Plant Molecular Biology

, Volume 73, Issue 6, pp 587–603

Terpene synthases of oregano (Origanum vulgare L.) and their roles in the pathway and regulation of terpene biosynthesis

  • Christoph Crocoll
  • Julia Asbach
  • Johannes Novak
  • Jonathan Gershenzon
  • Jörg Degenhardt

DOI: 10.1007/s11103-010-9636-1

Cite this article as:
Crocoll, C., Asbach, J., Novak, J. et al. Plant Mol Biol (2010) 73: 587. doi:10.1007/s11103-010-9636-1


The aroma, flavor and pharmaceutical value of cultivated oregano (Origanum vulgare L.) is a consequence of its essential oil which consists mostly of monoterpenes and sesquiterpenes. To investigate the biosynthetic pathway to oregano terpenes and its regulation, we identified and characterized seven terpene synthases, key enzymes of terpene biosynthesis, from two cultivars of O. vulgare. Heterologous expression of these enzymes showed that each forms multiple mono- or sesquiterpene products and together they are responsible for the direct production of almost all terpenes found in O. vulgare essential oil. The correlation of essential oil composition with relative and absolute terpene synthase transcript concentrations in different lines of O. vulgare demonstrated that monoterpene synthase activity is predominantly regulated on the level of transcription and that the phenolic monoterpene alcohol thymol is derived from γ-terpinene, a product of a single monoterpene synthase. The combination of heterologously-expressed terpene synthases for in vitro assays resulted in blends of mono- and sesquiterpene products that strongly resemble those found in vivo, indicating that terpene synthase expression levels directly control the composition of the essential oil. These results will facilitate metabolic engineering and directed breeding of O. vulgare cultivars with higher quantity of essential oil and improved oil composition.


Origanum vulgare L. Terpene synthase γ-Terpinene Thymol Essential oil Transcript regulation 



Flame ionization detector


Farnesyl diphosphate


Gas chromatography


Geranyl diphosphate


Mass spectrometry


Terpene synthase


Quantitative realtime polymerase chain reaction

Supplementary material

11103_2010_9636_MOESM1_ESM.doc (2.2 mb)
Supplementary material 1 (DOC 2231 kb)

Copyright information

© Springer Science+Business Media B.V. 2010

Authors and Affiliations

  • Christoph Crocoll
    • 1
  • Julia Asbach
    • 1
  • Johannes Novak
    • 2
  • Jonathan Gershenzon
    • 1
  • Jörg Degenhardt
    • 3
  1. 1.Department of BiochemistryMax Planck Institute for Chemical EcologyJenaGermany
  2. 2.Institute for Applied Botany and PharmacognosyUniversity of Veterinary MedicineWienAustria
  3. 3.Institute of PharmacyMartin Luther University HalleHalleGermany

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