Literature DB >> 23022377

An easy-to-perform photometric assay for methyltransferase activity measurements.

Till F Schäberle1, Christian Siba, Thomas Höver, Gabriele M König.   

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.
Copyright © 2012 Elsevier Inc. All rights reserved.

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Year:  2012        PMID: 23022377     DOI: 10.1016/j.ab.2012.09.026

Source DB:  PubMed          Journal:  Anal Biochem        ISSN: 0003-2697            Impact factor:   3.365


  4 in total

1.  A direct, ratiometric, and quantitative MALDI-MS assay for protein methyltransferases and acetyltransferases.

Authors:  Stacie L Richardson; Pahul Hanjra; Gang Zhang; Brianna D Mackie; Darrell L Peterson; Rong Huang
Journal:  Anal Biochem       Date:  2015-03-14       Impact factor: 3.365

2.  Function of the loading module in CorI and of the O-methyltransferase CorH in vinyl carbamate biosynthesis of the antibiotic corallopyronin A.

Authors:  Till F Schäberle; Mahsa Mir Mohseni; Friederike Lohr; Alexander Schmitz; Gabriele M König
Journal:  Antimicrob Agents Chemother       Date:  2013-11-25       Impact factor: 5.191

3.  A continuous kinetic assay for protein and DNA methyltransferase enzymatic activities.

Authors:  Dan Levy; Amir Aharoni; Shai Duchin; Zlata Vershinin
Journal:  Epigenetics Chromatin       Date:  2015-12-15       Impact factor: 4.954

4.  Inhibition of Chikungunya virus by an adenosine analog targeting the SAM-dependent nsP1 methyltransferase.

Authors:  Rajat Mudgal; Supreeti Mahajan; Shailly Tomar
Journal:  FEBS Lett       Date:  2019-11-02       Impact factor: 4.124

  4 in total

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