The fungal natural product aspergillomarasmine A has been identified as a potent and selective inhibitor of metallo-β-lactamases and a promising codrug candidate to fight antibiotic resistant bacteria. Poelarends and co-workers now report the efficient asymmetric chemoenzymatic synthesis of aspergillomarasmine A as well as similar complex natural products. The synthetic route highlights a highly regio- and stereoselective carbon–nitrogen bond-forming step catalysed by ethylenediamine-N,N′-disuccinic acid lyase. This enzyme accepts a wide variety of amino acids with terminal amino groups for selective addition to fumarate, facilitating the production of valuable metal-chelating aminocarboxylic acids, which are being used in a broad range of domestic products and industrial and medical applications. The results were published online last week in the prominent scientific journal Nature Catalysis.
Prof.dr. Gerrit J. Poelarends
Chemoenzymatic asymmetric synthesis of the metallo-β-lactamase inhibitor Aspergillomarasmine A and related aminocarboxylic acids
, Nature Catalysis, 8 March 2018. Authors: Haigen Fu, Jielin Zhang, Mohammad Saifuddin, Gea Cruiming, Pieter G. Tepper, and Gerrit J. Poelarends.
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