st 6

ST6Sialyltransferase6 (ST6GALNAC6) is a member of the sialyltransferase family, capable of modifying proteins and ceramides on the cell surface, thereby altering interactions between cells or between the cells and the extracellular matrix. ST6Sialyltransferase6 is useful in studies related to inflammatory bowel disease (IBD).

ST6Sialyltransferase5 (EC:2.4.3.3, ST6GALNAC5, SIAT7E, ST6 N-acetylgalactosaminide alpha-2,6-sialyltransferase 5) transfers sialic acid to N-acetylgalactosamine (GalNAc) residues. It may serve as a biomarker in cervical screening samples.

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.

ST8 alpha-2,8-Sialyltransferase 6 (ST8SIA6) is a type of sialyltransferase that produces α2,8-linked disialic acid which interacts with mouse Siglec-E and human Siglec-7 and -9, thereby promoting tumor growth by suppressing antitumor immune responses.

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.

Yeast 6-Phosphogluconic Dehydrogenase (EC 1.1.1.44) is a member of the oxidoreductase family, which acts on the CH-OH group of donor molecules using NAD+ or NADP+ as an acceptor. The two substrates for Yeast 6-Phosphogluconic Dehydrogenase are 6-phospho-D-gluconate and NADP+, and its three products are D-ribulose 5-phosphate, CO2, and NADPH.

Carbohydrate Sulfotransferase 6 (EC:2.8.2.21) catalyzes the transfer of sulfates to the 6-position of a non-reducing GlcNAc residue in keratan.