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Discovery of Unprecedented Hydrazine-Forming Machinery in Bacteria.

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... Full description

Journal Title: Journal of the American Chemical Society July 25, 2018, Vol.140(29), pp.9083-9086
Main Author: Matsuda, Kenichi
Other Authors: Tomita, Takeo , Shin-Ya, Kazuo , Wakimoto, Toshiyuki , Kuzuyama, Tomohisa , Nishiyama, Makoto
Format: Electronic Article Electronic Article
Language: English
Subjects:
ID: E-ISSN: 1520-5126 ; DOI: 10.1021/jacs.8b05354
Link: http://search.proquest.com/docview/2070241983/?pq-origsite=primo
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recordid: proquest2070241983
title: Discovery of Unprecedented Hydrazine-Forming Machinery in Bacteria.
format: Article
creator:
  • Matsuda, Kenichi
  • Tomita, Takeo
  • Shin-Ya, Kazuo
  • Wakimoto, Toshiyuki
  • Kuzuyama, Tomohisa
  • Nishiyama, Makoto
subjects:
  • Amino Acid Sequence–Genetics
  • Bacteria–Biosynthesis
  • Dipeptides–Metabolism
  • Hydrazones–Genetics
  • Mixed Function Oxygenases–Genetics
  • Multigene Family–Genetics
  • Transferases–Genetics
  • Dipeptides
  • Hydrazones
  • Mixed Function Oxygenases
  • Transferases
ispartof: Journal of the American Chemical Society, July 25, 2018, Vol.140(29), pp.9083-9086
description: 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.
language: eng
source:
identifier: E-ISSN: 1520-5126 ; DOI: 10.1021/jacs.8b05354
fulltext: fulltext
issn:
  • 15205126
  • 1520-5126
url: Link


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titleDiscovery of Unprecedented Hydrazine-Forming Machinery in Bacteria.
creatorMatsuda, Kenichi ; Tomita, Takeo ; Shin-Ya, Kazuo ; Wakimoto, Toshiyuki ; Kuzuyama, Tomohisa ; Nishiyama, Makoto
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identifierE-ISSN: 1520-5126 ; DOI: 10.1021/jacs.8b05354
subjectAmino Acid Sequence–Genetics ; Bacteria–Biosynthesis ; Dipeptides–Metabolism ; Hydrazones–Genetics ; Mixed Function Oxygenases–Genetics ; Multigene Family–Genetics ; Transferases–Genetics ; Dipeptides ; Hydrazones ; Mixed Function Oxygenases ; Transferases
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descriptionRecent 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.
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