Poelarends and coworkers publish in Nature Catalysis
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.
More information: Prof.dr. Gerrit J. Poelarends
Reference: 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.
| Last modified: | 15 March 2018 10.57 a.m. |
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