Alpha-1,3-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase (MGAT1)

Alpha-1,3-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase (MGAT1) is a type II transmembrane enzyme localized mainly in the medial Golgi. It plays an essential role in the biosynthesis of complex N-linked glycans by catalyzing the initial branching step, the transfer of N-acetylglucosamine (GlcNAc) from UDP-GlcNAc to the alpha-3 mannose of the trimannosyl core of N-linked oligosaccharides. This step is critical for generating hybrid and complex N-glycan structures that modulate cell surface protein behavior, including the residency of growth factor receptors and adhesion molecules. MGAT1 activity is indispensable for normal embryogenesis in mammals, and altered function or expression is implicated in the biology of cancers and potentially other disease states. While it is considered a potential therapeutic target, no drugs have reached clinical use specifically targeting MGAT1 to date[2][3][8].

Other names

GLCNAC-TIGLCT1GLYT1GNT-1GNT-IMGATGnTImannosyl (alpha-1,3-)-glycoprotein beta-1,2-N-acetylglucosaminyltransferase

Initiation of complex N-glycan formation by catalyzing transfer of N-acetylglucosamine (GlcNAc) to α-3-D-mannoside on glycoproteins within the medial Golgi; mechanisms for targeting involve inhibition or modulation of glycosylation