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
Angew. Chem. Int. Ed., 48, 5756-5759, (2010)

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

Keywords

Terpene biosynthesis

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.

Code

DOI: 10.1002/anie.200900548

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