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Promiscuous Yet Specific: A Methionine–Aromatic Interaction Drives the Reaction Scope of the Family 1 Glycosyltransferase Gm UGT88E3 from Soybean
Open accessPublished version of a preprint
Abstract
Family 1 glycosyltransferases (GT1s, UGTs) catalyze the regioselective glycosylation of natural products in a single step. We identified GmUGT88E3 as a particularly promising biocatalyst, able to produce a variety of pure, single glycosidic products from polyphenols with high chemical yields. We investigated this particularly desirable duality towards specificity, i.e., promiscuous towards acceptors while regiospecific. Using high-field NMR, kinetic characterization, molecular dynamics simulations and mutagenesis studies, we uncovered that the main molecular determinant of GmUGT88E3 specificity is a methionine-aromatic bridge, an interaction often present in protein structures but never reported for enzyme-substrate interactions.
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Highly accurate protein structure prediction with AlphaFold
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Harding-Larsen, D., Madsen, C. D., Teze, D., Kittilä, T., Langhorn, M. R., Gharabli, H., Hobusch, M., Otalvaro, F. M., Kırtel, O., Bidart, G. N., et al. (2024) · ACS Omega · doi:10.1021/acsomega.4c01583 · Cited by 14
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Metadata
- Authors
- de Boer, R. M., H. Hvid, D. E., Davail, E., Vaitkus, D., Duus, J. Ø., Welner, D. H., & Teze, D.
- Affiliations
- Novo Nordisk Foundation (DK)
- The Novo Nordisk Foundation Center for Biosustainability, Technical University of Denmark, DK- 2800 Kongens Lyngby, Denmark
- Technical University of Denmark (DK)
- Corresponding author
- Welner, Ditte H.
- Venue
- Biochemistry
- Publisher
- American Chemical Society (ACS)
- Published
- 2023-11-27
- Volume
- 62
- Issue
- 23
- Pages
- 3343-3346
- ISSN
- 0006-2960 (ISSN-L)
- 1520-4995
- OpenAlex
- W4389036158
- Cited by
- 12
- References
- 1
- Citations by year
- 2026: 5 · 2025: 4 · 2024: 2 · 2023: 1
- FWCI
- 1.07
- Type
- journal article
- Language
- en
- Open access
- green
- doi.org
- Licence
- Locations
- Biochemistry (publishedVersion)
- ChemRxiv (acceptedVersion, cc-by-nc-nd)
- PubMed (publishedVersion)
- Funders
- Novo Nordisk Fonden (NNF18OC0034744, NNF20CC0035580, NNF10CC1016517)
- Villum Fonden
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Enzyme Catalysis and Immobilization
- Physical Sciences › Chemistry › Organic Chemistry › Carbohydrate Chemistry and Synthesis
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Plant biochemistry and biosynthesis
- Keywords
- UGT, soybean, enzyme specificity, substrate binding, reaction scope, biocatalysis
- MeSH terms
- Glycosides, Glycosylation, Methionine, Glycine max, Substrate Specificity, Glycosyltransferases, Racemethionine
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- CoChat. (2026). Citation check: Promiscuous Yet Specific: A Methionine–Aromatic Interaction Drives the Reaction Scope of the Family 1 Glycosyltransferase Gm UGT88E3 from Soybean. https://app.cochat.ai/papers/10.1021/acs.biochem.3c00494
- The paper
- de Boer, R. M., H. Hvid, D. E., Davail, E., Vaitkus, D., Duus, J. Ø., Welner, D. H., & Teze, D. (2023). Promiscuous Yet Specific: A Methionine–Aromatic Interaction Drives the Reaction Scope of the Family 1 Glycosyltransferase Gm UGT88E3 from Soybean. Biochemistry. https://doi.org/10.1021/acs.biochem.3c00494
