Coenzyme A Tethering Mediates Dehydratase Substrate Promiscuity and Reaction Specificity in Platensimycin, Platencin, and Platensilin Biosynthesis.

ABSTRACT: Biosynthetic studies of the platensimycin (PTM), platencin (PTN), and platensilin (PTL) family of natural products have revealed numerous insights into the chemistry and enzymology of diterpenoid biosynthesis. A deeper understanding of the PTM biosynthetic machinery would advance fundamental knowledge in natural product biosynthesis and facilitate future efforts to exploit these compounds as potential leads for biomedical applications. Herein, we report the functional characterization of the ptmU1 gene that encodes the dehydratase responsible for the formation of the C6-C7 enone moiety in PTM, PTN, and PTL. In vitro experiments, enabled by the semisynthesis of designer substrates and mimics, reveal that PtmU1 is selective for multiple coenzyme A (CoA)-tethered substrates but specifi

SUBMITTER: Fluegel LL 

PROVIDER: S-EPMC12746908 | biostudies-literature | 2025 Aug

REPOSITORIES: biostudies-literature