Phosphonate biosynthesis and catabolism: A treasure trove of unusual enzymology

Spencer C. Peck, Wilfred A. van der Donk

Research output: Contribution to journalReview article

Abstract

Natural product biosynthesis has proven a fertile ground for the discovery of novel chemistry. Herein we review the progress made in elucidating the biosynthetic pathways of phosphonate and phosphinate natural products such as the antibacterial compounds dehydrophos and fosfomycin, the herbicidal phosphinothricin-containing peptides, and the antimalarial compound FR-900098. In each case, investigation of the pathway has yielded unusual, and often unprecedented, biochemistry. Likewise, recent investigations have uncovered novel ways to cleave the C. P bond to yield phosphate under phosphorus starvation conditions. These include the discovery of novel oxidative cleavage of the C. P bond catalyzed by PhnY and PhnZ as well as phosphonohydrolases that liberate phosphate from phosphonoacetate. Perhaps the crown jewel of phosphonate catabolism has been the recent resolution of the longstanding problem of the C-P lyase responsible for reductively cleaving the C. P bond of a number of different phosphonates to release phosphate. Taken together, the strides made on both metabolic and catabolic fronts illustrate an array of fascinating biochemistry.

Original languageEnglish (US)
Pages (from-to)580-588
Number of pages9
JournalCurrent Opinion in Chemical Biology
Volume17
Issue number4
DOIs
StatePublished - Aug 1 2013

ASJC Scopus subject areas

  • Analytical Chemistry
  • Biochemistry

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