Reductive dehydroxylation of allyl alcohols by IspH protein

Tobias Gräwert; Ingrid Span; Adelbert Bacher; Michael Groll

doi:10.1002/anie.201000833

Reductive dehydroxylation of allyl alcohols by IspH protein

Angew Chem Int Ed Engl. 2010 Nov 15;49(47):8802-9. doi: 10.1002/anie.201000833.

Authors

Tobias Gräwert¹, Ingrid Span, Adelbert Bacher, Michael Groll

Affiliation

¹ Center for Integrated Protein Science, Lehrstuhl für Biochemie, Technische Universität München, Lichtenbergstrasse 4, 85747 Garching, Germany. graewert@mytum.de

PMID: 20922726
DOI: 10.1002/anie.201000833

Abstract

The biosynthesis of natural products is a treasure trove of unusual reaction mechanisms. This Minireview summarizes recent work on the structure and mechanism of IspH protein, which catalyzes the reductive dehydroxylation of an allyl alcohol in a biosynthetic pathway leading to isoprenoid precursors.

Publication types

Research Support, Non-U.S. Gov't
Review

MeSH terms

Escherichia coli / enzymology
Escherichia coli Proteins / chemistry
Escherichia coli Proteins / metabolism*
Oxidation-Reduction
Oxidoreductases / chemistry
Oxidoreductases / metabolism*
Propanols / chemistry*
Protein Structure, Tertiary
Terpenes / metabolism*

Substances

Escherichia coli Proteins
Propanols
Terpenes
allyl alcohol
Oxidoreductases
ispH protein, E coli