Discovery of Unprecedented Hydrazine-Forming Machinery in Bacteria

J Am Chem Soc. 2018 Jul 25;140(29):9083-9086. doi: 10.1021/jacs.8b05354. Epub 2018 Jul 17.

Abstract

Recent studies described several different routes that facilitate nitrogen-nitrogen bond formation in natural product biosynthesis. We report herein the identification of unprecedented machinery for hydrazine formation involved in the biosynthesis of s56-p1, a dipeptide natural product with a unique hydrazone unit. The gene cassette comprising this machinery is widespread across several bacterial phyla, highlighting the overlooked potential of bacteria to synthesize hydrazine.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Bacteria / genetics*
  • Dipeptides / biosynthesis*
  • Hydrazones / metabolism*
  • Mixed Function Oxygenases / genetics
  • Multigene Family*
  • Transferases / genetics

Substances

  • Dipeptides
  • Hydrazones
  • Mixed Function Oxygenases
  • Transferases