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- Name help_outline a medium-chain (3S)-3-hydroxyacyl-CoA Identifier CHEBI:191200 Charge -4 Formula C24H35N7O18P3SR SMILEShelp_outline [C@@H]1(N2C3=C(C(=NC=N3)N)N=C2)O[C@H](COP(OP(OCC(C)([C@H](C(NCCC(NCCSC(=O)C[C@H](*)O)=O)=O)O)C)(=O)[O-])(=O)[O-])[C@H]([C@H]1O)OP([O-])([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 4 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline a medium-chain (2E)-enoyl-CoA Identifier CHEBI:83726 Charge -4 Formula C24H33N7O17P3SR SMILEShelp_outline CC(C)(COP([O-])(=O)OP([O-])(=O)OC[C@H]1O[C@H]([C@H](O)[C@@H]1OP([O-])([O-])=O)n1cnc2c(N)ncnc12)[C@@H](O)C(=O)NCCC(=O)NCCSC(=O)\C=C\[*] 2D coordinates Mol file for the small molecule Search links Involved in 13 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H2O Identifier CHEBI:15377 (Beilstein: 3587155; CAS: 7732-18-5) help_outline Charge 0 Formula H2O InChIKeyhelp_outline XLYOFNOQVPJJNP-UHFFFAOYSA-N SMILEShelp_outline [H]O[H] 2D coordinates Mol file for the small molecule Search links Involved in 6,204 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:71647 | RHEA:71648 | RHEA:71649 | RHEA:71650 | |
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| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Related reactions help_outline
Specific form(s) of this reaction
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Publications
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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.
Fong J.C., Schulz H.
A short chain enoyl-CoA hydratase (crotonase) from pig heart has been purified to apparent homogeneity. The enzyme has an estimated native molecular weight of 155,000 and appears to be composed of six subunits of molecular weight 27,300. A study of the kinetic properties of the enzyme revealed tha ... >> More
A short chain enoyl-CoA hydratase (crotonase) from pig heart has been purified to apparent homogeneity. The enzyme has an estimated native molecular weight of 155,000 and appears to be composed of six subunits of molecular weight 27,300. A study of the kinetic properties of the enzyme revealed that the maximal velocity decreases nearly linearly with increasing chain length of the substrates from 1,670 units/mg with crotonyl-CoA to 40 units/mg with hexadecenoyl-CoA. However, the same Km values of 30 muM were obtained for all substrates except for crotonyl-CoA for which a value of 13 muM was determined. Since the presence of both crotonase and long chain enoyl-CoA hydratase in pig heart has been reported earlier, the presence of the same two enoyl-CoA hydratases in various tissues of several animals was investigated by sequential extraction and chromatography on hydroxylapatite of tissue homogenates. The simultaneous occurrence of both types of enoyl-CoA hydratase in tissues of pig and guinea pig has thus been established. It is proposed that the complementary actions of the two enoyl-CoA hydratases assures a high rate of hydration of enoyl-CoA intermediates of all chain lengths in fatty acid oxidation. << Less
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Long chain enoyl coenzyme A hydratase from pig heart.
Schulz H.
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The multifunctional protein in peroxisomal beta-oxidation: structure and substrate specificity of the Arabidopsis thaliana protein MFP2.
Arent S., Christensen C.E., Pye V.E., Noergaard A., Henriksen A.
Plant fatty acids can be completely degraded within the peroxisomes. Fatty acid degradation plays a role in several plant processes including plant hormone synthesis and seed germination. Two multifunctional peroxisomal isozymes, MFP2 and AIM1, both with 2-trans-enoyl-CoA hydratase and l-3-hydroxy ... >> More
Plant fatty acids can be completely degraded within the peroxisomes. Fatty acid degradation plays a role in several plant processes including plant hormone synthesis and seed germination. Two multifunctional peroxisomal isozymes, MFP2 and AIM1, both with 2-trans-enoyl-CoA hydratase and l-3-hydroxyacyl-CoA dehydrogenase activities, function in mouse ear cress (Arabidopsis thaliana) peroxisomal beta-oxidation, where fatty acids are degraded by the sequential removal of two carbon units. A deficiency in either of the two isozymes gives rise to a different phenotype; the biochemical and molecular background for these differences is not known. Structure determination of Arabidopsis MFP2 revealed that plant peroxisomal MFPs can be grouped into two families, as defined by a specific pattern of amino acid residues in the flexible loop of the acyl-binding pocket of the 2-trans-enoyl-CoA hydratase domain. This could explain the differences in substrate preferences and specific biological functions of the two isozymes. The in vitro substrate preference profiles illustrate that the Arabidopsis AIM1 hydratase has a preference for short chain acyl-CoAs compared with the Arabidopsis MFP2 hydratase. Remarkably, neither of the two was able to catabolize enoyl-CoA substrates longer than 14 carbon atoms efficiently, suggesting the existence of an uncharacterized long chain enoyl-CoA hydratase in Arabidopsis peroxisomes. << Less
J. Biol. Chem. 285:24066-24077(2010) [PubMed] [EuropePMC]
This publication is cited by 10 other entries.