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    Structure of the Dioxygenase AsqJ: Mechanistic Insights into a One-Pot Multistep Quinolone Antibiotic Biosynthesis

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    Type
    Article
    Authors
    Bräuer, Alois
    Beck, Philipp
    Hintermann, Lukas
    Groll, Michael
    KAUST Grant Number
    1974-01
    Date
    2015-11-10
    Online Publication Date
    2015-11-10
    Print Publication Date
    2016-01-04
    Permanent link to this record
    http://hdl.handle.net/10754/599770
    
    Metadata
    Show full item record
    Abstract
    © 2016 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim. Multienzymatic cascades are responsible for the biosynthesis of natural products and represent a source of inspiration for synthetic chemists. The FeII/α-ketoglutarate-dependent dioxygenase AsqJ from Aspergillus nidulans is outstanding because it stereoselectively catalyzes both a ferryl-induced desaturation reaction and epoxidation on a benzodiazepinedione. Interestingly, the enzymatically formed spiro epoxide spring-loads the 6,7-bicyclic skeleton for non-enzymatic rearrangement into the 6,6-bicyclic scaffold of the quinolone alkaloid 4′-methoxyviridicatin. Herein, we report different crystal structures of the protein in the absence and presence of synthesized substrates, surrogates, and intermediates that mimic the various stages of the reaction cycle of this exceptional dioxygenase.
    Citation
    Bräuer A, Beck P, Hintermann L, Groll M (2015) Structure of the Dioxygenase AsqJ: Mechanistic Insights into a One-Pot Multistep Quinolone Antibiotic Biosynthesis. Angew Chem Int Ed 55: 422–426. Available: http://dx.doi.org/10.1002/anie.201507835.
    Sponsors
    This work was supported by the 1974-01 TUM-KAUST agreement on selective C[BOND]H bond activation (A.B.) and SFB749 (M.G.). We thank the staff of the beamline X06SA at the Paul Scherrer Institute, SLS, Villigen (Switzerland) for assistance during data collection.
    Publisher
    Wiley
    Journal
    Angewandte Chemie
    DOI
    10.1002/anie.201507835
    PubMed ID
    26553478
    ae974a485f413a2113503eed53cd6c53
    10.1002/anie.201507835
    Scopus Count
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