Structure of active IspH enzyme from escherichia coli provides mechanistic insights into substrate reduction

Handle URI:
http://hdl.handle.net/10754/561426
Title:
Structure of active IspH enzyme from escherichia coli provides mechanistic insights into substrate reduction
Authors:
Gräwert, Tobias; Rohdich, Felix; Span, Lngrid; Backer, Adelbert; Eisenreich, Wolfgang; Eppinger, Jorg ( 0000-0001-7886-7059 ) ; Groll, Michael
Abstract:
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.
KAUST Department:
KAUST Catalysis Center (KCC); Physical Sciences and Engineering (PSE) Division; Chemical Science Program; Biological & Organometallic Catalysis Laboratories
Publisher:
Wiley-Blackwell
Journal:
Angewandte Chemie International Edition
Issue Date:
20-Jul-2009
DOI:
10.1002/anie.200900548
PubMed ID:
19569147
Type:
Article
ISSN:
14337851
Appears in Collections:
Articles; Physical Sciences and Engineering (PSE) Division; Chemical Science Program; KAUST Catalysis Center (KCC)

Full metadata record

DC FieldValue Language
dc.contributor.authorGräwert, Tobiasen
dc.contributor.authorRohdich, Felixen
dc.contributor.authorSpan, Lngriden
dc.contributor.authorBacker, Adelberten
dc.contributor.authorEisenreich, Wolfgangen
dc.contributor.authorEppinger, Jorgen
dc.contributor.authorGroll, Michaelen
dc.date.accessioned2015-08-02T09:10:59Zen
dc.date.available2015-08-02T09:10:59Zen
dc.date.issued2009-07-20en
dc.identifier.issn14337851en
dc.identifier.pmid19569147en
dc.identifier.doi10.1002/anie.200900548en
dc.identifier.urihttp://hdl.handle.net/10754/561426en
dc.description.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.en
dc.publisherWiley-Blackwellen
dc.subjectEnzymesen
dc.subjectIron-sulfur clustersen
dc.subjectIsoprenesen
dc.subjectNon-mevalonate pathwayen
dc.subjectReaction mechanismsen
dc.titleStructure of active IspH enzyme from escherichia coli provides mechanistic insights into substrate reductionen
dc.typeArticleen
dc.contributor.departmentKAUST Catalysis Center (KCC)en
dc.contributor.departmentPhysical Sciences and Engineering (PSE) Divisionen
dc.contributor.departmentChemical Science Programen
dc.contributor.departmentBiological & Organometallic Catalysis Laboratoriesen
dc.identifier.journalAngewandte Chemie International Editionen
dc.contributor.institutionCenter for Integrated Protein Science, Lehrstuhl für Biochemie Department Chemie, Technische Universität München, Lichtenbergstrasse 4, 85747 Garching, Germanyen
dc.contributor.institutionDepartment Chemie Technische, Universität München, Germanyen
kaust.authorEppinger, Jorgen

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