Related Experiment Video
Updated: Apr 15, 2026
11:01
Preparation and In Vivo Use of an Activity-based Probe for N-acylethanolamine Acid Amidase
Published on: November 23, 2016
10.3K
Development of a clickable activity-based protein profiling (ABPP) probe for agmatine deiminases
Mikhail Marchenko1, Andrew Thomson1, Terri N Ellis2
1Department of Chemistry, University of North Florida, 1 UNF Dr., Jacksonville, FL 32224, USA.
Bioorganic & Medicinal Chemistry
|March 31, 2015
Summary
Researchers developed a new probe to study agmatine deiminases (AgDs) from pathogenic bacteria like Streptococcus mutans. This probe offers a selective and sensitive method for analyzing AgD enzyme activity and function.
Area of Science:
- Biochemistry
- Enzymology
- Microbiology
Background:
- Agmatine deiminases (AgDs) are enzymes involved in agmatine catabolism.
- AgDs are encoded by pathogenic bacteria, aiding their survival through energy production and acid tolerance.
- Understanding AgD function is crucial for targeting bacterial pathogens.
Purpose of the Study:
- To develop a novel chemical probe for studying AgDs.
- To specifically target the Agmatine Deiminase from Streptococcus mutans.
- To enable selective and sensitive analysis of AgD activity.
Main Methods:
- Development of a clickable activity-based protein profiling (ABPP) probe.
- The probe was designed to target the AgD enzyme.
- Testing for probe selectivity and sensitivity against Streptococcus mutans AgD.
Main Results:
- A clickable ABPP probe was successfully synthesized.
- The probe demonstrated high selectivity for the target AgD.
- The probe exhibited high sensitivity in detecting AgD activity.
- The probe facilitates the study of Streptococcus mutans AgD.
Conclusions:
- The developed clickable ABPP probe is a valuable tool for investigating AgD enzymes.
- This probe enables precise analysis of AgD from Streptococcus mutans.
- The findings contribute to understanding bacterial survival mechanisms and potential therapeutic targets.
