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A Universal, Continuous Assay for SAM-dependent Methyltransferases.

Marian J Menke1, Pascal Schneider2, Christoffel P S Badenhorst1

  • 1Department of Biotechnology and Enzyme Catalysis, Institute of Biochemistry, University of Greifswald, Felix-Hausdorff-Str. 4, 17487, Greifswald, Germany.

Angewandte Chemie (International Ed. in English)
|November 2, 2023
PubMed
Summary
This summary is machine-generated.

We developed a high-throughput assay for screening S-adenosyl-l-methionine-dependent methyltransferases (MTs). This enzyme assay enables efficient identification of methyltransferases for drug discovery and development.

Keywords:
Enzyme CatalysisHigh-Throughput ScreeningHomocysteineHydrogen SulfideSAM-Dependent Methyltransferases

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Area of Science:

  • Biochemistry
  • Enzymology
  • Drug Discovery

Background:

  • Enzyme-catalyzed late-stage functionalization (LSF) offers a route to potent active pharmaceutical ingredients (APIs).
  • S-adenosyl-l-methionine-dependent methyltransferases (MTs) perform selective methylation, surpassing traditional chemical methods.
  • Identifying suitable MTs is crucial for advancing API development.

Purpose of the Study:

  • To develop a continuous fluorescence-based, high-throughput assay for screening SAM-dependent methyltransferases.
  • To enable efficient identification and characterization of methyltransferases for pharmaceutical applications.

Main Methods:

  • A novel two-step enzymatic assay was designed for S-adenosyl-l-homocysteine conversion to H2S.
  • A selective fluorescence readout was achieved using an azidocoumarin sulfide probe.
  • The assay was validated using E. coli cell lysates expressing O-MTs and N-MTs.

Main Results:

  • The developed assay successfully determined methyltransferase activity in E. coli cell lysates.
  • The assay demonstrated suitability for high-throughput screening of SAM-dependent methyltransferases.
  • Two O-MTs and one N-MT were investigated, confirming assay performance.

Conclusions:

  • The fluorescence-based assay is effective for identifying and characterizing methyltransferases.
  • This high-throughput method facilitates the discovery of novel APIs through LSF.
  • The assay supports the development of more potent drug candidates by leveraging enzymatic methylation.