A substrate-multiplexed platform for profiling enzymatic potential of plant family 1 glycosyltransferases

Sasilada Sirirungruang, Vincent Blay, Elys P. Rodriguez, Yasmine F. Scott, Khanh M. Vuu, Collin R. Barnum, Paul H. Opgenorth, Fanzhou Kong, Yuanyue Li, Oliver Fiehn and Patrick M. Shih ()
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Sasilada Sirirungruang: University of California
Vincent Blay: Joint BioEnergy Institute
Elys P. Rodriguez: University of California
Yasmine F. Scott: Joint BioEnergy Institute
Khanh M. Vuu: Joint BioEnergy Institute
Collin R. Barnum: University of California
Paul H. Opgenorth: Joint BioEnergy Institute
Fanzhou Kong: University of California
Yuanyue Li: University of California
Oliver Fiehn: University of California
Patrick M. Shih: University of California

Nature Communications, 2025, vol. 16, issue 1, 1-12

Abstract: Abstract Plants have expanded various biosynthetic enzyme families to produce a wide diversity of natural products; however, most enzymes encoded in plant genomes remain uncharacterized, highlighting the need for new functional genomic approaches. Here, we report a platform enabling the rapid functional characterization of plant family 1 glycosyltransferases, which serve important roles in plant development, defense, and communication. Using substrate-multiplexed reactions, mass spectrometry, and automated analysis, we screen 85 enzymes against a diverse library of 453 natural products, for a total of nearly 40,000 possible reactions. The resulting dataset reveals a widespread promiscuity and a strong preference for planar, hydroxylated aromatic substrates among family 1 glycosyltransferases. We also characterize glycosyltransferases with an unusually wide substrate scope and with a non-canonical Cys-Asp catalytic dyad. This work establishes a widely-applicable enzymatic screening pipeline, reflects the immense glycosylation capability of plants, and has implications in biocatalysis, metabolic engineering, and gene discovery.

Date: 2025
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DOI: 10.1038/s41467-025-61530-6

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