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Plant diterpene synthases: exploring modularity and metabolic diversity for bioengineering

Journal

TRENDS IN BIOTECHNOLOGY
Volume 33, Issue 7, Pages 419-428

Publisher

ELSEVIER SCIENCE LONDON
DOI: 10.1016/j.tibtech.2015.04.006

Keywords

diterpene synthase; plant chemical diversity; synthetic biology; metabolic engineering; natural product biosynthesis

Funding

  1. University of British Columbia
  2. Natural Sciences and Engineering Research Council of Canada
  3. Genome Canada
  4. Genome British Columbia
  5. University of California at Davis

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Plants produce thousands of diterpenoid natural products; some of which are of significant industrial value as biobased pharmaceuticals (taxol), fragrances (sclareol), food additives (steviosides), and commodity chemicals (diterpene, resin acids). In nature, diterpene synthase (diTPS) enzymes are essential for generating diverse diterpene hydrocarbon scaffolds. While some diTPSs also form oxygenated compounds, more commonly, oxygenation is achieved by cytochrome P450-dependent mono-oxygenases. Recent genome-, transcriptome-, and metabolome-guided gene discovery and enzyme characterization identified novel diTPS functions that form the core of complex modular pathway systems. Insights into diterpene metabolism may translate into the development of new bioengineered microbial and plant-based production systems.

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