Terpene Synthase Structure-Function

Project Goals:..............Integrative approaches to tease out the determinants of product specificity in terpene synthases
Funding:......................Department of Energy - Energy Biosciences Program
Collaborators:.............Simone Raugei, Hoshin Kim - Pacific Northwest National Laboratory
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Executive Summary

Terpene synthases convert a prenyl diphosphate of a specific chain length to the first pathway-specific (often cyclic) intermediate in the biosynthesis of each class of terpenoids.  While some terpene synthases are remarkably specific and generate only one product, others release a larger number of products from a common substrate, thus contributing to terpenoid chemical diversity. We are using data from sequence comparisons, crystal structures, and molecular dynamics simulations to develop an understanding of how specificity arises in terpene synthases. Based on these insights we are developing models with a longer term goal to be able to predict the function of terpene synthases.

Selected Recent Publications

Srividya N., Lange I., Richter J.K., Wüst M., Lange B.M. (2022). Selectivity of enzymes involved in the formation of opposite enantiomeric series of p-menthane monoterpenoids in peppermint and Japanese catnip. Plant Sci. 314 , 111119.

Srividya N., Lange I., Lange B.M. (2020) Determinants of enantiospecificity in limonene synthases. Biochemistry 59, 1661-1664.

Lange B.M., Srividya N. (2019) Enzymology of monoterpene functionalization in glandular trichomes. J. Exp. Bot., 70, 1095-1108.

Srividya N., Lange I., Lange B.M. (2016) Generation and functional evaluation of designer monoterpene synthases. Methods Enzymol. 576, 147-165. Link

Srividya N., Davis E.M., Croteau R.B., Lange B.M. (2015) Functional analysis of (4S)-limonene synthase mutants reveals determinants of catalytic outcome in a model monoterpene synthase. Proc. Natl. Acad. Sci. USA 112, 3332-3337.