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ST6 N-acetylgalactosaminide alpha-2,6-sialyltransferase 6 (ST6GALNAC6)

Target
ST6GALNAC6
Molecular classification
Enzyme, glycosyltransferase, sialyltransferase
01

Overview

ST6 N-acetylgalactosaminide alpha-2,6-sialyltransferase 6 (ST6GALNAC6) is a sialyltransferase enzyme that catalyzes the transfer of sialic acid (N-acetylneuraminic acid, NeuAc) to glycolipids and glycoproteins, specifically forming alpha-2,6 linkages to N-acetylgalactosaminide (GalNAc) or N-acetylglucosaminide (GlcNAc) residues on cell surface molecules[3]. It is involved in the biosynthesis of branched disialyl structures and certain gangliosides, such as GD1alpha, from precursors like GM1b. ST6GALNAC6 preferentially acts on glycolipids, is implicated in the generation of antigens associated with cancer (such as disialyl Lewis a), and may regulate cell-cell and cell-matrix interactions by modifying surface sialylation patterns[3]. Potentially, changes in ST6GALNAC6 activity can affect the composition of gangliosides in cells, with functional consequences for tumor progression and metastasis[1][3].

Other names
Alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase 6SIAT7FUNQ708/PRO1359ST6GalNAcVIhST6GalNAc VISIAT7-FST6GALNACVIGalNAc alpha-2,6-sialyltransferase VISialyltransferase 7Falpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase 6ST6 (alpha-N-acetyl-neuraminyl-2,3-beta-galactosyl-1,3)-N-acetylgalactosaminide alpha-2,6-sialyltransferase 6ST6 GalNAc alpha-2,6-sialyltransferase 6epididymis secretory sperm binding proteingalNAc alpha-2,6-sialyltransferase VIsialyltransferase 7 ((alpha-N-acetylneuraminyl 2,3-betagalactosyl-1,3)-N-acetyl galactosaminide alpha-2,6-sialytransferase) F
02

Biological functions

Sialylation of glycoproteins and glycolipidsModification of cell-surface proteins and ceramidesRegulation of cell-cell and cell-matrix interactionsSphingolipid metabolismBiosynthesis of complex gangliosides, like GD1alpha and disialyl structures
03

Disease associations

Cancer (via synthesis of disialyl Lewis a, a cancer-associated antigen)Potential role in other diseases involving altered glycosylation

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