Active site mutagenesis of the putative Diels–Alderase macrophomate synthase
Literature Information
Jörg M. Serafimov, Hans Christian Lehmann, Hideaki Oikawa, Donald Hilvert
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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