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Sialyltransferase enzymes are a family of glycosyltransferases (primarily in glycosyltransferase family 29, GT29) that catalyze the transfer of sialic acid from CMP-sialic acid (usually CMP-Neu5Ac) to terminal positions of oligosaccharide chains on glycoproteins and glycolipids. This process (sialylation) modifies the physicochemical and biological properties of glycoconjugates, influencing cell–cell recognition, adhesion, signal transduction, immune interactions, pathogen binding, and development. There are multiple sialyltransferase subfamilies, with specificity for particular linkages (e.g., α2,3-, α2,6-, or α2,8-), acceptor substrates (galactose, N-acetylgalactosamine, sialic acid), and tissue expression patterns. Alterations in sialyltransferase expression or activity are associated with cancer progression, immune regulation disorders, neurodevelopment, and pathogen–host interactions.
Inhibition of sialic acid transfer during glycosylation reduces cell surface sialylation, affecting cell-cell adhesion, immune evasion, and signal transduction
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