ReviewBiochemical Society transactions2020
Promiscuity and specificity of eukaryotic glycosyltransferases.
Review in Biochemical Society transactions, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 55 citations in OpenAlex.
- A chromosome level genome, as well as transcriptomes and metabolomes, insights into genome evolution and the biosynthesis of kaempferol and kaempferol derivatives inFrontiers in plant science · 2026Article
- Siamese Twins: The Multimodular Mechanisms of Golgi Maturation and Glycan Synthesis Are Coupled at Their Core.Sub-cellular biochemistry · 2026Review
- A structural basis for the strain-dependent UDP-sugar specificity of glycosyltransferase C from the Limosilactobacillus reuteri accessory secretion system.Acta crystallographica. Section D, Structural biology · 2025Article
- Limits on the computational expressivity of non-equilibrium biophysical processes.Nature communications · 2025Article
- Article
- Defined Glycan Ligands for Detecting Rare l-Sugar-Binding Proteins.Journal of the American Chemical Society · 2025Article
- Three-component systems represent a common pathway for extracytoplasmic addition of pentofuranose sugars into bacterial glycans.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- First Clarification of the Involvement of Glycosyltransferase MdUGT73CG22 in the Detoxification Metabolism of Nicosulfuron in Apple.Plants (Basel, Switzerland) · 2024Article
- The biosynthesis, degradation, and function of cell wall β-xylosylated xyloglucan mirrors that of arabinoxyloglucan.The New phytologist · 2023Article
- Recombinant mucin biotechnology and engineering.Advanced drug delivery reviews · 2023Review
- Potential Role of Quercetin Glycosides as Anti-Atherosclerotic Food-Derived Factors for Human Health.Antioxidants (Basel, Switzerland) · 2023Review
- Small molecule inhibitors of mammalian glycosylation.Matrix biology plus · 2022Article
- Review
- General Theory of Specific Binding: Insights from a Genetic-Mechano-Chemical Protein Model.Molecular biology and evolution · 2022Article
- In silico analysis of the human milk oligosaccharide glycome reveals key enzymes of their biosynthesis.Scientific reports · 2022Article
- Catalytic flexibility of rice glycosyltransferase OsUGT91C1 for the production of palatable steviol glycosides.Nature communications · 2021Article
- GRASP55 regulates intra-Golgi localization of glycosylation enzymes to control glycosphingolipid biosynthesis.The EMBO journal · 2021Article
- NleB/SseK-catalyzed arginine-glycosylation and enteropathogen virulence are finely tuned by a single variable position contiguous to the catalytic machinery.Chemical science · 2021Article
- Posttranslational modification of pyruvate kinase type M2 (PKM2): novel regulation of its biological roles to be further discovered.Journal of physiology and biochemistry · 2021Review
- Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Glycosyltransferases are a large family of enzymes responsible for covalently linking sugar monosaccharides to a variety of organic substrates. These enzymes drive the synthesis of complex oligosaccharides known as glycans, which play key roles in inter-cellular interactions across all the kingdoms of life; they also catalyze sugar attachment during the synthesis of small-molecule metabolites such as plant flavonoids. A given glycosyltransferase enzyme is typically responsible for attaching a specific donor monosaccharide, via a specific glycosidic linkage, to a specific moiety on the acceptor substrate. However these enzymes are often promiscuous, able catalyze linkages between a variety of donors and acceptors. In this review we discuss distinct classes of glycosyltransferase promiscuity, each illustrated by enzymatic examples from small-molecule or glycan synthesis. We highlight the physical causes of promiscuity, and its biochemical consequences. Structural studies of glycosyltransferases involved in glycan synthesis show that they make specific contacts with 'recognition motifs' that are much smaller than the full oligosaccharide substrate. There is a wide range in the sizes of glycosyltransferase recognition motifs: highly promiscuous enzymes recognize monosaccharide or disaccharide motifs across multiple oligosaccharides, while highly specific enzymes recognize large, complex motifs found on few oligosaccharides. In eukaryotes, the localization of glycosyltransferases within compartments of the Golgi apparatus may play a role in mitigating the glycan variability caused by enzyme promiscuity.
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