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- Name help_outline 3-[(3aS,4S,5R,7aS)-5-hydroxy-7a-methyl-1-oxo-octahydro-1H-inden-4-yl]propanoyl-CoA Identifier CHEBI:83738 Charge -4 Formula C34H50N7O19P3S InChIKeyhelp_outline AKNIQSRWPADUMX-ODLRQIBISA-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@H]1[C@@H]2CCC(=O)[C@@]2(C)CC[C@H]1O 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 A Identifier CHEBI:13193 Charge Formula R SMILEShelp_outline * 2D coordinates Mol file for the small molecule Search links Involved in 2,883 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline (2E)-3-[(3aS,4S,5R,7aS)-5-hydroxy-7a-methyl-1-oxo-octahydro-1H-inden-4-yl]prop-2-enoyl-CoA Identifier CHEBI:167059 Charge -4 Formula C34H48N7O19P3S InChIKeyhelp_outline MHYJAWUBQZNCMM-OQKZBKOQSA-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(\C=C\[C@]4([C@@]5(CCC([C@]5(CC[C@H]4O)C)=O)[H])[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 1 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline AH2 Identifier CHEBI:17499 Charge 0 Formula RH2 SMILEShelp_outline *([H])[H] 2D coordinates Mol file for the small molecule Search links Involved in 2,812 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:66348 | RHEA:66349 | RHEA:66350 | RHEA:66351 | |
|---|---|---|---|---|
| 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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IpdE1-IpdE2 is a heterotetrameric acyl coenzyme A dehydrogenase that is widely distributed in steroid-degrading bacteria.
Gadbery J.E., Round J.W., Yuan T., Wipperman M.F., Story K.T., Crowe A.M., Casabon I., Liu J., Yang X., Eltis L.D., Sampson N.S.
Steroid-degrading bacteria, including <i>Mycobacterium tuberculosis</i> (<i>Mtb</i>), utilize an architecturally distinct subfamily of acyl coenzyme A dehydrogenases (ACADs) for steroid catabolism. These ACADs are α<sub>2</sub>β<sub>2</sub> heterotetramers that are usually encoded by adjacent <i>f ... >> More
Steroid-degrading bacteria, including <i>Mycobacterium tuberculosis</i> (<i>Mtb</i>), utilize an architecturally distinct subfamily of acyl coenzyme A dehydrogenases (ACADs) for steroid catabolism. These ACADs are α<sub>2</sub>β<sub>2</sub> heterotetramers that are usually encoded by adjacent <i>fadE-</i>like genes. In mycobacteria, <i>ipdE1</i> and <i>ipdE2</i> (formerly <i>fadE30</i> and <i>fadE33</i>) occur in divergently transcribed operons associated with the catabolism of 3aα-<i>H</i>-4α(3'-propanoate)-7aβ-methylhexahydro-1,5-indanedione (HIP), a steroid metabolite. In <i>Mycobacterium smegmatis</i>, Δ<i>ipdE1</i> and Δ<i>ipdE2</i> mutants had similar phenotypes, showing impaired growth on cholesterol and accumulating 5-OH HIP in the culture supernatant. Bioinformatic analyses revealed that IpdE1 and IpdE2 share many of the features of the α- and β-subunits, respectively, of heterotetrameric ACADs that are encoded by adjacent genes in many steroid-degrading proteobacteria. When coproduced in a rhodococcal strain, IpdE1 and IpdE2 of <i>Mtb</i> formed a complex that catalyzed the dehydrogenation of 5OH-HIP coenzyme A (5OH-HIP-CoA) to 5OH-3aα-<i>H</i>-4α(3'-prop-1-enoate)-7aβ-methylhexa-hydro-1,5-indanedione coenzyme A ((<i>E</i>)<i>-</i>5OH-HIPE-CoA). This corresponds to the initial step in the pathway that leads to degradation of steroid C and D rings via β-oxidation. Small-angle X-ray scattering revealed that the IpdE1-IpdE2 complex was an α<sub>2</sub>β<sub>2</sub> heterotetramer typical of other ACADs involved in steroid catabolism. These results provide insight into an important class of steroid catabolic enzymes and a potential virulence determinant in <i>Mtb</i>. << Less