CoA hydro-lyase
Acts in the reverse direction. The best substrate for the porcine enzyme is oct-2-enoyl-CoA. Unlike EC 4.2.1.17 enoyl-CoA hydratase, it does not act on crotonoyl-CoA.
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trans-2-decenoyl-CoA + H2O
(3S)-3-hydroxydecanoyl-CoA
trans-2-dodecenoyl-CoA + H2O
(3S)-3-hydroxydodecanoyl-CoA
trans-2-hexadecenoyl-CoA + H2O
(3S)-3-hydroxyhexadecanoyl-CoA
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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
trans-2-octenoyl-CoA + H2O
(3S)-3-hydroxyoctanoyl-CoA
trans-2-tetradecenoyl-CoA + H2O
(3S)-3-hydroxytetradecanoyl-CoA
additional information
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enoyl-CoA + H2O
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enoyl-CoA + H2O
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inhibitory effects of acetylenic acids on fatty acid oxidation
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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
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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
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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
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trans-2-hexenoyl-CoA + H2O
(3S)-3-hydroxyhexanoyl-CoA
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Vmax is 78% of Vmax for trans-octenoyl-CoA
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trans-2-octenoyl-CoA + H2O
(3S)-3-hydroxyoctanoyl-CoA
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best substrate
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trans-2-octenoyl-CoA + H2O
(3S)-3-hydroxyoctanoyl-CoA
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71% of the activity with trans-2-tetradecenoyl-CoA
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trans-2-tetradecenoyl-CoA + H2O
(3S)-3-hydroxytetradecanoyl-CoA
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best substrate
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trans-2-tetradecenoyl-CoA + H2O
(3S)-3-hydroxytetradecanoyl-CoA
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34% of the activity with trans-2-octenoyl-CoA
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trans-2-tetradecenoyl-CoA + H2O
(3S)-3-hydroxytetradecanoyl-CoA
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Vmax is 34% of Vmax for trans-octenoyl-CoA
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additional information
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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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additional information
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no activity with crotonyl-CoA
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enoyl-CoA + H2O
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iodoacetamide
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5 mM, 16% inhibition
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)
N-Methylmaleimide
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N-Methylmaleimide
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1 mM, 69% inhibition, substrate: trans-octenoyl-CoA
p-chloromercuribenzoate
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p-chloromercuribenzoate
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1 mM, complete inhibition
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
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long chain enoyl-CoA hydratase of pig heart is not inhibited by acetoacetyl-CoA
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additional information
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no inhibition by acetoacetyl-CoA
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0.024
trans-2-decenoyl-CoA
0.024
trans-2-dodecenoyl-CoA
0.045
trans-2-hexenoyl-CoA
0.024
trans-2-octenoyl-CoA
0.024
trans-2-tetradecenoyl-CoA
0.024
trans-2-decenoyl-CoA
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0.024
trans-2-decenoyl-CoA
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25°C
0.024
trans-2-dodecenoyl-CoA
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0.024
trans-2-dodecenoyl-CoA
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25°C
0.045
trans-2-hexenoyl-CoA
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0.045
trans-2-hexenoyl-CoA
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25°C
0.024
trans-2-octenoyl-CoA
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0.024
trans-2-octenoyl-CoA
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25°C
0.024
trans-2-tetradecenoyl-CoA
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0.024
trans-2-tetradecenoyl-CoA
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25°C
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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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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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7 - 9
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pH 7: about 50% of maximal activity, pH 9: 80% of maximal activity
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brenda
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brenda
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brenda
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brenda
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brenda
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brenda
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brenda
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brenda
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inner membrane
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E3TGN9_ICTPU
291
0
31285
TrEMBL
Mitochondrion (Reliability: 4 )
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45000
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x * 81000 + x * 45000, SDS-PAGE
81000
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x * 81000 + x * 45000, SDS-PAGE
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x * 81000 + x * 45000, SDS-PAGE
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- 20°C, stable for several months
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-20°C, purified enzyme is stable for several months
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expression in Escherichia coli
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Fong, J.C.; Schulz, H.
Purification and properties of pig heart crotonase and the presence of short chain and long chain enoyl coenzyme A hydratases in pig and guinea pig tissues
J. Biol. Chem.
252
542-547
1977
Cavia porcellus, Sus scrofa
brenda
Fong, J.C.; Schulz, H.
Short-chain and long-chain enoyl-CoA hydratases from pig heart muscle
Methods Enzymol.
71
390-398
1981
Sus scrofa
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Luo, M.J.; He, X.Y.; Sprecher, H.; Schulz, H.
Purification and characterization of the trifunctional beta-oxidation complex from pig heart mitochondria
Arch. Biochem. Biophys.
304
266-271
1993
Sus scrofa
brenda
Wu, L.; Liu, X.; Li, D.
Oct-2-yn-4-enoyl-CoA as a multifunctional enzyme inhibitor in fatty acid oxidation
Org. Lett.
10
2235-2238
2008
Rattus norvegicus
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Schulz, H.
Long chain enoyl coenzyme A hydratase from pig heart
J. Biol. Chem.
249
2704-2709
1974
Sus scrofa
brenda
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