Plant specialized metabolism: Diversity of terpene synthases and their products

Curr Opin Plant Biol. 2024 Oct:81:102607. doi: 10.1016/j.pbi.2024.102607. Epub 2024 Jul 24.

Abstract

Terpenoids are ubiquitous to all kingdoms of life and are one of the most diverse groups of compounds, both structurally and functionally. Despite being derived from common precursors, isopentenyl diphosphate and dimethylallyl diphosphate, their exceptional diversity is partly driven by the substrate and product promiscuity of terpene synthases that produce a wide array of terpene skeletons. Plant terpene synthases can be subdivided into different subfamilies based on sequence homology and function. However, in many cases, structural architecture of the enzyme is more essential to product specificity than primary sequence alone, and distantly related terpene synthases can often mediate similar reactions. As such, the focus of this brief review is on some of the recent progress in understanding terpene synthase function and diversity.

Keywords: Functional diversity; Promiscuous enzymes; Secondary metabolism; Terpene synthase; Terpenoids.

Publication types

  • Review

MeSH terms

  • Alkyl and Aryl Transferases* / genetics
  • Alkyl and Aryl Transferases* / metabolism
  • Plant Proteins / genetics
  • Plant Proteins / metabolism
  • Plants* / enzymology
  • Plants* / metabolism
  • Terpenes* / metabolism

Substances

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