sialyltransferase

α-2,3-sialyltransferase-IN-1 (Lith-O-Asp analog) is an α-2,3-sialyltransferase inhibitor with anticancer activity. Vapendavir diphosphate inhibits EV71 replication.

Alpha-2,8-Sialyltransferase (CstII) (ST8Sia VI), belonging to the alpha2,8-sialyltransferase (ST8Sia) family, primarily catalyzes the elongation of the α2,8-linked oligo polysialic acid chain on the sialic acid (Sia) residue. It is frequently utilized in biochemical research.

Alpha-2,3-Sialyltransferase (PmST3) is a beta-galactoside that catalyzes the transfer of sialic acid to carbohydrate groups of glycoproteins and glycolipids [1].

Alpha-2,6-Sialyltransferase (Pd26ST) efficiently catalyzes the sialylation of both terminal and internal galactose and N-acetylgalactosamine residues, resulting in the production of terminal α2,6-sialosides [1].

P-3FAX-Neu5Ac is a sialic acid analog and a sialyltransferase inhibitor.

ST3 beta-Gal alpha-2,3-Sialyltransferase 2 (EC:2.4.3.4, ST3GAL2) catalyzes the transfer of sialic acid from CMP-sialic acid to galactose-containing substrates.

ST3 beta-Gal alpha-2,3-Sialyltransferase 6 (EC:2.4.99., ST3GAL6; SIAT10, Type 2 lactosamine alpha-2,3-sialyltransferase) is responsible for transferring sialic acid from activated cytidine 5'-monophospho-N-acetylneuraminic acid to terminal positions on sialylated glycolipids (gangliosides) or to N- or O-linked glycans on glycoproteins. This enzyme plays a significant role in cancer.

ST6Sialyltransferase1 (EC:2.4.3.3, ST6GALNAC1, SIAT7A, Alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase 1) connects salivary acid, N-acetylneuraminic acid (NeuAc) ST6Sialyltransferase1 plays a key role in the pathogenesis of cancer by transferring sialic acid, N-acetylneuraminic acid (NeuAc), to O-linked GalNAc residues via an alpha-2,6 linkage.

ST6Sialyltransferase2 (EC:2.4.3.3, ST6GALNAC2) catalyzes the addition of sialic acid to the non-reducing end of complex carbohydrates.

ST6Sialyltransferase4 (EC:2.4.3.7; ST6GALNAC4; SIAT3-C; SIAT3C; SIAT7-D; SIAT7D) catalyzes the transfer of sialic acid from CMP-sialic acid to substrates containing galactose. By inducing abnormal glycosylation, ST6Sialyltransferase4 promotes hepatocarcinogenesis.

ST6 GalSialyltransferase1 (EC:2.4.3.1, ST6GAL1) catalyzes the transfer of sialic acid from CMP-sialic acid to substrates containing galactose.

ST6 GalSialyltransferase2 (EC:2.4.3.1, ST6GAL2) catalyzes the transfer of sialic acid from CMP to oligosaccharide substrates. It plays a significant role in schizophrenia research.

Alpha-2-3,6-sialidase (BiNanH2), a sialyltransferase commonly utilized in biochemical research, catalyzes the transfer of α-2,3 2,6-sialyl from CMP-Neu5Ac to galactoside acceptors [1].