Journalartikel
Autorenliste: Schäberle, TF; Siba, C; Höver, T; König, GM
Jahr der Veröffentlichung: 2013
Seiten: 38-40
Zeitschrift: Analytical Biochemistry
Bandnummer: 432
Heftnummer: 1
ISSN: 0003-2697
DOI Link: https://doi.org/10.1016/j.ab.2012.09.026
Verlag: 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.
Zitierstile
Harvard-Zitierstil: 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-Zitierstil: 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