An analysis of characterized plant sesquiterpene synthases

Phytochemistry. 2019 Feb:158:157-165. doi: 10.1016/j.phytochem.2018.10.020. Epub 2018 Nov 13.

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.

Keywords: Database; Enzyme; Product specificity; Sesquiterpene; Sesquiterpene synthase; Terpene synthase.

MeSH terms

  • Alkyl and Aryl Transferases / chemistry*
  • Alkyl and Aryl Transferases / genetics
  • Alkyl and Aryl Transferases / metabolism*
  • Amino Acid Motifs
  • Amino Acid Sequence
  • Conserved Sequence
  • Databases, Protein
  • Phylogeny
  • Plant Proteins / genetics
  • Plant Proteins / metabolism*
  • Sesquiterpenes / chemistry
  • Sesquiterpenes / metabolism*
  • Substrate Specificity

Substances

  • Plant Proteins
  • Sesquiterpenes
  • Alkyl and Aryl Transferases
  • terpene synthase