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Publication in Nature Communications: Covalent warhead assembly in fostriecin biosynthesis involves malonylationlactonisation by a bifunctional thioesterase and enzymatic demalonylation
10.03.2026
A part of Lisa's PhD thesis was just published in Nature Communications.
In this article we analyzed the biosynthesis of fostriecin and could demonstrate that FosMod8 produces a 3-O-malonyllactone by the unusual bifunctional thioesterase FosTE, which catalyses O-malonylation and subsequent lactonisation. Additionally, we show that the formation of the α,β-Unsaturated δ-lactone (AUDL) is carried out by the demalonylating enzyme FosM, whose activity strongly depends on prior fostriecin backbone phosphorylation by the broad-specific kinase FosH.
Congratulations to Lisa and all other contributors!