title: An easy-to-perform photometric assay for methyltransferase activity measurements.
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.
authors.affiliation: Institute for Pharamceutical Biology, University of Bonn, 53115 Bonn, Germany.
authors.forename: Till F
authors.initials: TF
authors.lastname: Schäberle
authors.forename: Christian
authors.initials: C
authors.lastname: Siba
authors.forename: Thomas
authors.initials: T
authors.lastname: Höver
authors.forename: Gabriele M
authors.initials: GM
authors.lastname: König
mesh_terms: D057075:Enzyme Assays / Q000379:methods*; D008745:Methylation; D008780:Methyltransferases / Q000032:analysis* / Q000378:metabolism; D010783:Photometry; D015203:Reproducibility of Results; D013997:Time Factors
chemical_list: D008780:Methyltransferases