Enzymes
| UniProtKB help_outline | 2 proteins |
Reaction participants Show >> << Hide
- Name help_outline IC-asc-C9-CoA Identifier CHEBI:166973 Charge -4 Formula C45H63N8O22P3S InChIKeyhelp_outline NQNMAMRMBCYUJB-XOGJWDHUSA-J SMILEShelp_outline C(CC(SCCNC(CCNC(=O)[C@@H](C(COP(OP(OC[C@H]1O[C@@H](N2C3=C(C(=NC=N3)N)N=C2)[C@@H]([C@@H]1OP([O-])([O-])=O)O)(=O)[O-])(=O)[O-])(C)C)O)=O)=O)CCCC[C@H](O[C@@H]4O[C@@H](C)[C@@H](C[C@H]4O)OC(C=5C=6C=CC=CC6NC5)=O)C 2D coordinates Mol file for the small molecule Search links Involved in 3 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline O2 Identifier CHEBI:15379 (CAS: 7782-44-7) help_outline Charge 0 Formula O2 InChIKeyhelp_outline MYMOFIZGZYHOMD-UHFFFAOYSA-N SMILEShelp_outline O=O 2D coordinates Mol file for the small molecule Search links Involved in 2,727 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline IC-asc-ΔC9-CoA Identifier CHEBI:166974 Charge -4 Formula C45H61N8O22P3S InChIKeyhelp_outline ULAHBGLKYQKMTI-VSHRVGAASA-J SMILEShelp_outline C(=C/C(SCCNC(CCNC(=O)[C@@H](C(COP(OP(OC[C@H]1O[C@@H](N2C3=C(C(=NC=N3)N)N=C2)[C@@H]([C@@H]1OP([O-])([O-])=O)O)(=O)[O-])(=O)[O-])(C)C)O)=O)=O)\CCCC[C@H](O[C@@H]4O[C@@H](C)[C@@H](C[C@H]4O)OC(C=5C=6C=CC=CC6NC5)=O)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 H2O2 Identifier CHEBI:16240 (CAS: 7722-84-1) help_outline Charge 0 Formula H2O2 InChIKeyhelp_outline MHAJPDPJQMAIIY-UHFFFAOYSA-N SMILEShelp_outline [H]OO[H] 2D coordinates Mol file for the small molecule Search links Involved in 452 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:66236 | RHEA:66237 | RHEA:66238 | RHEA:66239 | |
|---|---|---|---|---|
| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
| UniProtKB help_outline |
|
Related reactions help_outline
More general form(s) of this reaction
Publications
-
Biosynthetic tailoring of existing ascaroside pheromones alters their biological function in C. elegans.
Zhou Y., Wang Y., Zhang X., Bhar S., Jones Lipinski R.A., Han J., Feng L., Butcher R.A.
<i>Caenorhabditis elegans</i> produces ascaroside pheromones to control its development and behavior. Even minor structural differences in the ascarosides have dramatic consequences for their biological activities. Here, we identify a mechanism that enables <i>C. elegans</i> to dynamically tailor ... >> More
<i>Caenorhabditis elegans</i> produces ascaroside pheromones to control its development and behavior. Even minor structural differences in the ascarosides have dramatic consequences for their biological activities. Here, we identify a mechanism that enables <i>C. elegans</i> to dynamically tailor the fatty-acid side chains of the indole-3-carbonyl (IC)-modified ascarosides it has produced. In response to starvation, <i>C. elegans</i> uses the peroxisomal acyl-CoA synthetase ACS-7 to activate the side chains of medium-chain IC-ascarosides for β-oxidation involving the acyl-CoA oxidases ACOX-1.1 and ACOX-3. This pathway rapidly converts a favorable ascaroside pheromone that induces aggregation to an unfavorable one that induces the stress-resistant dauer larval stage. Thus, the pathway allows the worm to respond to changing environmental conditions and alter its chemical message without having to synthesize new ascarosides de novo. We establish a new model for biosynthesis of the IC-ascarosides in which side-chain β-oxidation is critical for controlling the type of IC-ascarosides produced. << Less
Elife 7:0-0(2018) [PubMed] [EuropePMC]
This publication is cited by 14 other entries.