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Broad-range glycosidase activity profiling.

Balakumaran Chandrasekar¹, Thomas Colby², Asif Emran Khan Emon³

¹From the ‡Plant Chemetics Laboratory, Department of Plant Sciences, University of Oxford, South Parks Road, Oxford OX1 3RB, United Kingdom; §Plant Chemetics Laboratory, Max Planck Institute for Plant Breeding Research, Carl-von-Linne Weg 10, 50829 Cologne, Germany;

Molecular & Cellular Proteomics : MCP

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Summary

Researchers developed a new method to identify active plant glycosidases, revealing previously unknown enzymes and their functions in plant biology. This activity-based profiling offers a powerful tool for understanding these crucial enzymes.

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Area of Science:

Biochemistry
Plant Biology
Proteomics

Background:

Plants possess numerous glycosidases vital for cell wall remodeling, protein/lipid modification, and metabolite conversion.
Understanding these enzymes is limited due to post-translational regulation and elusive substrates.

Purpose of the Study:

To develop and apply an activity-based glycosidase profiling method for identifying active retaining glycosidases in plants.
To uncover previously uncharacterized glycosidases and their functional states.

Main Methods:

Utilized cell-permeable small molecular probes for activity-dependent covalent labeling of active site nucleophiles in retaining glycosidases.
Employed mass spectrometry to detect and identify labeled glycosidases.
Applied the method across different plant organs, species, and subproteomes, including living cells.

Main Results:

Successfully detected the active state of dozens of myrosinases, glucosidases, xylosidases, and galactosidases from seven families.
Identified active states of previously uncharacterized glycosidases, including one from a pseudogene.
Revealed diverse active xylosidases, galactosidases, glucanases, and heparanases in the cell wall of Nicotiana benthamiana.

Conclusions:

Activity-based glycosidase profiling is a simple, broadly applicable method for functional proteomic analysis.
This approach provides novel insights into the active repertoire of plant glycosidases.
The study highlights a new layer of functional proteomic information on active glycosidases in plants.