Article published in Angew. Chem. Int. Ed.

Our new methyltransferase assay has been just accepted for publication in Angew. Chem. Int. Ed., see here. In this publication, we describe a continuous fluorescence-based, high-throughput assay for SAM-dependent methyltransferases (MTs). This assay involves two enzymatic steps for the conversion of S-adenosyl-L-homocysteine into hydrogensulfide (H2S) to result in a selective fluorescence readout via reduction of a azidocoumarin sulfide probe. Investigation of two O-MTs and an N-MT confirmed that this assay is suitable for the determination of methyltransferase activity directly in E. coli cell lysates without the need of protein purification. Enjoy reading.

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