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High-throughput assays for SAM-dependent methyltransferases: advances, challenges, and future perspectives.

Renia Fotiadou1, Florian Heinz2, Konstantin F G Weigmann2

  • 1Department of Chemistry, University of Crete, Voutes University Campus, 70013 Heraklion, Greece. ipavlidis@uoc.gr.

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Summary

Methyltransferases are diverse enzymes that methylate substrates using S-adenosyl-L-methionine. This review examines high-throughput screening assays for monitoring their activity, crucial for enzyme engineering.

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Area of Science:

  • Biochemistry and enzymology
  • Molecular biology
  • Enzyme kinetics

Background:

  • Methyltransferases (EC 2.1.1.-) are functionally diverse enzymes found across all life domains, catalyzing essential methylation reactions.
  • Despite substrate diversity, most methyltransferases use S-adenosyl-L-methionine (SAM) as a common methyl donor.
  • Existing assays often struggle with complex substrates and regiospecificity, limiting enzyme engineering applications.

Purpose of the Study:

  • To critically review high-throughput screening assays for methyltransferase activity.
  • To address the need for efficient analysis in enzyme engineering.
  • To cover advancements in methyltransferase assay development up to January 2026.

Main Methods:

  • Review of colorimetric and fluorometric assays for methyltransferase activity.
  • Analysis of strategies based on detecting S-adenosyl-L-homocysteine (SAH) or its degradation products.
  • Evaluation of assays for purified enzymes versus crude cell lysates.

Main Results:

  • Colorimetric and fluorometric assays are widely used but have limitations.
  • Detection of SAH or its by-products is a common strategy.
  • Sophisticated tools are needed for regiospecificity determination in complex methylations.

Conclusions:

  • High-throughput screening assays are essential for exploiting methyltransferases, especially in enzyme engineering.
  • Continued development of robust and specific assays is needed.
  • This review provides a critical overview of current assay technologies.