Structure of Active IspH Enzyme from Escherichia coli Provides Mechanistic Insights into Substrate Reduction

Structure of Active IspH Enzyme from Escherichia coli Provides Mechanistic Insights into Substrate Reduction

Structure of Active IspH Enzyme from Escherichia coli Provides Mechanistic Insights into Substrate Reduction
T. Gräwert, F. Rohdich, I. Span, A. Bacher, W. Eisenreich, J. Eppinger, M. Groll
Angewandte Chemie International Edition, Volume 48, Issue 31, pages 5756–5759, (2009)
T. Gräwert, F. Rohdich, I. Span, A. Bacher, W. Eisenreich, J. Eppinger, M. Groll
Iron–sulfur clusters, Enzymes, Isoprenes, Non-mevalonate pathway, Reaction mechanisms
2009
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.
 







 
10.1002/anie.200900548
14337851