Strategies for the Manipulation of Carbocations by Aristolochene Synthase

  • David J. Miller
  • Rudolf K. Allemann


Aristolochene synthase is a sesquiterpene cyclase that catalyses the high-precision conversion of farnesyl diphosphate to the sesquiterpene (+)-aristolochene via a tightly chaperoned carbocationic reaction cascade. This article examines recent work focussed on understanding the role this and other related enzymes play in controlling this chemistry. Through the use of X-ray crystallography, site-directed mutagenesis and substrate analogues, a better picture of how such proteins manipulate carbocations to arrive at specific hydrocarbon products is emerging.


Terpenes Aristolochene synthase Farnesyl diphosphate Inhibition Carbocation Template 



The authors would like to acknowledge the many contributions made by the members of the Allemann group. This work was supported by the UK’s Biotechnology and Biological Sciences Research Council through research grants 6/B17177, BBS/Q/Q/2004/05499 and BB/G003572/1, the Engineering and Physical Sciences Research Council through grant EP/D06958/1, the Royal Society (grant 2007R2) and Cardiff University. We are grateful to Neil Young for preparing Figs. 12.4 and 12.6.


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Copyright information

© Springer Science+Business Media New York 2012

Authors and Affiliations

  1. 1.School of Chemistry & Cardiff Catalysis InstituteCardiff UniversityCardiffUK

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