Lytic transglycosidases catalyze the breakdown of glycosidic linkages (MurNAc to GlcNAc) of peptidoglycan in Gram-negative bacteria. The natural product bulgecin A has been shown to inhibit lytic transglycosidase activity as well as potentiate the activity of b-lactam antibiotics. Bulgecin A has been isolated from two ATCC strains (31433 and 31363), which are historically phenotypically characterized as taxonomically distinct Pseudomonads. Yet, the lack of a robust synthetic route or a bacterial over-producing strain has limited further study. The assembled genomes provide a detailed genetic understanding of the isolates’ taxonomy, operon regulation elements, and proteins coded in putative natural-product pathways. Comparative bioinformatic analysis of the shared secondary metabolite pathways revealed a conserved NRPS and a poorly annotated glycoamino acid pathway. These results enable pathway biochemical characterization and strain growth conditioning for the production of these novel compounds.

Analysis of pathways from ATCC 31433 and ATCC 31363, two Burkholderiaceae producers of Bulgecin A and sulfazecin-type monobactams

2019 Fall National Meeting

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