Structure of active IspH enzyme from escherichia coli provides mechanistic insights into substrate reduction

Tobias Gräwert, Felix Rohdich, Lngrid Span, Adelbert Backer, Wolfgang Eisenreich, Jörg Eppinger, Michael Groll

Research output: Contribution to journalArticlepeer-review

63 Scopus citations

Abstract

The terminal step of the non-mevalonate pathway of terpene biosynthesis is catalyzed by IspH (see scheme). In the crystal structure of IspH from E. coli, a bound inorganic diphosphate ligand occupies the position of the diphosphate residue of the substrate. Together with mutation studies and theoretical calculations, these data support a mechanism which is analogous to the Birch reduction of allylic alcohols. © 2009 Wiley-VCH Verlag GmbH & Co. KGaA.
Original languageEnglish (US)
Pages (from-to)5756-5759
Number of pages4
JournalAngewandte Chemie International Edition
Volume48
Issue number31
DOIs
StatePublished - Jul 20 2009

ASJC Scopus subject areas

  • Chemistry(all)
  • Catalysis

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