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Related Experiment Video

Updated: Jan 7, 2026

Determination of Microbial Extracellular Enzyme Activity in Waters, Soils, and Sediments using High Throughput Microplate Assays
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Fluorogenic Substrate for Monitoring Activity of Muralytic Enzymes.

Marcell Simon1, Amber L B Mogg1, Chloë F Klein1

  • 1Department of Natural Sciences of Pitzer and Scripps Colleges, Claremont, California 91711, United States.

ACS Omega
|January 1, 2026
PubMed
Summary

Researchers developed a novel substrate to easily measure the activity of muralytic enzymes, which are promising alternatives to antibiotics for fighting bacterial infections. This tool aids in developing new enzyme therapeutics against antibiotic-resistant bacteria.

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Area of Science:

  • Biochemistry
  • Microbiology
  • Enzymology

Background:

  • Antibiotic-resistant infections pose a significant global health threat, driving the need for novel therapeutic strategies.
  • Muralytic enzymes offer a promising alternative to traditional antibiotics due to their potent bactericidal activity and limited bacterial resistance.
  • Current limitations in high-throughput assays hinder the development and characterization of muralytic enzyme therapeutics.

Purpose of the Study:

  • To develop and validate a novel internally quenched substrate for high-throughput assessment of muralytic enzyme activity.
  • To demonstrate the substrate's utility in characterizing enzymes targeting Gram-positive bacteria.
  • To facilitate the development of new enzyme-based antibacterial therapies.

Main Methods:

  • Design and synthesis of an internally quenched substrate.
  • Enzyme activity assays using the substrate with bacterial lysates containing LytM and lysostaphin catalytic domains.
  • Evaluation of substrate performance with native enzymes and their mutants.
  • Mock screening to assess high-throughput capability.

Main Results:

  • The internally quenched substrate successfully detected activity of LytM and lysostaphin catalytic domains in bacterial lysate.
  • A robust signal-to-background ratio was achieved, confirming substrate sensitivity.
  • The substrate differentiated activity levels between native enzymes and their engineered mutants.
  • Mock screening demonstrated the substrate's suitability for high-throughput analysis.

Conclusions:

  • A novel, sensitive substrate has been developed for assaying muralytic enzyme activity against Gram-positive bacteria.
  • This tool enables high-throughput characterization of existing and engineered muralytic enzymes.
  • The developed substrate lays the foundation for broader applications in enzyme therapeutic development.