Active site mutagenesis of the putative Diels–Alderase macrophomate synthase

Jörg M. Serafimov; Hans Christian Lehmann; Hideaki Oikawa; Donald Hilvert

doi:10.1039/B703177G

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Chemical Communications

Issue 17, 2007

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Active site mutagenesis of the putative Diels–Alderase macrophomate synthase

Jörg M. Serafimov , Hans Christian Lehmann , Hideaki Oikawa and Donald Hilvert

Chem. Commun., 2007, 1701-1703

DOI: 10.1039/B703177G
Received 02 Mar 2007, Accepted 15 Mar 2007
First published on the web 28 Mar 2007

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Abstract
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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.

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Details on preparation and characterization of the protein variants
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Chemical Communications

Active site mutagenesis of the putative Diels–Alderase macrophomate synthase

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