Enzymes
| UniProtKB help_outline | 4 proteins |
| Enzyme class help_outline |
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| GO Molecular Function help_outline |
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- Name help_outline acetoacetate Identifier CHEBI:13705 (Beilstein: 4128534; CAS: 141-81-1) help_outline Charge -1 Formula C4H5O3 InChIKeyhelp_outline WDJHALXBUFZDSR-UHFFFAOYSA-M SMILEShelp_outline CC(=O)CC([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 21 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline butanoyl-CoA Identifier CHEBI:57371 Charge -4 Formula C25H38N7O17P3S InChIKeyhelp_outline CRFNGMNYKDXRTN-CITAKDKDSA-J SMILEShelp_outline CCCC(=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 36 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline acetoacetyl-CoA Identifier CHEBI:57286 Charge -4 Formula C25H36N7O18P3S InChIKeyhelp_outline OJFDKHTZOUZBOS-CITAKDKDSA-J SMILEShelp_outline CC(=O)CC(=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 15 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline butanoate Identifier CHEBI:17968 (Beilstein: 3601060; CAS: 461-55-2) help_outline Charge -1 Formula C4H7O2 InChIKeyhelp_outline FERIUCNNQQJTOY-UHFFFAOYSA-M SMILEShelp_outline CCCC([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 22 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:12961 | RHEA:12962 | RHEA:12963 | RHEA:12964 | |
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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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Butyryl-CoA:acetoacetate CoA-transferase from a lysine-fermenting Clostridium.
Barker H.A., Jeng I.M., Neff N., Robertson J.M., Tam F.K., Hosaka S.
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Cloning and expression of Clostridium acetobutylicum ATCC 824 acetoacetyl-coenzyme A:acetate/butyrate:coenzyme A-transferase in Escherichia coli.
Cary J.W., Petersen D.J., Papoutsakis E.T., Bennett G.N.
Coenzyme A (CoA)-transferase (acetoacetyl-CoA:acetate/butyrate:CoA-transferase [butyrate-acetoacetate CoA-transferase] [EC 2.8.3.9]) of Clostridium acetobutylicum ATCC 824 is an important enzyme in the metabolic shift between the acid-producing and solvent-forming states of this organism. The puri ... >> More
Coenzyme A (CoA)-transferase (acetoacetyl-CoA:acetate/butyrate:CoA-transferase [butyrate-acetoacetate CoA-transferase] [EC 2.8.3.9]) of Clostridium acetobutylicum ATCC 824 is an important enzyme in the metabolic shift between the acid-producing and solvent-forming states of this organism. The purification and properties of the enzyme have recently been described (D. P. Weisenborn, F. B. Rudolph, and E. T. Papoutsakis, Appl. Environ. Microbiol. 55:323-329, 1989). The genes encoding the two subunits of this enzyme have been cloned by using synthetic oligodeoxynucleotide probes designed from amino-terminal sequencing data from each subunit of the CoA-transferase. A bacteriophage lambda EMBL3 library of C. acetobutylicum DNA was prepared and screened by using these probes. Subsequent subcloning experiments established the position of the structural genes for CoA-transferase. Complementation of Escherichia coli ato mutants with the recombinant plasmid pCoAT4 (pUC19 carrying a 1.8-kilobase insert of C. acetobutylicum DNA encoding CoA-transferase activity) enabled the transformants to grow on butyrate as a sole carbon source. Despite the ability of CoA-transferase to complement the ato defect in E. coli mutants, Southern blot and Western blot (immunoblot) analyses showed that neither the C. acetobutylicum genes encoding CoA-transferase nor the enzyme itself shared any apparent homology with its E. coli counterpart. Polypeptides of Mr of the purified CoA-transferase subunits were observed by Western blot and maxicell analysis of whole-cell extracts of E. coli harboring pCoAT4. The proximity and orientation of the genes suggest that the genes encoding the two subunits of CoA-transferase may form an operon similar to that found in E. coli.(ABSTRACT TRUNCATED AT 250 WORDS) << Less
Appl. Environ. Microbiol. 56:1576-1583(1990) [PubMed] [EuropePMC]