MGAT2 Human

MGAT2 is a Golgi enzyme characterized by several distinct domains:

• N-terminal cytoplasmic domain: A short segment located at the beginning of the protein.
• Hydrophobic non-cleavable signal-anchor domain: This domain helps anchor the enzyme to the Golgi membrane.
• C-terminal catalytic domain: The active site of the enzyme responsible for its catalytic activity .

The primary function of MGAT2 is to catalyze the transfer of N-acetylglucosamine (GlcNAc) from UDP-GlcNAc to the α1-6 linked mannose of Asn-linked oligosaccharides of glycoproteins. This reaction is a critical step in the formation of complex N-glycans, which are important for various cellular processes, including cell-cell communication, protein stability, and immune response .

Mutations in the MGAT2 gene can lead to carbohydrate-deficient glycoprotein syndrome, type II (CDG-II), a rare genetic disorder characterized by defects in glycoprotein biosynthesis. This condition can result in a wide range of symptoms, including developmental delays, neurological issues, and immune system deficiencies .

Recombinant MGAT2 is produced using various expression systems, such as Escherichia coli (E. coli). The recombinant protein is often tagged with a His-tag for easy purification and is used in research to study the enzyme’s function, structure, and potential therapeutic applications .

Recombinant MGAT2 is widely used in biochemical and structural studies to understand its role in glycosylation. It is also employed in high-throughput screening assays to identify potential inhibitors or modulators of the enzyme, which could have therapeutic implications for diseases related to glycosylation defects .