Beta-1,3-galactosyltransferase 6 (B3GALT6)

Beta-1,3-galactosyltransferase 6 (B3GALT6) is a Golgi-localized enzyme that catalyzes the transfer of galactose from UDP-galactose to the glycosaminoglycan linker region of proteoglycan core proteins, specifically at the third position of the tetrasaccharide linker initiating glycosaminoglycan chain synthesis. This reaction is essential for the biosynthesis of dermatan sulfate, chondroitin sulfate, and heparan sulfate glycosaminoglycans, all major components of the extracellular matrix critical for tissue structure and integrity. Pathogenic mutations in B3GALT6 disrupt proteoglycan assembly and collagen maturation, resulting in connective tissue disorders like spondyloepimetaphyseal dysplasia and subtypes of Ehlers-Danlos syndrome characterized by joint hypermobility, skin hyperextensibility, and skeletal abnormalities. Experimental evidence indicates B3GALT6 function is partially compensated by other enzymes in the GAG pathway, but deficiency leads to distinctive biochemical and structural tissue defects. No direct therapeutic agents currently target this enzyme; biomarker and safety profiles rely on clinical and molecular pathology assessments.

Other names

Beta-1,3-GalTase 6Beta3Gal-T6Beta3GalT6Galactosyltransferase IIGalactosylxylosylprotein 3-beta-galactosyltransferaseUDP-Gal:betaGal beta 1,3-galactosyltransferase polypeptide 6GAG GalTIIALGAZEDSP2EDSSPD2SEMDJL1galactosyltransferase IIUDP-Gal:betaGal beta 1,3-galactosyltransferase 6UDP-Gal:betaGlcNAc beta 1,3-galactosyltransferase, polypeptide 6

null (No specific drugs are known to directly modulate B3GALT6 in clinical or preclinical settings)