Structure of active IspH enzyme from escherichia coli provides mechanistic insights into substrate reduction
KAUST DepartmentKAUST Catalysis Center (KCC)
Physical Sciences and Engineering (PSE) Division
Chemical Science Program
Biological & Organometallic Catalysis Laboratories
Permanent link to this recordhttp://hdl.handle.net/10754/561426
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AbstractThe 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.
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