TY - JOUR
T1 - Structure of active IspH enzyme from escherichia coli provides mechanistic insights into substrate reduction
AU - Gräwert, Tobias
AU - Rohdich, Felix
AU - Span, Lngrid
AU - Backer, Adelbert
AU - Eisenreich, Wolfgang
AU - Eppinger, Jörg
AU - Groll, Michael
N1 - KAUST Repository Item: Exported on 2020-10-01
PY - 2009/7/20
Y1 - 2009/7/20
N2 - 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.
AB - 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.
UR - http://hdl.handle.net/10754/561426
UR - http://doi.wiley.com/10.1002/anie.200900548
UR - http://www.scopus.com/inward/record.url?scp=70349786242&partnerID=8YFLogxK
U2 - 10.1002/anie.200900548
DO - 10.1002/anie.200900548
M3 - Article
C2 - 19569147
SN - 1433-7851
VL - 48
SP - 5756
EP - 5759
JO - Angewandte Chemie International Edition
JF - Angewandte Chemie International Edition
IS - 31
ER -