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Galactose-3-O-sulfotransferase 4 (GAL3ST4) is an enzyme encoded by the GAL3ST4 gene, which belongs to the sulfotransferase family[1][4][6]. It catalyzes the transfer of a sulfate group to the C-3' position of galactose residues within core 1 structures of O-linked glycoproteins, a process known as sulfonation[1][2][6][7]. This modification is crucial for the physiological function of glycoproteins, influencing the structure and function of cartilage and bone and potentially impacting the development of congenital skeletal deformities[3]. GAL3ST4 operates predominantly in the Golgi apparatus[3] and alteration of its activity through mutation or deficiency is linked to diseases such as Fanconi anemia, scoliosis, and pectus excavatum[1][3]. The enzyme exhibits high substrate specificity for asialofetuin, Gal-beta-1,3-GalNAc, and Gal-beta-1,3(GlcNAc-beta-1,6)GalNAc[1][6]. Currently, there are no known drugs that directly target GAL3ST4 or known clinical biomarkers; its principal relevance is as an enzyme involved in the biosynthesis of sulfated proteoglycans and diseases related to sulfate metabolism.
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