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Bacterial diterpene synthases prenylate small molecules.

Baofu Xu1, Zining Li1, Tyler A Alsup1

  • 1Department of Chemistry, University of Florida, Gainesville, FL, USA.

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Summary

Bacterial diterpene synthases can perform both cyclization and prenylation reactions, expanding their known catalytic capabilities. This dual function in terpene biosynthesis has significant implications for natural product discovery.

Keywords:
natural productprenylationprenyltransferasesubstrate decoyterpene synthase

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Area of Science:

  • Biochemistry
  • Natural Products Chemistry
  • Enzymology

Background:

  • Terpenoid biosynthesis initiates with carbocation cyclization or prenylation.
  • Terpene synthases (cyclization) and prenyltransferases (prenylation) are distinct enzyme families.
  • Bacterial diterpene synthases were traditionally viewed as cyclization-specific.

Purpose of the Study:

  • To investigate the dual reactivity of bacterial diterpene synthases.
  • To explore their ability to catalyze both cyclization and prenylation.
  • To understand the mechanistic basis and evolutionary implications of this dual function.

Main Methods:

  • Kinetic studies
  • Biocatalytic assays
  • Structural analysis
  • Bioinformatics

Main Results:

  • Diterpene synthases efficiently catalyze both diterpene cyclization and prenylation of small molecules.
  • Demonstrated C-, N-, O-, and S-prenylation capabilities.
  • Proposed a substrate decoy mechanism for prenylation.
  • Supported in vivo physiological relevance of terpene synthase-catalyzed prenylation.

Conclusions:

  • Terpene synthases possess broader catalytic versatility than previously recognized.
  • This dual activity expands the known pathways for natural product biosynthesis.
  • Provides insights into enzyme evolution and the discovery of novel prenylated compounds.