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Related Experiment Videos

Trichodiene synthase. Substrate specificity and inhibition

D E Cane1, G Yang, Q Xue

  • 1Department of Chemistry, Brown University, Providence, Rhode Island 02912.

Biochemistry
|February 28, 1995
PubMed
Summary
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Trichodiene synthase exhibits specific substrate preferences, with 10-fluorofarnesyl diphosphate (15) acting as a potent competitive inhibitor. This research clarifies enzyme kinetics and potential inhibitor development for sesquiterpene biosynthesis.

Area of Science:

  • Biochemistry
  • Enzymology
  • Organic Chemistry

Background:

  • Sesquiterpene synthases are crucial enzymes in plant secondary metabolism.
  • Trichodiene synthase catalyzes the formation of sesquiterpenes, a diverse class of natural products.
  • Understanding substrate specificity is key to enzyme mechanism elucidation and inhibitor design.

Purpose of the Study:

  • To investigate the substrate specificity of trichodiene synthase.
  • To characterize kinetic parameters (Vmax, Km) for natural and analog substrates.
  • To identify potent inhibitors of trichodiene synthase activity.

Main Methods:

  • Enzyme kinetics assays using native fungal and recombinant trichodiene synthase.
  • Determination of Vmax and Km for trans,trans-farnesyl diphosphate, cis,trans-farnesyl diphosphate, and (3R)-nerolidyl diphosphate.

Related Experiment Videos

  • Evaluation of farnesyl diphosphate analogs as competitive inhibitors.

    • Main Results:

    • Trichodiene synthase displayed distinct kinetic parameters for different farnesyl diphosphate isomers.
    • 10-Fluorofarnesyl diphosphate (15) emerged as the most effective competitive inhibitor (K1 = 16 nM).
    • An ether analog (8), potent against squalene synthase, showed only moderate inhibition (K1/Km = 70).

    Conclusions:

    • Trichodiene synthase exhibits defined substrate recognition and catalytic mechanisms.
    • 10-Fluorofarnesyl diphosphate is a valuable tool for studying trichodiene synthase inhibition.
    • Enzyme specificity suggests potential for targeted inhibitor development in sesquiterpene pathways.