An analysis of characterized plant sesquiterpene synthases. (February 2019)

• Record Type: Journal Article
• Authors: Durairaj, Janani; Di Girolamo, Alice; Bouwmeester, Harro J.; de Ridder, Dick; Beekwilder, Jules; van Dijk, Aalt DJ.
• Is Part Of: Phytochemistry. Volume 158(2019)
• Page Start: 157
• Page End: 165
• Publication Date: 2019-02
• Subjects: Database -- Product specificity -- Enzyme -- Sesquiterpene -- Sesquiterpene synthase -- Terpene synthase; Botanical chemistry -- Periodicals; Biochemistry -- Periodicals; Botany -- Periodicals; Chimie végétale -- Périodiques; 572.2
• DOI: 10.1016/j.phytochem.2018.10.020
• Languages: English
• ISSNs: 0031-9422

Abstract

Abstract: Plants exhibit a vast array of sesquiterpenes, C15 hydrocarbons which often function as herbivore-repellents or pollinator-attractants. These in turn are produced by a diverse range of sesquiterpene synthases. A comprehensive analysis of these enzymes in terms of product specificity has been hampered by the lack of a centralized resource of sufficient functionally annotated sequence data. To address this, we have gathered 262 plant sesquiterpene synthase sequences with experimentally characterized products. The annotated enzyme sequences allowed for an analysis of terpene synthase motifs, leading to the extension of one motif and recognition of a variant of another. In addition, putative terpene synthase sequences were obtained from various resources and compared with the annotated sesquiterpene synthases. This analysis indicated regions of terpene synthase sequence space which so far are unexplored experimentally. Finally, we present a case describing mutational studies on residues altering product specificity, for which we analyzed conservation in our database. This demonstrates an application of our database in choosing likely-functional residues for mutagenesis studies aimed at understanding or changing sesquiterpene synthase product specificity. Graphical abstract: Highlights: Over 250 plant sesquiterpene synthases with experimentally characterized products have been gathered from literature. Sequence similarity of sesquiterpene synthases reflects phylogeny more than product specificity. Hundreds of sesquiterpenes derive from a small number of precursor carbocations. Uncharacterized sequences are compared to characterized synthases in terms of product precursor. Terpene synthase motifs are not as well-conserved or as strict as previously thought. The dataset of synthases with known function allows for finding residue positions likely to be involved in product specificity.