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Exploring biosynthetic diversity with trichodiene synthase.

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Summary

Trichodiene synthase flexibly converts farnesyl diphosphate into trichodiene and other sesquiterpenes. Its active site accommodates diverse substrates, suggesting broad biosynthetic potential for this terpenoid cyclase.

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Area of Science:

Biochemistry
Enzymology
Structural Biology

Background:

Trichodiene synthase is a key enzyme in sesquiterpene biosynthesis.
It catalyzes the cyclization of farnesyl diphosphate (FPP).

Purpose of the Study:

To investigate the substrate flexibility of trichodiene synthase.
To elucidate the structural basis for this flexibility.

Main Methods:

Enzyme kinetics with modified FPP analogs.
X-ray crystallography of trichodiene synthase-inhibitor complex.

Main Results:

Trichodiene synthase produces trichodiene (89%) and sesquiterpene mixtures (11%) from FPP.
Enzyme accommodates derivatized FPP substrates with altered electronic or steric properties.
X-ray structure reveals a flexible active site accommodating a bulky intermediate mimic.

Conclusions:

Trichodiene synthase possesses a flexible active site.
This flexibility allows for accommodation of diverse substrates and intermediates.
Suggests potential for expanded biosynthetic applications of this terpenoid cyclase.