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- Name help_outline vinylacetyl-CoA Identifier CHEBI:57396 Charge -4 Formula C25H36N7O17P3S InChIKeyhelp_outline UATIGEHITDTAGF-CITAKDKDSA-J 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)CC=C 2D coordinates Mol file for the small molecule Search links Involved in 1 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline (2E)-butenoyl-CoA Identifier CHEBI:57332 Charge -4 Formula C25H36N7O17P3S InChIKeyhelp_outline KFWWCMJSYSSPSK-PAXLJYGASA-J SMILEShelp_outline C\C=C\C(=O)SCCNC(=O)CCNC(=O)[C@H](O)C(C)(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 2D coordinates Mol file for the small molecule Search links Involved in 20 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:10572 | RHEA:10573 | RHEA:10574 | RHEA:10575 | |
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| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Publications
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On the mechanism and some properties of vinylacetyl-CoA delta-isomerase of Clostridium kluyveri.
Schleicher E., Simon H.
Vinylacetyl-CoA delta-isomerase from Clostridium kluyveri grown on ethanol/acetate was purified 32-fold. The enzyme is rather labile. All experiments were conducted with the substrate analog thioester of vinylacetic acid and N-acetylchysteamine (vinylacetyl-SEtNAc (1 f)). 3-Butinoyl-SEtNAc is a st ... >> More
Vinylacetyl-CoA delta-isomerase from Clostridium kluyveri grown on ethanol/acetate was purified 32-fold. The enzyme is rather labile. All experiments were conducted with the substrate analog thioester of vinylacetic acid and N-acetylchysteamine (vinylacetyl-SEtNAc (1 f)). 3-Butinoyl-SEtNAc is a strong inhibitor of the isomerase. The hydrogen transfer from the alpha-position of vinylacetyl-SEtNAc to the gamma-position of 2-butenoyl-SEtNAc (1f leads to 2 f) occurs partially intramolecularly (40-50%) as shown by experiments in 3HOH/H2O, 2H2O and 3HOH/2H2O as well as by experiments with [2,3-3H]vinylacetyl-SEtNAc. Only 0.07 atoms of tritium are incorporated into the gamma-position of 2f when the isomerisation takes place in 3HOH/H2O. The extent of intramolecularity is in agreement with results of experiments conducted in 2H2O with whole cells [4]. The reaction 1f leads to 2f shows no or only negligiebl reversibility and at least no considerable isotope effect. << Less
Hoppe Seylers Z Physiol Chem 357:535-541(1976) [PubMed] [EuropePMC]
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Crystal structure of 4-hydroxybutyryl-CoA dehydratase: radical catalysis involving a [4Fe-4S] cluster and flavin.
Martins B.M., Dobbek H., Cinkaya I., Buckel W., Messerschmidt A.
Dehydratases catalyze the breakage of a carbon-oxygen bond leading to unsaturated products via the elimination of water. The 1.6-A resolution crystal structure of 4-hydroxybutyryl-CoA dehydratase from the gamma-aminobutyrate-fermenting Clostridium aminobutyricum represents a new class of dehydrata ... >> More
Dehydratases catalyze the breakage of a carbon-oxygen bond leading to unsaturated products via the elimination of water. The 1.6-A resolution crystal structure of 4-hydroxybutyryl-CoA dehydratase from the gamma-aminobutyrate-fermenting Clostridium aminobutyricum represents a new class of dehydratases with an unprecedented active site architecture. A [4Fe-4S](2+) cluster, coordinated by three cysteine and one histidine residues, is located 7 A from the Re-side of a flavin adenine dinucleotide (FAD) moiety. The structure provides insight into the function of these ubiquitous prosthetic groups in the chemically nonfacile, radical-mediated dehydration of 4-hydroxybutyryl-CoA. The substrate can be bound between the [4Fe-4S](2+) cluster and the FAD with both cofactors contributing to its radical activation and catalytic conversion. Our results raise interesting questions regarding the mechanism of acyl-CoA dehydrogenases, which are involved in fatty acid oxidation, and address the divergent evolution of the ancestral common gene. << Less
Proc. Natl. Acad. Sci. U.S.A. 101:15645-15649(2004) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.