4.8 Article

Biochemical Characterization of a Eukaryotic Decalin-Forming Diels-Alderase

Journal

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
Volume 138, Issue 49, Pages 15837-15840

Publisher

AMER CHEMICAL SOC
DOI: 10.1021/jacs.6b10452

Keywords

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Funding

  1. NIH [1DP1GM106413, 1R35GM118056]
  2. NSF [CHE-1361104]
  3. JSPS Program for Advancing Strategic International Networks To Accelerate the Circulation of Talented Researchers [G2604]
  4. Grants-in-Aid for Scientific Research [15KT0068, 16H06449] Funding Source: KAKEN
  5. Division Of Chemistry
  6. Direct For Mathematical & Physical Scien [1361104] Funding Source: National Science Foundation

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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.

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