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Multienzyme Cascade Catalyzed Skeleton Rearrangement in a Caged Polyketide Biosynthesis.

Jia-Liang Zhou1, Qiu-Yue Nie1, Xian-Feng Hou1

  • 1State Key Laboratory of Chemical Biology, Shanghai Institute of Organic Chemistry, University of Chinese Academy of Sciences (CAS), CAS, Shanghai 200032, China.

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Summary
This summary is machine-generated.

Skeletal rearrangement is key for type II polyketide diversity. This study reveals how five oxidoreductases transform a planar intermediate into complex caged lactones, uncovering a multifunctional short-chain dehydrogenase.

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Area of Science:

  • Natural Product Biosynthesis
  • Enzymology
  • Organic Chemistry

Background:

  • Type II polyketides exhibit significant structural complexity and diversity.
  • Skeletal rearrangements are critical for generating this structural diversity.

Purpose of the Study:

  • To investigate the enzymatic rearrangement of a planar tetracyclic intermediate to caged lactones in type II polyketide biosynthesis.
  • To elucidate the mechanism of this skeletal rearrangement and identify key enzymes involved.

Main Methods:

  • Chemical synthesis of the proposed linear tetracyclic substrate.
  • In vivo and in vitro experiments to validate the transformation process.
  • Isotope labeling studies to elucidate the enzyme-catalyzed mechanism.

Main Results:

  • Demonstrated the transformation of a planar tetracyclic intermediate to caged lactones.
  • Identified a cascade of five oxidoreductases responsible for the skeletal rearrangement.
  • Discovered that the short-chain dehydrogenase TjhD5 possesses multifunctional activity, catalyzing multiple steps in the reaction sequence.

Conclusions:

  • The skeletal rearrangement of type II polyketides involves a complex enzymatic cascade.
  • TjhD5 is a key enzyme with a multifunctional role in this process, highlighting enzyme adaptability in natural product biosynthesis.