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- Name help_outline lithocholoyl-CoA Identifier CHEBI:87438 Charge -4 Formula C45H70N7O18P3S InChIKeyhelp_outline MHVCMYOMCROIEL-FYYKUXHTSA-J 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)CC[C@@](C)([C@]4(CC[C@@]5([C@@]4(CC[C@@]6([C@]7(CC[C@H](C[C@]7(CC[C@@]56[H])[H])O)C)[H])C)[H])[H])[H])=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 7 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline chenodeoxycholate Identifier CHEBI:36234 (Beilstein: 3703074) help_outline Charge -1 Formula C24H39O4 InChIKeyhelp_outline RUDATBOHQWOJDD-BSWAIDMHSA-M SMILEShelp_outline [H][C@@]12C[C@H](O)CC[C@]1(C)[C@@]1([H])CC[C@]3(C)[C@]([H])(CC[C@@]3([H])[C@]1([H])[C@H](O)C2)[C@H](C)CCC([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 18 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline chenodeoxycholoyl-CoA Identifier CHEBI:62989 Charge -4 Formula C45H70N7O19P3S InChIKeyhelp_outline IIWDDMINEZBCTG-RUAADODMSA-J SMILEShelp_outline [H][C@@](C)(CCC(=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)[C@@]1([H])CC[C@@]2([H])[C@]3([H])[C@H](O)C[C@]4([H])C[C@H](O)CC[C@]4(C)[C@@]3([H])CC[C@]12C 2D coordinates Mol file for the small molecule Search links Involved in 6 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline lithocholate Identifier CHEBI:29744 Charge -1 Formula C24H39O3 InChIKeyhelp_outline SMEROWZSTRWXGI-HVATVPOCSA-M SMILEShelp_outline [H][C@]12CC[C@]3([H])[C@]([H])(CC[C@]4(C)[C@]([H])(CC[C@@]34[H])[C@H](C)CCC([O-])=O)[C@@]1(C)CC[C@@H](O)C2 2D coordinates Mol file for the small molecule Search links Involved in 16 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:53772 | RHEA:53773 | RHEA:53774 | RHEA:53775 | |
|---|---|---|---|---|
| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
| UniProtKB help_outline |
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Publications
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Identification and characterization of two bile acid coenzyme A transferases from Clostridium scindens, a bile acid 7alpha-dehydroxylating intestinal bacterium.
Ridlon J.M., Hylemon P.B.
The human bile acid pool composition is composed of both primary bile acids (cholic acid and chenodeoxycholic acid) and secondary bile acids (deoxycholic acid and lithocholic acid). Secondary bile acids are formed by the 7α-dehydroxylation of primary bile acids carried out by intestinal anaerobic ... >> More
The human bile acid pool composition is composed of both primary bile acids (cholic acid and chenodeoxycholic acid) and secondary bile acids (deoxycholic acid and lithocholic acid). Secondary bile acids are formed by the 7α-dehydroxylation of primary bile acids carried out by intestinal anaerobic bacteria. We have previously described a multistep biochemical pathway in Clostridium scindens that is responsible for bile acid 7α-dehydroxylation. We have identified a large (12 kb) bile acid inducible (bai) operon in this bacterium that encodes eight genes involved in bile acid 7α-dehydroxylation. However, the function of the baiF gene product in this operon has not been elucidated. In the current study, we cloned and expressed the baiF gene in E. coli and discovered it has bile acid CoA transferase activity. In addition, we discovered a second bai operon encoding three genes. The baiK gene in this operon was expressed in E. coli and found to encode a second bile acid CoA transferase. Both bile acid CoA transferases were determined to be members of the type III family by amino acid sequence comparisons. Both bile acid CoA transferases had broad substrate specificity, except the baiK gene product, which failed to use lithocholyl-CoA as a CoA donor. Primary bile acids are ligated to CoA via an ATP-dependent mechanism during the initial steps of 7α-dehydroxylation. The bile acid CoA transferases conserve the thioester bond energy, saving the cell ATP molecules during bile acid 7α-dehydroxylation. ATP-dependent CoA ligation is likely quickly supplanted by ATP-independent CoA transfer. << Less
J. Lipid Res. 53:66-76(2012) [PubMed] [EuropePMC]
This publication is cited by 12 other entries.