Structural basis and enzymatic mechanism of the biosynthesis of C 9from C10-monoterpenoid indole alkaloids

Liuqing Yang, Marco Hill, Meitian Wang, Santosh Panjikar, Joachim Stöckigt

Research output: Contribution to journalArticleResearchpeer-review

12 Citations (Scopus)


Cutting carbons: The three-dimensional structure of polyneuridine aldehyde esterase (PNAE) gives insight into the enzymatic mechanism of the biosynthesis of C9- from C10-monoterpenoid indole alkaloids (see scheme). PNAE is a very substrate-specific serine esterase. It harbors the catalytic triad S87-D216-H244, and is a new member of the α/ β-fold hydrolase superfamily. Its novel function leads to the diversification of alkaloid structures.

Original languageEnglish
Pages (from-to)5211-5213
Number of pages3
JournalAngewandte Chemie - International Edition
Issue number28
Publication statusPublished - 29 Jun 2009
Externally publishedYes


  • Alkaloids
  • Biosynthesis
  • Enzyme catalysis
  • Esterases
  • Protein structures

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