Abstract
Abstract Recent studies on a novel C–C bond formation enzyme, Diels–Alderase, show that this unusual enzyme is involved in the biosynthesis of secondary metabolites. In this account, I describe studies related to Diels–Alderases including biomimetic synthesis, the biological utilization of the Diels–Alder reaction, and natural Diels–Alderases. The function and catalytic mechanism of natural Diels–Alderases, such as solanapyrone synthase, lovastatin nonaketide synthase, and macrophomate synthase, are of great interest due to the diversity of molecular skeletons in natural Diels–Alder adducts. The first structure analysis of macrophomate synthase provided information on detailed mechanisms regarding active site organization among the substrates, metal and amino acid residues, and regarding how to avoid product inhibition.
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