Structure and Function of a "head-to-Middle" Prenyltransferase: Lavandulyl Diphosphate Synthase

Meixia Liu, Chun Chi Chen, Lu Chen, Xiansha Xiao, Yingying Zheng, Jian Wen Huang, Weidong Liu, Tzu Ping Ko, Ya Shan Cheng, Xinxin Feng, Eric Oldfield, Rey Ting Guo, Yanhe Ma

Research output: Contribution to journalArticlepeer-review


We report the first X-ray structure of the unique "head-to-middle" monoterpene synthase, lavandulyl diphosphate synthase (LPPS). LPPS catalyzes the condensation of two molecules of dimethylallyl diphosphate (DMAPP) to form lavandulyl diphosphate, a precursor to the fragrance lavandulol. The structure is similar to that of the bacterial cis-prenyl synthase, undecaprenyl diphosphate synthase (UPPS), and contains an allylic site (S1) in which DMAPP ionizes and a second site (S2) which houses the DMAPP nucleophile. Both S-thiolo-dimethylallyl diphosphate and S-thiolo-isopentenyl diphosphate bind intact to S2, but are cleaved to (thio)diphosphate, in S1. His78 (Asn in UPPS) is essential for catalysis and is proposed to facilitate diphosphate release in S1, while the P1 phosphate in S2 abstracts a proton from the lavandulyl carbocation to form the LPP product. The results are of interest since they provide the first structure and structure-based mechanism of this unusual prenyl synthase.

Original languageEnglish (US)
Pages (from-to)4721-4724
Number of pages4
JournalAngewandte Chemie - International Edition
Issue number15
StatePublished - Apr 4 2016


  • biosynthesis
  • fragrance
  • monoterpenes
  • natural products
  • structure elucidation

ASJC Scopus subject areas

  • Catalysis
  • General Chemistry


Dive into the research topics of 'Structure and Function of a "head-to-Middle" Prenyltransferase: Lavandulyl Diphosphate Synthase'. Together they form a unique fingerprint.

Cite this