Jump to main content
Jump to site search

Issue 2, 2014
Previous Article Next Article

Oxidative dearomatisation: the key step of sorbicillinoid biosynthesis

Author affiliations

Abstract

An FAD-dependent monooxygenase encoding gene (SorbC) was cloned from Penicillium chrysogenum E01-10/3 and expressed as a soluble protein in Escherichia coli. The enzyme efficiently performed the oxidative dearomatisation of sorbicillin and dihydrosorbicillin to give sorbicillinol and dihydrosorbicillinol respectively. Bioinformatic examination of the gene cluster surrounding SorbC indicated the presence of two polyketide synthase (PKS) encoding genes designated sorbA and sorbB. The gene sorbA-encodes a highly reducing iterative PKS while SorbB encodes a non-reducing iterative PKS which features a reductive release domain usually involved in the production of polyketide aldehydes. Using these observations and previously reported results from isotopic feeding experiments a new and simpler biosynthetic route to the sorbicillin class of secondary metabolites is proposed which is consistent with all reported experimental results.

Graphical abstract: Oxidative dearomatisation: the key step of sorbicillinoid biosynthesis

Back to tab navigation

Supplementary files

Publication details

The article was received on 21 Oct 2013, accepted on 15 Nov 2013 and first published on 20 Nov 2013


Article type: Edge Article
DOI: 10.1039/C3SC52911H
Author version
available:
Download author version (PDF)
Chem. Sci., 2014,5, 523-527
  • Open access: Creative Commons BY license
    All publication charges for this article have been paid for by the Royal Society of Chemistry

  •   Request permissions

    Oxidative dearomatisation: the key step of sorbicillinoid biosynthesis

    A. A. Fahad, A. Abood, K. M. Fisch, A. Osipow, J. Davison, M. Avramović, C. P. Butts, J. Piel, T. J. Simpson and R. J. Cox, Chem. Sci., 2014, 5, 523
    DOI: 10.1039/C3SC52911H

    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

Spotlight

Advertisements