Characterization of the cyclodipeptide synthase gene cluster in Streptomyces sp. NRRL F-5123 by unraveling the biosynthesis of drimentine B

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2023.0

Abstract

Drimentines (DMTs) are a family of bacterial alkaloids featuring a 2,5-diketopiperazine (2, 5-DKP) ring with diverse bioactivities. In this study, we characterized the biosynthetic pathway of DMT B through gene combinations and biochemical investigations. While cyclo(L-Trp-L-Pro) (cWP) is synthesized by a tRNA-dependent cyclodipeptide synthase (CDPS) DmtB2, further tailoring steps are achieved sequen-tially through cyclodipeptide oxidases DmtD2_E2, prenyltransferase DmtC2, and terpene cyclase DmtA2. Our results deepen the understanding of the biosynthetic logic of DMT compounds, providing additional biological information for the structural diversification of terpenylated DKP compounds.(c) 2022 Elsevier Ltd. All rights reserved.

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