Reaction participants Show >> << Hide
- Name help_outline (5Z)-5-(2-methylpropylidene)-3-[(2E,6R,8E,10E,12E)-6,8,10,12-tetramethyltetradeca-2,8,10,12-tetraenoyl]-2,5-dihydro-1H-pyrrol-2-one Identifier CHEBI:169932 Charge 0 Formula C26H37NO2 InChIKeyhelp_outline OGOOQDHSWFFUNL-PIUTVPOOSA-N SMILEShelp_outline C=1(C(N\C(\C1)=C/C(C)C)=O)C(/C=C/CC[C@H](C/C(=C/C(=C/C(=C/C)/C)/C)/C)C)=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 myceliothermophin E Identifier CHEBI:167709 Charge 0 Formula C26H37NO2 InChIKeyhelp_outline TXVWNUBEANXHMB-FXVWVMPXSA-N SMILEShelp_outline [C@]12(CC[C@@H](C)C[C@]1(C=C([C@H]([C@H]2C(=O)C3=C\C(\NC3=O)=C\C(C)C)/C(=C/C)/C)C)C)[H] 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
Cross-references
| RHEA:67312 | RHEA:67313 | RHEA:67314 | RHEA:67315 | |
|---|---|---|---|---|
| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
| UniProtKB help_outline |
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Publications
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Biochemical characterization of a eukaryotic decalin-forming Diels-Alderase.
Li L., Yu P., Tang M.C., Zou Y., Gao S.S., Hung Y.S., Zhao M., Watanabe K., Houk K.N., Tang Y.
The trans-decalin structure formed by intramolecular Diels-Alder cycloaddition is widely present among bioactive natural products isolated from fungi. We elucidated the concise three-enzyme biosynthetic pathway of the cytotoxic myceliothermophin and biochemically characterized the Diels-Alderase t ... >> More
The trans-decalin structure formed by intramolecular Diels-Alder cycloaddition is widely present among bioactive natural products isolated from fungi. We elucidated the concise three-enzyme biosynthetic pathway of the cytotoxic myceliothermophin and biochemically characterized the Diels-Alderase that catalyzes the formation of trans-decalin from an acyclic substrate. Computational studies of the reaction mechanism rationalize both the substrate and stereoselectivity of the enzyme. << Less
J. Am. Chem. Soc. 138:15837-15840(2016) [PubMed] [EuropePMC]
This publication is cited by 6 other entries.