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

被引：62

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

来源：

ANGEWANDTE CHEMIE-INTERNATIONAL EDITION | 2009年 / 48卷 / 31期

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：

0703 ;

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

页码：5756 / 5759

页数：4

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