Alpha-1,6-mannosylglycoprotein 6-beta-N-acetylglucosaminyltransferase V (MGAT5)

Alpha-1,6-mannosylglycoprotein 6-beta-N-acetylglucosaminyltransferase V (MGAT5) is a type-II transmembrane glycosyltransferase enzyme located in the Golgi apparatus. It catalyzes the addition of N-acetylglucosamine in β1,6 linkage to α1,6-mannose of N-glycans, producing branched glycan structures crucial for cell surface protein regulation. MGAT5 activity enhances the formation of complex tri- and tetra-antennary N-glycans, which modulate cellular signaling, adhesion, migration, and immune responses. Overexpression is closely linked to increased cancer malignancy, poor prognosis, and is implicated in autoimmune and neurodevelopmental conditions. It is actively investigated as a therapeutic target but lacks clinical inhibitors as of 2024.

Other names

MGAT5N-acetylglucosaminyltransferase VGlcNAc transferase VGnT-VGGNT5GNT-VMGAT5AAlpha-mannoside beta-1,6-N-acetylglucosaminyltransferase VGlcNAc-T VMannoside acetylglucosaminyltransferase 5N-acetylglucosaminyl-transferase VSecreted beta-1,6-N-acetylglucosaminyltransferase VSecreted alpha-1,6-mannosylglycoprotein 6-beta-N-acetylglucosaminyltransferase AGNT-VA

For anticipated drugs: inhibition of MGAT5 N-glycosylation reduces pathogenic glycan branching, which may impact cell surface receptor stability, signaling, and immune evasion in cancer and inflammation