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 sequentially 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.
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