Enzymes
| UniProtKB help_outline | 1 proteins |
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- Name help_outline 7α-hydroxy-3-oxochol-4-en-24-oyl-CoA Identifier CHEBI:140636 Charge -4 Formula C45H66N7O19P3S InChIKeyhelp_outline WTSQHJYZDLRRNB-WZRVWTAJSA-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(CCC(C=C7C[C@H]([C@@]56[H])O)=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 2 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline 3-oxochol-4,6-dien-24-oyl-CoA Identifier CHEBI:140634 Charge -4 Formula C45H64N7O18P3S InChIKeyhelp_outline IQGCDPWHEHJEGO-ABDXREKHSA-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(CCC(C=C7C=C[C@@]56[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 2 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H2O Identifier CHEBI:15377 (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 6,337 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:65348 | RHEA:65349 | RHEA:65350 | RHEA:65351 | |
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| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
| UniProtKB help_outline |
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| MetaCyc help_outline |
Publications
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Structure and functional characterization of a bile acid 7alpha dehydratase BaiE in secondary bile acid synthesis.
Bhowmik S., Chiu H.P., Jones D.H., Chiu H.J., Miller M.D., Xu Q., Farr C.L., Ridlon J.M., Wells J.E., Elsliger M.A., Wilson I.A., Hylemon P.B., Lesley S.A.
Conversion of the primary bile acids cholic acid (CA) and chenodeoxycholic acid (CDCA) to the secondary bile acids deoxycholic acid (DCA) and lithocholic acid (LCA) is performed by a few species of intestinal bacteria in the genus Clostridium through a multistep biochemical pathway that removes a ... >> More
Conversion of the primary bile acids cholic acid (CA) and chenodeoxycholic acid (CDCA) to the secondary bile acids deoxycholic acid (DCA) and lithocholic acid (LCA) is performed by a few species of intestinal bacteria in the genus Clostridium through a multistep biochemical pathway that removes a 7α-hydroxyl group. The rate-determining enzyme in this pathway is bile acid 7α-dehydratase (baiE). In this study, crystal structures of apo-BaiE and its putative product-bound [3-oxo-Δ(4,6) -lithocholyl-Coenzyme A (CoA)] complex are reported. BaiE is a trimer with a twisted α + β barrel fold with similarity to the Nuclear Transport Factor 2 (NTF2) superfamily. Tyr30, Asp35, and His83 form a catalytic triad that is conserved across this family. Site-directed mutagenesis of BaiE from Clostridium scindens VPI 12708 confirm that these residues are essential for catalysis and also the importance of other conserved residues, Tyr54 and Arg146, which are involved in substrate binding and affect catalytic turnover. Steady-state kinetic studies reveal that the BaiE homologs are able to turn over 3-oxo-Δ(4) -bile acid and CoA-conjugated 3-oxo-Δ(4) -bile acid substrates with comparable efficiency questioning the role of CoA-conjugation in the bile acid metabolism pathway. << Less
Proteins 84:316-331(2016) [PubMed] [EuropePMC]
This publication is cited by 2 other entries.