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

被引:64
作者
Graewert, Tobias [1 ]
Rohdich, Felix [1 ]
Span, Ingrid [1 ]
Bacher, Adelbert [1 ]
Eisenreich, Wolfgang [1 ]
Eppinger, Joerg
Groll, Michael [1 ]
机构
[1] Tech Univ Munich, Dept Chem, Lehrstuhl Biochem, Ctr Integrated Prot Sci, D-85747 Garching, Germany
关键词
iron-sulfur clusters; enzymes; isoprenes; non-mevalonate pathway; reaction mechanisms; DEOXYXYLULOSE PHOSPHATE-PATHWAY; NON-MEVALONATE PATHWAY; IRON-SULFUR PROTEINS; ISOPRENOID BIOSYNTHESIS; ISOPENTENYL DIPHOSPHATE; LYTB PROTEIN; FOSMIDOMYCIN; CLUSTERS;
D O I
10.1002/anie.200900548
中图分类号
O6 [化学];
学科分类号
070301 [无机化学];
摘要
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.
引用
收藏
页码:5756 / 5759
页数:4
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