Beta-1,4-N-acetylgalactosaminyltransferase 3 (B4GALNT3)

Beta-1,4-N-acetylgalactosaminyltransferase 3 (B4GALNT3) is an enzyme of the chondroitin N-acetylgalactosaminyltransferase family that catalyzes the transfer of N-acetylgalactosamine (GalNAc) from UDP-GalNAc to N-acetylglucosamine-containing glycans, forming LacdiNAc (GalNAcβ1-4GlcNAc) structures on N- and probably O-linked glycans[2][3][4][5]. B4GALNT3 contains a unique PA14 domain, critical for its glycan-recognition and catalytic activity[1][3]. Through its enzymatic activity, B4GALNT3 regulates the maturation and terminal modifications (e.g., sialylation, fucosylation) of glycoproteins, thereby affecting protein behavior such as clearance from the bloodstream and cell signaling. Disruption of B4GALNT3 activity alters glycoprotein stability and has been linked to bone loss (via sclerostin regulation) and may have broader implications in glycoprotein-related diseases[3]. The enzyme plays a key role in the biosynthesis of LacdiNAc, impacting various aspects of glycoprotein function and homeostasis.

Other names

Beta4GalNAc-T3Beta4GalNAcT3NGalNAc-T2FLJ16224FLJ40362Beta-1,4-N-acetylgalactosaminyltransferase IIIN-acetyl-beta-glucosaminyl-glycoprotein 4-beta-N-acetylgalactosaminyltransferase 2beta-1,4-N-acetyl-galactosaminyl transferase 3beta4GalNAcT3[2][3][5]