| Literature DB >> 29606578 |
Martin Klapper1, Daniel Braga2, Gerald Lackner2, Rosa Herbst1, Pierre Stallforth3.
Abstract
Chemical and biochemical analyses of one of the most basic nonribosomal peptide synthetases (NRPS) from a Pseudomonas fluorescens strain 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 of Pseudomonas entomophila was successful and allowed us to perform a phylogenetic analysis of their thioesterase domains.Entities:
Keywords: A domain specificity; Dieckmann cyclization; Pseudomonas; Te domain phylogeny; bacterial alkaloids; biosynthesis; heterologous expression; monomodular nonribosomal peptide synthetase; pyreudiones
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Year: 2018 PMID： 29606578 DOI： 10.1016/j.chembiol.2018.02.013
Source DB: PubMed Journal: Cell Chem Biol ISSN： 2451-9448 Impact factor: 8.116