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Review
. 2015 Jul;33(7):419-28.
doi: 10.1016/j.tibtech.2015.04.006. Epub 2015 May 20.

Plant diterpene synthases: exploring modularity and metabolic diversity for bioengineering

Philipp Zerbe  1 , Jörg Bohlmann  2
Affiliations
Review

Plant diterpene synthases: exploring modularity and metabolic diversity for bioengineering

Philipp Zerbe et al. Trends Biotechnol. 2015 Jul.

Abstract

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.

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

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