Jump to main content
Jump to site search

Issue 89, 2012
Previous Article Next Article

Heterologous production of the lantibiotic Ala(0)actagardine in Escherichia coli

Author affiliations

Abstract

We report the heterologous production of Ala(0)actagardine in E. coli by co-expression of the substrate peptide GarA and its modification enzymes GarM and GarO. The activity of GarO, a luciferase-like monooxygenase that introduces the unique sulfoxide group of actagardine, was also investigated in vitro.

Graphical abstract: Heterologous production of the lantibiotic Ala(0)actagardine in Escherichia coli

Back to tab navigation
Please wait while Download options loads

Supplementary files

Publication details

The article was received on 31 Aug 2012, accepted on 19 Sep 2012, published on 04 Oct 2012 and first published online on 04 Oct 2012


Article type: Communication
DOI: 10.1039/C2CC36336D
Citation: Chem. Commun., 2012,48, 10966-10968
  • Open access: Creative Commons BY license
  •   Request permissions

    Heterologous production of the lantibiotic Ala(0)actagardine in Escherichia coli

    Y. Shi, A. Bueno and W. A. van der Donk, Chem. Commun., 2012, 48, 10966
    DOI: 10.1039/C2CC36336D

    This article is licensed under a Creative Commons Attribution 3.0 Unported Licence. Material from this article can be used in other publications provided that the correct acknowledgement is given with the reproduced material.

    Reproduced material should be attributed as follows:

    • For reproduction of material from NJC:
      [Original citation] - Published by The Royal Society of Chemistry (RSC) on behalf of the Centre National de la Recherche Scientifique (CNRS) and the RSC.
    • For reproduction of material from PCCP:
      [Original citation] - Published by the PCCP Owner Societies.
    • For reproduction of material from PPS:
      [Original citation] - Published by The Royal Society of Chemistry (RSC) on behalf of the European Society for Photobiology, the European Photochemistry Association, and RSC.
    • For reproduction of material from all other RSC journals:
      [Original citation] - Published by The Royal Society of Chemistry.

    Information about reproducing material from RSC articles with different licences is available on our Permission Requests page.

Search articles by author