Bacterial Alkaloid Biosynthesis: Structural Diversity via a Minimalistic Nonribosomal Peptide Synthetase

Martin Klapper, Daniel Braga, Gerald Lackner, Rosa Herbst, Pierre Stallforth

Index: 10.1016/j.chembiol.2018.02.013

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Abstract

Chemical and biochemical analyses of one of the most basic nonribosomal peptide synthetases (NRPS) from aPseudomonas fluorescensstrain revealed its striking plasticity. Determination of the potential substrate scope enabled us to anticipate novel secondary metabolites that could subsequently be isolated and tested for their bioactivities. Detailed analyses of the monomodular pyreudione synthetase showed that the biosynthesis of the bacterial pyreudione alkaloids does not require additional biosynthetic enzymes. Heterologous expression of a similar and functional, yet cryptic, NRPS ofPseudomonas entomophilawas successful and allowed us to perform a phylogenetic analysis of their thioesterase domains.