Issue 17, 2007
From the journal:

Chemical Communications

Active site mutagenesis of the putative Diels–Alderase macrophomate synthase†

Jörg M. Serafimov,a   Hans Christian Lehmann,a   Hideaki Oikawab  and  Donald Hilvert*a  

* Corresponding authors

a Laboratory of Organic Chemistry, ETH Zurich, CH-8093 Zurich, Switzerland
E-mail: hilvert@org.chem.ethz.ch
Fax: +41-44-632-1486
Tel: +41-44-632-3176

b Division of Chemistry, Graduate School of Science, Hokkaido University, Sapporo 060-0810, Japan

Abstract

Although the macrophomate synthase active site is rich in potential functional groups, site-directed mutagenesis shows that only three residues are absolutely required for catalysis of oxaloacetate decarboxylation and trapping of the resulting enolate with a 2-pyrone; the other residues that line the binding pocket are surprisingly tolerant to substitution.

Graphical abstract: Active site mutagenesis of the putative Diels–Alderase macrophomate synthase

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Article information

DOI
https://doi.org/10.1039/B703177G
Article type
Communication
Submitted
02 Mar 2007
Accepted
15 Mar 2007
First published
28 Mar 2007

Chem. Commun., 2007, 1701-1703

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Active site mutagenesis of the putative Diels–Alderase macrophomate synthase

J. M. Serafimov, H. C. Lehmann, H. Oikawa and D. Hilvert, Chem. Commun., 2007, 1701 DOI: 10.1039/B703177G

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