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A substrate-multiplexed platform for profiling enzymatic potential of plant family 1 glycosyltransferases
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A substrate-multiplexed platform for profiling enzymatic potential of plant family 1 glycosyltransferases
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Journal Article
A substrate-multiplexed platform for profiling enzymatic potential of plant family 1 glycosyltransferases
2025
Overview
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.
Most enzymes involved in plant natural products biosynthesis remain uncharacterized. Here, the authors establish a screening pipeline and apply it to family 1 glycosyltransferases to reveal their promiscuity and preference for planar, hydroxylated aromatic substrates.
Publisher
Nature Publishing Group UK,Nature Publishing Group,Nature Portfolio
