Sialyltransferase (ST (also commonly ST3Gal, ST6Gal, ST6GalNAc, ST8Sia for human isoforms))

Sialyltransferases are a family of glycosyltransferase enzymes that catalyze the transfer of sialic acid residues from the activated donor cytidine 5′-monophosphate-sialic acid (CMP-Sia) to the terminal positions of glycan chains on glycoproteins and glycolipids, forming sialylated glycoconjugates[1][2][4]. This enzymatic process predominantly occurs in the Golgi apparatus. Sialyltransferases are essential for generating the sialome, the collection of sialylated structures shaping cell–cell interactions, immune regulation, and pathogen recognition in vertebrates[1][2][4]. Humans possess about 20 sialyltransferase isoenzymes, classified by the type of glycosidic linkage they form (α2,3; α2,6; α2,8) and their substrate specificity[1]. Sialyltransferase activity is essential for normal development, nervous system function (modulating sodium channel function and neural excitability), and immune modulation; its dysregulation is implicated in cancer, inflammation, infection, and neural disorders[3][4][6]. Sialyltransferase inhibitors are emerging as experimental tools and potential therapeutics, but no specific inhibitors are yet clinically established[5].

Other names

SialyltransferaseSTSiaTSIATST3GalST6GalST8SiaDSiaT (in Drosophila)glycosyltransferase family 29

Inhibition: Prevents addition of sialic acid to glycans, potentially suppressing cancer cell evasion or invasiveness, or altering pathogen attachment[5]. Modulation of cell–cell interaction by altering surface glycosylation patterns.