Journal article

Publication year: 2013

Pages: 38-40

Journal: Analytical Biochemistry

Volume number: 432

Issue number: 1

ISSN: 0003-2697

DOI Link: https://doi.org/10.1016/j.ab.2012.09.026

Publisher: Elsevier

Abstract: 
Methyltransferases (MTs) catalyze the transfer of a methyl group from S-adenosylmethionine (SAM) to a suitable substrate. Such methylations are important modifications in secondary metabolisms, especially on natural products produced by polyketide synthases and nonribosomal peptide synthetases, many of which are of special interest due to their prominent pharmacological activities (e.g., lovastatin, cyclosporin). To gain basic biochemical knowledge on the methylation process, it is of immense relevance to simplify methods concerning experimental problems caused by a large variety in substrates. Here, we present a photometric method to analyze MT activity by measuring SAM consumption in a coupled enzyme assay. (C) 2012 Elsevier Inc. All rights reserved.

Harvard Citation style: Schäberle, T., Siba, C., Höver, T. and König, G. (2013) An easy-to-perform photometric assay for methyltransferase activity measurements, Analytical Biochemistry, 432(1), pp. 38-40. https://doi.org/10.1016/j.ab.2012.09.026

APA Citation style: Schäberle, T., Siba, C., Höver, T., & König, G. (2013). An easy-to-perform photometric assay for methyltransferase activity measurements. Analytical Biochemistry. 432(1), 38-40. https://doi.org/10.1016/j.ab.2012.09.026