Cytochrome P450 as Dimerization Catalyst in Diketopiperazine Alkaloid Biosynthesis

ChemBioChem
2014.0

Abstract

As dimeric natural products frequently exhibit useful biological activities, identifying and understanding their mechanisms of dimerization is of great interest. One such compound is (-)-ditryptophenaline, isolated from Aspergillus flavus, which inhibits substance P receptor for potential analgesic and anti-inflammatory activity. Through targeted gene knockout in A. flavus and heterologous yeast gene expression, we determined for the first time the gene cluster and pathway for the biosynthesis of a dimeric diketopiperazine alkaloid. We also determined that a single cytochrome P450, DtpC, is responsible not only for pyrroloindole ring formation but also for concurrent dimerization of N-methylphenylalanyltryptophanyl diketopiperazine monomers into a homodimeric product. Furthermore, DtpC exhibits relaxed substrate specificity, allowing the formation of two new dimeric compounds from a non-native monomeric precursor, brevianamide F. A radical-mediated mechanism of dimerization is proposed. Two for the price of one: Dimeric natural products exhibit useful biological activities. We identified a cytochrome P450, DtpC, that performed pyrroloindole ring formation and concurrent dimerization of a diketopiperazine into a homodimeric substance P receptor-inhibiting alkaloid, (-)-ditryptophenaline. Relaxed substrate specificity of DtpC also allowed the formation of two additional novel homo- and heterodimeric compounds. © 2014 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.

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