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| glycosyltransferase | |
|---|---|
| Name | Glycosyltransferase |
| Ec number | EC 2.4.-.- |
glycosyltransferase
Glycosyltransferases are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor substrates, forming glycosidic bonds. They are central to processes in biosynthesis of glycoproteins, glycolipids, and glycan structures across organisms including Homo sapiens, Escherichia coli, and Saccharomyces cerevisiae. These enzymes are studied by laboratories at institutions such as the Max Planck Society, Howard Hughes Medical Institute, and Cold Spring Harbor Laboratory and are the focus of research published in journals like Nature, Science, and Cell.
Glycosyltransferases comprise a diverse group of proteins first characterized in work related to Ludwig Pasteur's studies on fermentation and later in biochemical research by groups at Massachusetts Institute of Technology and the University of Cambridge. They utilize activated donors such as nucleotide sugars (e.g., UDP-glucose) and lipid-linked oligosaccharides and act on acceptors ranging from proteins to lipids; key historical milestones include discoveries at the Rockefeller University and methods developed at the Sanger Institute. Modern techniques from laboratories at Stanford University, University of California, Berkeley, and University of Oxford have resolved many aspects of their function.
Glycosyltransferases are divided into families and clans cataloged in resources like the CAZy database and classified by sequence and fold into families such as GT-A, GT-B, and GT-C. Prominent families include those containing members like β-1,4-galactosyltransferase (family GT7) studied at Johns Hopkins University and N-acetylglucosaminyltransferases examined at Columbia University. Comparative genomics initiatives at institutions such as the National Institutes of Health and European Molecular Biology Laboratory have mapped glycosyltransferase repertoires across taxa including Arabidopsis thaliana, Drosophila melanogaster, and Mycobacterium tuberculosis.
Structural studies using X-ray crystallography at facilities like the European Synchrotron Radiation Facility and cryo-EM at the Institute of Cancer Research reveal conserved folds and active-site motifs. Mechanistic insights into inverting and retaining mechanisms derive from work by researchers at Princeton University and Yale University, showing roles for divalent cations and catalytic residues. Structural models integrate data from collaborations with groups at the Max Planck Institute for Biochemistry, Weizmann Institute of Science, and Riken and inform computational efforts at Flatiron Institute and Lawrence Berkeley National Laboratory.
Glycosyltransferases function in pathways including N-linked glycosylation in the endoplasmic reticulum, O-linked glycosylation in the Golgi apparatus, and biosynthesis of proteoglycans and glycolipids implicated in signaling pathways studied at MIT, Imperial College London, and The Scripps Research Institute. They modulate cell–cell recognition in systems researched at Harvard University Medical School and control developmental processes in organisms like Caenorhabditis elegans and Zea mays. Networks involving glycosyltransferases intersect with pathways analyzed by consortia such as the Human Genome Project and initiatives at the Broad Institute.
Mutations in glycosyltransferase genes cause congenital disorders of glycosylation identified by clinical groups at Mayo Clinic, Great Ormond Street Hospital, and Johns Hopkins Hospital. Altered glycosyltransferase activity is implicated in cancer metastasis investigated by teams at Dana-Farber Cancer Institute and MD Anderson Cancer Center, and in infectious disease host–pathogen interactions studied at Centers for Disease Control and Prevention and Institut Pasteur. Therapeutic targeting efforts occur in pharmaceutical programs at companies such as GlaxoSmithKline, Pfizer, and Roche.
Engineered glycosyltransferases are used in glycoengineering of therapeutic antibodies produced at facilities like Genentech and Amgen and in vaccine design pursued at GSK Vaccines and Moderna. Industrial applications include synthesis of oligosaccharides in collaborations with Novozymes and DuPont and enzymatic glycosylation platforms developed at Biogen. Structure-guided inhibitor design leverages computational chemistry from groups at Merck Research Laboratories and academic partnerships with University of Toronto and University of Melbourne.
Category:Enzymes