Issue 20, 2011
From the journal:

Organic & Biomolecular Chemistry

Templating effects in aristolochene synthase catalysis: elimination versus cyclisation†

Juan A. Faraldos,‡a   Verónica González,‡a   Michael Senske§a  and  Rudolf K. Allemann*a  

* Corresponding authors

a School of Chemistry, Cardiff University, Main Building, Park Place, Cardiff, United Kingdom
E-mail: allemannrk@cf.ac.uk
Fax: +44 29 2087 4030

Abstract

Analysis of the products generated by mutants of aristolochene synthase from P. roqueforti (PR-AS) revealed the prominent structural role played by the aliphatic residue Leu 108 in maintaining the productive conformation of farnesyl diphosphate to ensure C1–C10 (σ-bond) ring-closure and hence (+)-aristolochene production.

Graphical abstract: Templating effects in aristolochene synthase catalysis: elimination versus cyclisation

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Article information

DOI
https://doi.org/10.1039/C1OB06184D
Article type
Communication
Submitted
16 Jul 2011
Accepted
11 Aug 2011
First published
12 Aug 2011

Org. Biomol. Chem., 2011,9, 6920-6923

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Templating effects in aristolochene synthase catalysis: elimination versus cyclisation

J. A. Faraldos, V. González, M. Senske and R. K. Allemann, Org. Biomol. Chem., 2011, 9, 6920 DOI: 10.1039/C1OB06184D

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