Structure of active IspH enzyme from escherichia coli provides mechanistic insights into substrate reduction
KAUST DepartmentBiological & Organometallic Catalysis Laboratories
Biological and Environmental Sciences and Engineering (BESE) Division
Chemical Science Program
KAUST Catalysis Center (KCC)
Office of the VP
Physical Science and Engineering (PSE) Division
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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