ArticleGlycobiology2021
A phylogenetic view and functional annotation of the animal β1,3-glycosyltransferases of the GT31 CAZy family.
Article in Glycobiology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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16 citing papers in PubMed, 21 citations in OpenAlex.
- Crystal structure of a β1,3-Glucosyltransferase reveals an unusual substrate recognition by a two-domain GT-A fold glycosyltransferase.The Journal of biological chemistry · 2026Article
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- Integrative analysis of the metabolome and transcriptome reveals the mechanism of flower color and antioxidant capacity in threeFrontiers in plant science · 2026Article
- Structural basis for human chondroitin sulfate chain polymerization.Nature communications · 2025Article
- Evolutionary analyses of the animal glycosyltransferase family 54 reveals two β1,4-N-acetylglucosaminyltransferase families.iScience · 2025Article
- Adhesion to aggression: unravelling sLeClinical & experimental metastasis · 2025Review
- Identification of a free-N-glycan with difucosylated type-1 lactosamine in cancerous tissue and its validation for cancer diagnosis by urinary testing.Scientific reports · 2025Article
- Structure-Based Mechanism and Specificity of Human Galactosyltransferase β3GalT5.Journal of the American Chemical Society · 2025Article
- Glycosyltransferases: glycoengineers in human milk oligosaccharide synthesis and manufacturing.Frontiers in molecular biosciences · 2025Review
- Substrate binding and catalytic mechanism of UDP-α-D-galactofuranose: β-galactofuranoside β-(1→5)-galactofuranosyltransferase GfsA.PNAS nexus · 2024Article
- Identification of glycogene-based prognostic signature and validation of B3GNT7 as a potential biomarker and therapeutic target in breast cancer.Journal of cancer research and clinical oncology · 2023Article
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- Role of Globotriaosylceramide in Physiology and Pathology.Frontiers in molecular biosciences · 2022Review
- Biochemical and Functional Characterization of GALT8, anFrontiers in plant science · 2021Article
- Lewis A Glycans Are Present on Proteins Involved in Cell Wall Biosynthesis and Appear Evolutionarily Conserved Among NaturalFrontiers in plant science · 2021Article
- How to extend your (polylactosamine) antennae.The Journal of biological chemistryArticle
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3 authors at 2 institutions in 1 country.
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Abstract
The formation of β1,3-linkages on animal glycoconjugates is catalyzed by a subset of β1,3-glycosyltransferases grouped in the Carbohydrate-Active enZYmes family glycosyltransferase-31 (GT31). This family represents an extremely diverse set of β1,3-N-acetylglucosaminyltransferases [B3GNTs and Fringe β1,3-N-acetylglucosaminyltransferases], β1,3-N-acetylgalactosaminyltransferases (B3GALNTs), β1,3-galactosyltransferases [B3GALTs and core 1 β1,3-galactosyltransferases (C1GALTs)], β1,3-glucosyltransferase (B3GLCT) and β1,3-glucuronyl acid transferases (B3GLCATs or CHs). The mammalian enzymes were particularly well studied and shown to use a large variety of sugar donors and acceptor substrates leading to the formation of β1,3-linkages in various glycosylation pathways. In contrast, there are only a few studies related to other metazoan and lower vertebrates GT31 enzymes and the evolutionary relationships of these divergent sequences remain obscure. In this study, we used bioinformatics approaches to identify more than 920 of putative GT31 sequences in Metazoa, Fungi and Choanoflagellata revealing their deep ancestry. Sequence-based analysis shed light on conserved motifs and structural features that are signatures of all the GT31. We leverage pieces of evidence from gene structure, phylogenetic and sequence-based analyses to identify two major subgroups of GT31 named Fringe-related and B3GALT-related and demonstrate the existence of 10 orthologue groups in the Urmetazoa, the hypothetical last common ancestor of all animals. Finally, synteny and paralogy analysis unveiled the existence of 30 subfamilies in vertebrates, among which 5 are new and were named C1GALT2, C1GALT3, B3GALT8, B3GNT10 and B3GNT11. Altogether, these various approaches enabled us to propose the first comprehensive analysis of the metazoan GT31 disentangling their evolutionary relationships.
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