Active site mutagenesis of the putative Diels–Alderase macrophomate synthase

Literature Information

Publication Date 2007-03-28
DOI 10.1039/B703177G
Impact Factor 6.222
Authors

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


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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.

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