Oxidative dearomatisation: the key step of sorbicillinoid biosynthesis†Electronic supplementary information (ESI) available: Containing all experimental details. See DOI: 10.1039/c3sc52911hClick here for additional data file

An FAD-dependent monooxygenase encoding gene (SorbC) was cloned from E01-10/3 and expressed as a soluble protein in . The enzyme efficiently performed the oxidative dearomatisation of sorbicillin and dihydrosorbicillin to give sorbicillinol and dihydrosorbicillinol respectively. Bioinformatic examin...

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Bibliographic Details
Published in:Chemical science (Cambridge) 2014-02, Vol.5 (2), p.523-527
Main Authors: Fahad, Ahmed Al, Abood, Amira, Fisch, Katja M, Osipow, Anna, Davison, Jack, Avramović, Marija, Butts, Craig P, Piel, Jörn, Simpson, Thomas J, Cox, Russell J
Format: Article
Language:English
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Summary:An FAD-dependent monooxygenase encoding gene (SorbC) was cloned from E01-10/3 and expressed as a soluble protein in . 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 and . The gene -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.
ISSN:2041-6520