The predominance of nucleotidyl activation in bacterial phosphonate biosynthesis

Kyle Rice, Kissa Batul, Jacqueline Whiteside, Jayne Kelso, Monica Papinski, Edward Schmidt, Alena Pratasouskaya, Dacheng Wang, Rebecca Sullivan, Christopher Bartlett, Joel T. Weadge, Marc W. Kamp, Gabriel Moreno-Hagelsieb, Michael D. Suits and Geoff P. Horsman ()
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Kyle Rice: Wilfrid Laurier University
Kissa Batul: Wilfrid Laurier University
Jacqueline Whiteside: Wilfrid Laurier University
Jayne Kelso: Wilfrid Laurier University
Monica Papinski: Wilfrid Laurier University
Edward Schmidt: Wilfrid Laurier University
Alena Pratasouskaya: Wilfrid Laurier University
Dacheng Wang: Wilfrid Laurier University
Rebecca Sullivan: Wilfrid Laurier University
Christopher Bartlett: Wilfrid Laurier University
Joel T. Weadge: Wilfrid Laurier University
Marc W. Kamp: University of Bristol
Gabriel Moreno-Hagelsieb: Wilfrid Laurier University
Michael D. Suits: Wilfrid Laurier University
Geoff P. Horsman: Wilfrid Laurier University

Nature Communications, 2019, vol. 10, issue 1, 1-12

Abstract: Abstract Phosphonates are rare and unusually bioactive natural products. However, most bacterial phosphonate biosynthetic capacity is dedicated to tailoring cell surfaces with molecules like 2-aminoethylphosphonate (AEP). Although phosphoenolpyruvate mutase (Ppm)-catalyzed installation of C-P bonds is known, subsequent phosphonyl tailoring (Pnt) pathway steps remain enigmatic. Here we identify nucleotidyltransferases in over two-thirds of phosphonate biosynthetic gene clusters, including direct fusions to ~60% of Ppm enzymes. We characterize two putative phosphonyl tailoring cytidylyltransferases (PntCs) that prefer AEP over phosphocholine (P-Cho) – a similar substrate used by the related enzyme LicC, which is a virulence factor in Streptococcus pneumoniae. PntC structural analyses reveal steric discrimination against phosphocholine. These findings highlight nucleotidyl activation as a predominant chemical logic in phosphonate biosynthesis and set the stage for probing diverse phosphonyl tailoring pathways.

Date: 2019
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Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:10:y:2019:i:1:d:10.1038_s41467-019-11627-6

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DOI: 10.1038/s41467-019-11627-6

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