Evidence map›Paper›PMID 40640145›Full record

ArticleNature communications2025

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 1 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Nature communications, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

2 citing papers in PubMed.

  1. Article
  2. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

11 authors.

Sasilada Sirirungruang *Department of Plant and Microbial Biology, University of California, Berkeley, CA, USA.ORCID http://orcid.org/0000-0002-2624-5124
Vincent Blay *Joint BioEnergy Institute, Emeryville, CA, USA.ORCID http://orcid.org/0000-0001-9602-2375
Elys P RodriguezDepartment of Chemistry, University of California, Davis, CA, USA.
Yasmine F ScottJoint BioEnergy Institute, Emeryville, CA, USA.
Khanh M VuuJoint BioEnergy Institute, Emeryville, CA, USA.ORCID http://orcid.org/0000-0002-9167-9041
Collin R BarnumDepartment of Plant Biology, University of California, Davis, CA, USA.
Paul H OpgenorthJoint BioEnergy Institute, Emeryville, CA, USA.
Fanzhou KongDepartment of Chemistry, University of California, Davis, CA, USA.
Yuanyue LiWest Coast Metabolomics Center, University of California, Davis, CA, USA.ORCID http://orcid.org/0000-0001-5971-0355
Oliver FiehnDepartment of Chemistry, University of California, Davis, CA, USA.ORCID http://orcid.org/0000-0002-6261-8928
Patrick M ShihDepartment of Plant and Microbial Biology, University of California, Berkeley, CA, USA. pmshih@berkeley.edu.ORCID http://orcid.org/0000-0002-2119-3345

Funding

UC Davis Training Program in Chemical BiologyT32GM136597 · NIGMS · UNIVERSITY OF CALIFORNIA AT DAVIS · PI SHEILA Sue DAVID, Marie C. Heffern · 2021 to 2026
$1.7M
Developing plant synthetic biology platforms to elucidate the role of natural productsR00AT009573 · NCCIH · UNIVERSITY OF CALIFORNIA BERKELEY · PI SHIH, PATRICK · 2018 to 2020
$704k
NCCIH NIH HHS R00 AT009573NIGMS NIH HHS T32 GM136597U.S. Department of Energy (DOE) DE-AC02-05CH11231
6 · The paper itself

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.

Indexed as

GlycosyltransferasesPlant ProteinsPlantsBiological ProductsGlycosylationSubstrate SpecificityBiological ProductsGlycosyltransferasesPlant Proteins

Identifiers

PMID40640145
PMCPMC12246196

What OpenQuestion holds

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LicenceCC BY
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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.