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Issue 17, 2007
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Active site mutagenesis of the putative Diels–Alderase macrophomate synthase

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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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Publication details

The article was received on 02 Mar 2007, accepted on 15 Mar 2007 and first published on 28 Mar 2007


Article type: Communication
DOI: 10.1039/B703177G
Citation: Chem. Commun., 2007,0, 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, 0, 1701
    DOI: 10.1039/B703177G

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